Molecular characterization of a novel soybean gene encoding a neutral PR-5 protein induced by high-salt stress.
Tachi H; Fukuda-Yamada K; Kojima T; Shiraiwa M; Takahara H., In this study, we characterized a novel soybean gene encoding a neutral PR-5 protein and compared it to two acidic isoforms of soybean PR-5 protein. This gene, designated as Glycine max osmotin-like protein, b isoform (GmOLPb, accession no. AB370233), encoded a putative protein having the greatest similarity to chickpea PR-5b (89% identity). Unlike the two acidic PR-5, GmOLPa and P21, the protein had a C-terminal elongation responsible for possible vacuolar targeting and after maturation showed a calculated molecular mass of 21.9 kDa with pl 6.0. The 3D models, predicted by the homology modeling, contained four alpha-helixes and 16 beta-strands and formed three characteristic domains. The two acidic PR-5 proteins also showed a 3D structure very similar to GmOLPb, although the electrostatic potential on molecular surface of each PR-5 was significantly different. In the study of the gene expression under conditions of high-salt stress, GmOLPb was highly induced in the leaves of the soybean, particularly in the lower part of a leaf The expression started at 2 h after initiation of the stress and was highly induced between 18-72 h. Gene expression of P21e (protein homologous to P21) was transiently induced by high-salt stress, but took place earlier than the gene expressions of GmOLPa and GmOLPb. Such differential expression was observed also under investigation with methyl jasmonate and salicylic acid. These results suggested that each soybean PR-5 might play a distinctive role in the defensive system protecting the soybean plant against high-salt stress, particularly in the leaves of the soybean. (C) 2008 Elsevier Masson SAS. All rights reserved., ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Plant Physiol Biochem., Jan. 2009, [Reviewed]

Crucial Role of MZF1 and Sp1 for the Transcriptional Regulation of the Peptidylarginine Deiminase Type I Gene (PADI1) in Human Keratinocytes
S.Dong; S.Ying; T.Kojima; M.Shiraiwa; A.Kawada; M.C.Méchin; V.Adoue; S.Chavanas; G.Serre; M.Simon; H.Takahara, Pepticlylarginine deiminases (PADs) catalyze the conversion of protein-bound arginine residues into citrulline residues in a calcium-dependent manner. The PAD1 gene (PADI1) is expressed in a few tissues, including the epidermis, where the protein is detected with a higher level in the more differentiated keratinocytes. Using quantitative reverse transcription-PCR experiments, we show that PADI1 mRNAs are more abundant in keratinocytes cultured with 1.2 than 0.15 mm calcium. We cloned and characterized the promoter region using human keratinocytes transfected with variously deleted fragments of the 5'-upstream region of PADI1 coupled to the luciferase gene. We found that as few as 195bp upstream from the transcription initiation site were sufficient to direct transcription of the reporter gene. Mutations of MZF1- or Sp1-binding sites markedly reduced PADI1 promoter activity. Chromatin immunoprecipitation assays revealed that MZF1 and Sp1/Sp3 bind to this region in vivo. Furthermore, MZF1 or Sp1 small interfering RNAs (siRNAs) effectively diminished PADI1 expression in keratinocytes cultured in both low- and high-calcium-containing medium. In addition, the expression of MZF1 and PAD1 increased in parallel when normal human epidermal keratinocytes underwent differentiation. These data indicate that MZF1 and Sp1/Sp3 binding to the promoter region drive the PADI1 expression., NATURE PUBLISHING GROUP
J. Invest. Dermatol., Mar. 2008, [Reviewed]

Molecular characterization of a novel salt-induible gene for an OSBP (oxysterol-binding protein)-homologue from soybean
D.Y.Li; H.Inoue; M.Takahashi; T.Kojima; M.Shiraiwa; H.Takahara, Oxysterol-binding protein (OSBP) and its homologues constitute a protein family in many eukaryotes from yeast to humans, which are involved in cellular lipid metabolism, vesicle transport and signal transduction. In this study, we characterized a novel salt-inducible gene for an OSBP-homologue from soybean (Glycine max [L.] Merr.). The soybean OSBP-homologous gene, denoted as G. max OSBP (GmOSBP), encoded a 789 aa putative protein with two characteristic domains; the pleckstrin homology (PH) domain and the ligand-binding (LB) domain, in the Nand C-terminus, respectively. The GmOSBP-PH domain showed localization into/around the nucleus in a transient subcellular localization assay. The phylogenetic relationship of the GmOSBP-LB domain to those in other OSBP-homologues suggested that GmOSBP might bind a lipid molecule(s) different from the ligand-candidates found for the human/yeast OSBP-homologues. The GmOSBP gene was constitutively transcribed in all of the soybean organs examined - root, stem and trifoliate leaf - at low levels and was highly induced in all these organs by high-salt stress (300 mM NaCl). Interestingly, gene expression of GmOSBP was also markedly induced in the senesced soybean cotyledon, which contains high levels of a variety of cellular lipids utilized for energy for germination and as membrane components. Therefore, we suggest that GmOSBP may be involved in some physiological reactions for stress-response and cotyledon senescence in the soybean. (c) 2007 Elsevier B.V All rights reserved., ELSEVIER SCIENCE BV
GENE, Jan. 2008, [Reviewed]

Purification and characterization of three neutral extracellular peroxidase isoenzymes from rye leaves
Satoshi Murakami; Hidenari Takahara; Masakazu Shiraiwa, Rye (Secale cereale L.) seedlings; contain two major flavone glucuronides, luteolin 7-O-diglucuronyl-4'-O-glucuronide (L3GlcUA) (1) and luteolin 7-O-diglucuronide (L2GlcUA) (2) in abundance in the apoplast of primary leaves; express a large number of peroxidase isoenzymes: and release H2O2 into the apoplast during primary leaf development. We purified and characterized three neutral extracellular peroxidase isoenzymes (rPOXs N1, N2, and N3) that can oxidize L2GlcUA as a natural substrate. The isoclectric points and molecular weights of rPOXs N1, N2, and N3 were 6.1, 7.2, and 6.3, and 42, 37, and 51 kDa, respectively. The optimum pH of the rPOXs N1, N2, and N3 were 5.5, 5.5, and 8.5, respectively, and their optimum temperatures ranged from 45 to 50 degrees C for all isoenzymes. rPOXs N1, N2, and N3 recognized flavonoids with 3', 4'-OH groups as potential substrates, but not flavonoids with a glycosylated 4'-OH group or those without a 3'-OH group. The activities on phenol-type substrates were high in the order of guaiacol > catechol > o-cresol for all isoenzymes. rPOXs N1, N2, and N3 exhibited broad reactivity with endogenous hydrogen donors including luteolin glucuronides derived from the apoplast of rye primary leaves. (c) 2006 Elsevier Ltd. All rights reserved., PERGAMON-ELSEVIER SCIENCE LTD
Phytochemistry, Mar. 2007, [Reviewed]

Molecular cloning and characterization of a salt-inducible gene encoding an acidic isoform of PR-5 protein in soybean (Glycine max [L.]Merr.)
Mari Onishi; Hiroyuki Tachi; Toshio Kojima; Masakazu Shiraiwa; Hidenari Takahara, We identified a novel salt-inducible soybean gene encoding an acidic-isoform of pathogenesis-related protein group 5 (PR-5 protein). The soybean PR-5-homologous gene, designated as Glycine max osmotin-like protein, acidic isoform (GmOLPa); accession no, AB116251), encodes a putative polypeptide having an N-terminal signal peptide. The mature GmOLPa protein without the signal peptide has a calculated molecular mass of 21.5 kDa and a pI value of 4.4, and was distinguishable from a known PR-5-homologous gene of soybean (namely P21 protein) through examination of the structural features. A comparison with two intracellular salt-inducible PR-5 proteins, tobacco osmotin and tomato NP24, revealed that GmOLPa did not have a C-terminal extension sequence functioning as a vacuole-targeting motif The GmOLPa gene was transcribed constitutively in the soybean root and was induced almost exclusively in the root during 24 It of high-salt stress (300 mM NaCl). Interestingly, GmOLPa gene expression in the stein and leaf, not observed until 24 h, was markedly induced at 48 and 72 h after commencement of the high-salt stress. Abscisic acid (ABA) and dehydration also induced expression of the GmOLPa gene in the root; additionally, dehydration slightly induced expression in the stem and leaf. In fact, the 5'-upstream sequence of the GmOLPa gene contained several putative cis-elements known to be involved in responsiveness to ABA and dehydration, e.g. ABA-responsive element (ABRE), MYB/MYC, and low temperature-responsive element (LTRE). These results suggested that GmOLPa may function as a protective PR-5 protein in the extracellular space of the soybean root in response to high-salt stress and dehydration. (c) 2006 Elsevier Masson SAS. All rights reserved., ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Plant Physiol. Biochem, Oct. 2006, [Reviewed]

NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes.
Sijun Dong; Takuya Kanno; Ayako Yamaki; Toshio Kojima; Masakazu Shiraiwa; Akira Kawada; Marie-Claire Mechin; Stephane Chavanas; Guy Serre; Michel Simon; Hidenari Takahara, Human peptidylarginine deiminase type III gene (PADI3) encodes a crucial post-translational modification enzyme that converts protein-bound arginine residues into citrulline residues. Its expression is restricted to a few cell types, including keratinocytes in the granular layer of the epidermis and in the inner root sheath of hair follicles. In these cells, the enzyme is involved in terminal processing of intermediate filament-binding proteins such as filaggrin and trichohyalin. To study the molecular mechanisms that control the expression of PADI3 in human keratinocytes at the transcriptional level, we characterized its promoter region using human keratinocytes transfected with variously deleted fragments of the 5'-upstream region of PADI3 coupled to the luciferase gene. We found that as few as 129 bp upstream from the transcription initiation site were sufficient to direct transcription of the reporter gene. Electrophoretic mobility-shift and chromatin immunoprecipitation assays revealed that NF-Y (nuclear factor Y) and Sp1/Sp3 (specificity protein 1/3) bind to this region in vitro and in vivo. Moreover, mutation of the Sp1- or NF-Y-binding motif markedly reduced PADI3 promoter activity. Furthermore, Sp1 or NF-YA (NF-Y subunit) small interfering RNAs effectively diminished PADI3 expression in keratinocytes cultured in both low- and high-calcium medium. These data indicate that PADI3 expression is driven by Sp1/Sp3 and NF-Y binding to the promoter region., PORTLAND PRESS LTD
Biochem J., Aug. 2006, [Reviewed]

Molecular cloning and characterization of a novel soybean gene encoding a leucine-protein induced to salt stress zipper-like protein induced to salt stress
Ayako Aoki; Akemi Kanegami; Michiko Mihara; Toshio Kojima; Masakazu Shiraiwa; Hidenari Takahara, To understand molecular responses to salt stress in soybean (Glycine max [L.] Merr.), we identified 106 salt-inducible soybean genes that expressed differentially at 72 h after 100 mM NaCl treatment using the cDNA-amplified fragment length polymorphism (AFLP) method. The genes were designated as G. max Transcript-Derived Fragments (GmTDFs). Among these genes, we characterized a soybean gene GmTDF-5 that encoded an unknown protein of 367 amino acids. The GmTDF-5 protein was a putative cytosolic protein with two leucine-zipper motifs at the N-terminal and was calculated as 40.7 kDa. Southern blot analysis indicated that GmTDF-5 presents as an intron-less single gene on soybean genome and possibly distributes narrowly throughout the higher plants. By 100 mM NaCl treatment, the gene expression of Gm TDF-5 was induced in the stem and lower-expanded leaf, and the amount of mRNA increased 5.1- and 2.0-fold up to 72 h, respectively. Interestingly, GmTDF-5 expression in the upper-leaf appeared dramatically with 10.0-fold increase at 72 h after the salt stress, but not until 48 h. Hyperosmotic pressure (mannitol treatment) and dehydration also caused the increases similar to NaCl treatment in the levels of GmTDF-5 expression. These results suggest that GmTDF-5 might be a novel cytosolic leucine-zipper-like protein functioning in mature organs of soybean shoot against water-potential changes. (c) 2005 Elsevier B.V. All rights reserved., ELSEVIER SCIENCE BV
gene, Aug. 2005, [Reviewed]

Regulation of the Expression of Peptidylarginine Deiminase Type II Gene (PADI2) in Human Keratinocytes Involves Sp1 and Sp3 Transcription Factors
SJ Dong; T Kojima; M Shiraiwa; MC Mechin; S Chavanas; G Serre; M Simon; A Kawada; H Takahara, Peptidylarginine deiminases (PAD) convert protein-bound arginine residues into citrulline residues in a Ca2+ ion-dependent manner. Among the five isoforms (PAD1, 2, 3, 4, and 6) existing in rodents and humans, PAD2 is the most widely expressed in both species, tissues, and organs. In order to study the mechanisms regulating the expression of the human PAD2 gene, PADI2, we characterized its promoter region using transfected human keratinocytes. A series of reporter gene constructions derived from the 2 kb region upstream of the transcription initiation site defined a minimal promoter sequence from nucleotides -132 to -41. This PADI2 region is GC-rich and lacks canonical TATA and CAAT boxes. Investigation of cis-acting elements in the region, further deletion analyses and electrophoretic mobility shift assays using specific antibodies revealed four Sp1-binding sites and identified Sp1 and Sp3 as binding factors important for the promoter activity. These results suggest that Sp1/Sp3 cooperation may provide a mechanism to control the transcription of PADI2., BLACKWELL PUBLISHING INC
J Invest Dermatol, May 2005, [Reviewed]

Cloning of two cysteine proteinase genes, CysP1 and CysP2, from soybean cotyledons by cDNA representational difference analysis
Jian-Qun Ling; Toshio Kojima; Masakazu Shiraiwa; Hidenari Takahara
Biochim.Biophys.Acta, Jun. 2003, [Reviewed]

UDP-glucuronic acid:soyasapogenol glucuronosyltransferase involved in saponin biosynthesis in germinating soybean seed
Yasunori Kurosawa; Hidenari Takahara; Masakazu Shiraiwa, We detected UDP-glucuronic acid:soyasapogenol glucuronosyltransferase (UGASGT) activity in the microsomal fraction from germinating soybean (Glycine max [L.] Merr.) seed. A microsomal fraction was isolated from germinating soybean seed and treated with various detergents to solubilize the enzyme. UGASGT activity was monitored throughout purification using UDP-[U-C-14]glucuronic acid and soyasapogenol B as substrates. Purification of UGASGT was achieved by HiTrap Q, Superdex 200, and HiTrap Blue chromatography procedures. This resulted in >205-fold enrichment relative to the starting homogenate. UGASGT was found to require divalent cations for activity. Studies on the substrate specificity of UGASGT demonstrated that the specificity for the sugar residue transferred was very high, as activity was scarcely found when UDP-glucuronic acid was replaced by other UDP sugars: UDP-glucose and UDP-galactose. Soyasapogenols, which are the aglycons of soybean saponin, are usable acceptors, but glycyrrhetinic acid, sophoradiol, beta-amyrin, and flavonoids are not. These findings suggest that this UGASGT was a specific enzyme for UDPglucuronic acid as a donor and soyasapogenols as acceptors, and that it was related to the biosynthesis of the sugar chain in soybean saponin. This study provides a basis for the molecular characterization of a key enzyme in saponin biosynthesis in soybean. The isolation of the gene may enable its use in the elucidation of the biosynthesis and physiological role of saponins in soybean., SPRINGER-VERLAG
Planta, Aug. 2002, [Reviewed]

Human peptidylarginine deiminase type III : molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin
Takuya Kanno; Akira Kawada; Jun Yamanouchi; Chikako Yoshida-Noro; Atsushi Yoshiki; Masakazu Shiraiwa; Moriaki Kusakabe; Motomu Manabe; Tadashi Tezuka; Hidenari Takahara, Peptidylarginine deiminase catalyzes the post-translational modification of proteins through the conversion of arginine to citrulline in the presence of calcium ions. In rodents, peptidylarginine deiminase has been classified into four isoforms, types I, II, III, and IV, which are distinct in their molecular weights, substrate specificities, and tissue localization. Of these isoforms, only type III was detected in epidermis and hair follicles. Although the role of this enzyme in these tissues is not yet clear, indirect data have shown that several structural proteins such as filaggrin, trichohyalin, and keratin are substrates for peptidylarginine deiminase. In this study, we cloned the full-length cDNA of human peptidylarginine deiminase type III (3142 bp) from cultured human keratinocytes by reverse transcription-polymerase chain reaction and by rapid amplification of cDNA ends methods. This cDNA contained a 1995 bp open reading frame encoding 664 amino acids (Mr = 74 770). To explore the physicochemical and enzymatic properties of human peptidylarginine deiminase type III, we constructed a plasmid for producing a recombinant human peptidylarginine deiminase type III in bacteria. The enzymatic characteristics of the recombinant enzyme were very similar to those of the rodent peptidylarginine deiminase type III. The recombinant enzyme showed the catalytic activities toward structural proteins of epidermis and hair follicle, filaggrin and trichohyalin, in which the deiminations maxima of about 60% and 13% arginine residues were observed in filaggrin and trichohyalin, respectively. An immunohistochemical study of human scalp skin with a monospecific anti-peptidyl-arginine deiminase type III antibody revealed that the type III enzyme was localized to the inner root sheath and outer root sheath of hair follicles. Peptidylarginine deiminase type III in the inner root sheath was notable between supramatrix and keratogenous zone and was scarcely detected in cornified hair zone. The enzyme was also expressed in the cuticle layer of hair. On the other hand, expression of the enzyme in the epidermis was very low. These data imply that human peptidylarginine deiminase type III is the predominant isoform in hair follicles and may function as a modulator of hair structural proteins, including trichohyalin during hair and hair follicle formation., BLACKWELL SCIENCE INC
J Invest Dermatol, Nov. 2000, [Reviewed]

Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and typeIV, and the expression pattern of type I in mouse
Ahmed Abu Rus'd; Yasuko Ikejiri; Hiroyuki Ono; Toshihiro Yonekawa; Masakazu Shiraiwa; Akira Kawada; Hidenari Takahara, Peptidylarginine deiminases (PADs), a group of post-translational enzymes, catalyze the conversion of protein-bound arginine residues to citrulline residues in a calcium ion-dependent manner and are widely distributed in various organs of vertebrates. Although the existence of four isoforms of PAD (types I, II, III, and IV) is reported in rodents, the relative functions of the isoforms with respect to their colocation in the tissues have yet to be explored. In this study, we cloned the full-length cDNA encoding mouse PAD type I by screening a uterine cDNA library and using the RACE method. This cDNA consists of an open reading frame of 1989 bases encoding 662 amino acids (73 823 Da), a 5'-untranslated region of 127 bases and a 3'-untranslated region of 1639 bases. Comparative reverse transcription-PCR and Northern-blot analyses detected PAD type I mRNA only in the epidermis and uterus. Administration of estrogen to adult ovariectomized mice increased the content of PAD type I mRNA in the uterus, providing evidence that its expression is under the control of the sex steroid hormone. We also cloned the full-length cDNAs of mouse PAD type III and type IV by the reverse transcription-PCR and RACE methods. The primary structure of PAD type III contains 664 amino acids (75 098 Da) deduced from the coding region of 1995 bases, and the primary structure of PAD type TV consists of 666 amino acids (74 475 Da) deduced from the coding region of 2001 bases. Comparison of the deduced amino acid sequences of all four isoforms of PAD showed about 50% identity with each other, the 3' regions being highly homologous compared with the 5' regions., BLACKWELL SCIENCE LTD
Eur. J. Biochem, Feb. 1999, [Reviewed]

Cloning of cDNA encoding a novel isoform (type IV) of peptidylarginine deiminase from rat epidermis
Atushi Yamakoshi; Hiroyuki Ono; Takayuki NIshijyo; Masakazu Shiraiwa; Hidenari Takahara, We isolated a new clone that showed structural similarities with the rat peptidylarginine deiminase (PAD) types II and III. The full-length cDNA sequence of this novel PAD comprised 1998 bp encoding a sequence for 666 amino acid residues (M-r 74 467), a 3'-non-coding region of 115 bp and a 5'-non-coding region of 16 bp. The derived amino acid sequence of the PAD showed 51.1 and 54.0% identities with the sequences of types II and III, respectively. Semi-quantitative reverse transcription-polymerase chain reaction (RT-PCR) assays of mRNAs from several tissues of rat indicated that the PAD message is highly expressed in the pancreas, spleen, and ovary and, less strongly expressed in the liver, lung, stomach, kidney, uterus, and dermis, and weakly expressed in the brain, heart and epidermis. Since this expression pattern was quite different from those of the previously reported PAD types I, II, and III, we designated this novel PAD as type IV. (C) 1998 Elsevier Science B.V. All rights reserved., ELSEVIER SCIENCE BV
Biochim. Biophys. Acta, Jul. 1998, [Reviewed]

Isolation and molecular cloning of epidermal-and hair follicle-specific peptidylarginine deiminase (TypeIII) from rat
Takayuki Nishijyo; Akira Kawada; Takuya Kanno; Masakazu Shiraiwa; Kiyoshi Sugawara; Hidenari Takahara, Peptidylarginine deiminase (PAD) is a post-translational modification enzyme that catalyzes deimination of arginine residues of proteins in the presence of calcium ions, There are three types of PAD in rodent tissues: PAD types I, II, and III [Terakawa et al, (1991) J, Biochem, 110, 661-666], Type III enzyme was detected only in the epidermis and in hair follicles, In this study, we have purified PAD type III from 2-day-old rat epidermis by a four-step procedure that included soybean trypsin inhibitor-affinity chromatography. The enzyme was purified about 600-fold from the crude extract and the recovery was 23%, The final preparation of the enzyme gave only a single protein band on SDS-PAGE and showed an apparent molecular weight of 76,000, Subsequently, we cloned and sequenced the full-length cDNA encoding rat PAD type III by reverse transcription-polymerase chain reaction (RT-PCR) using degenerate oligonucleotide primers designed from the internal amino acid sequences and by the rapid amplification of the cDNA ends method, The composite cDNA sequence contained a 5' untranslated region of 42 bp, an open reading frame of 1,995 bases that encoded 664 amino acids (M-r=75,036), a 3' untranslated region of 1,063 bp, and part of a poly(A)(+) tail, The entire reading frame sequence of rat PAD type III showed 51% homology with that of rat PAD type II, and the C-terminal region is highly conserved between the two types, The cloned gene was expressed in Escherichia coli cells to produce PAD type III, which had not only enzymatic activity, but also immunoreactivity against specific antibodies toward PAD type II, Furthermore, the specific expression of the enzyme in the epidermis and hair follicles was confirmed by RT-PCR assays of mRNAs from several tissues., JAPANESE BIOCHEMICAL SOC
J. Biochem., May 1997, [Reviewed]

Stimulation of human Keratinocyte growth by alginate oligosaccharides, a possible co-factor for epidermal growth factor in cell culture
Akira Kawada; Nozomi Hiura; Masakazu Shiraiwa; Shingo Tajima; Masataro Hiruma; Kenji Hara; Akira Ishibashi; Hidenari Takahara, Oligosaccharides, involved in regulation of plant developmental and defensive processes, were tested to determine their ability to enhance proliferation of human keratinocytes. A mixture of alginate oligosaccharides remarkably stimulated keratinocyte growth and [H-3]thymidine uptake in the presence of epidermal growth factor (EGP). The activity was comparable to bovine pituitary extract, a common complement in keratinocyte culture, and additive on BPE-induced stimulation. The most effective oligosaccharide in the mixture was identified and its chemical structure was determined. These findings demonstrate a novel activity of alginate oligosaccharide(s) in keratinocyte growth and suggest a possible co-factor for EGF-dependent stimulation in medium for keratinocytes. (C) 1997 Federation of European Biochemical Societies., ELSEVIER SCIENCE BV
FEBS Lett., May 1997, [Reviewed]

Mouse uterus peptidylarginine deiminase in expredded in the decidualized cells guring pregnancy
Tomoji Arai; Masashi Kusubata; Tetsuya Kohsaka; Masakazu Shiraiwa Kiyoshi Sugawara; Hidenari Takahara, Peptidylarginine deiminase is localized in the cytosol of the luminal and glandular epithelia of the nonpregnant murine uterus and its expression is regulated by sex hormones [Takahara et al., [1989]: J Biol Chem 264, 13361-13368; Takahara et al. [1992]: J Biol Chem 267,520-525]. Here, we demonstrate that changes occur in the enzyme level in the mouse uterus during pregnancy and parturition. After a rapid decrease in enzymatic activity from day 1 to day 5 of pregnancy, the activity sharply increased during the middle stage of pregnancy (day 8 to day 10) and then gradually decreased during late pregnancy. Expression of the enzyme occurred only in the decidual cells that had differentiated from endometrial stroma cells surrounding the implantation site. The immunochemical properties of the enzyme expressed in the decidualized cells was indistinguishable from those in the uterine epithelia. These results suggest that peptidylarginine deiminase has important roles in decidual cells and not just in the epithelia of the nonpregnant uterus. Moreover, the level of enzyme activity increased slightly just before parturition (day 17), and then decreased during the 12 h period after parturition. The tissue localization of the enzyme expressed around the time of parturition changed from decidua to the luminal and glandular epithelia. Semiquantitative analyses of the enzyme mRNA content in the pregnant uteri showed a remarkable increase from day 7 leading to the onset of the enzyme synthesis in the decidual cells. After reaching the maximal level at day 12, small peaks in the mRNA level were observed at two times during late pregnancy. Since these serial changes in the mRNA level did not correlate with changes in sex hormones, the expression of decidual peptidylarginine deiminase seemed to be controlled by factors other than sex hormones. (C) 1995 Wiley-Liss, Inc., WILEY-LISS
J. Cell. Biochem., Jul. 1995, [Reviewed]

Agregated form of dextransucrases from Leuconostoc mesenteroides NRRLB-512F and its constitutive mutant
Kazumi Funane; Masahiko Yamada; Masakazu Shiraiwa; Hidenari Takahara; Nobuhisa Yamamoto; Eiji Ichishima; Mikihiko Kobayashi, Purified dextransucrases [EC 2.4.1.5], DSW-D and DSW-G, from Leuconostoc mesenteroides B-512F were obtained from affinity chromatography with DEAE-Sephadex A-50 by elution with clinical dextran and guanidine-HCl, respectively, DSM-G was purified from the B-512F mutant strain SH 3002, which produces dextransucrase constitutively, Although the sugar contents of the purified enzymes were different, their molecular masses by SDS-PAGE were all 170kDa, DSW-D and DSW-G were highly aggregated and the all the activities were eluted at the void volume (V-o) on Sepharose 6B, while the DSM-G was eluted at 1.2 x V-o volume, On rechromatography, DSM-G was separated into three peaks corresponding to the aggregated form, monomeric form, and partially digested form, respectively, The aggregation of Leuconostoc dextransucrase was looser than that of streptococcal glucosyltransferases, but the structures of these enzymes had high homology with each other., TAYLOR & FRANCIS LTD
Biosci. Biotech. Biochem., May 1995, [Reviewed]

Existence and differential changes of peptidylarginine deiminase type II in mouse yolk-sac erythroid cells
Hiroko Koike; Masakazu Shiraiwa; Kiyoshi Sugawara; Tetsuya Kohsaka; Hidenari Takahara, Peptidylarginine deiminase (PAD) catalyzes the conversion of arginyl residues in proteins to citrullyl residues in the presence of Ca2+. Recently, we obtained a monoclonal antibody, EH7, which reacted only with mouse PAD type II. Here, we describe immunohistochemical findings on the cellular localization of PAD type II in mouse fetus by using the monoclonal antibody. PAD type II is expressed in yolk-sac erythroid cells and the level of the enzyme in these cells decreases as the cells differentiate., TAYLOR & FRANCIS LTD
Biosci. Biotech. Biochem., Mar. 1995, [Reviewed]

Expression of mouse uterine peptidylarginine deiminase in scherichia coli : construction of expression plasmid and properties of the recombinant enzyme
Itaru Ohsugi; Hidenari Takahara; Masakazu Shiraiwa; Kiyoshi Sugawara, To study the structure/function relationships of peptidylarginine deiminase (PAD), we constructed an Escherichia coli expression plasmid for mouse uterine PAD. First, segments of a cDNA encoding murine PAD were subcloned into a single plasmid, and the resulting plasmid, pKSPAD1, was inserted into an expression vector, pKK223-3, at the EcoRI and HindIII restriction sites. Since no detectable amount or activity of the PAD was produced by E. coli carrying that plasmid, the 5'-untranslated sequence of the cDNA was replaced with several synthetic DNAs. One of the constructed plasmids, pKKPAD4, which had a unique DNA linker containing a pair of Shine-Dalgarno sequences and a short preceding cistron inserted into the adjacent 5'-region of the coding region, produced a large quantity of mouse PAD as an unfused protein in E. coli. The purified recombinant PAD was indistinguishable from the native enzyme with respect to some structural properties, such as molecular mass, amino- and carboxyl-terminal sequences, and circular dichroism spectra. However, the Lu-amino group of the amino-terminal methionine residue of the recombinant PAD was not acetylated as was that of the native enzyme. Comparison of the recombinant PAD with the natural enzyme did not indicate significant differences in their sensitivity to activation by Ca2+ and in their substrate specificity toward arginine derivatives. The rates of modification of soybean trypsin inhibitor (Kunitz) were also similar for the recombinant and native PADs. These results indicate that the recombinant PAD has biological activities identical to those of the native enzyme and that the N-Alpha-acetyl group in the native PAD does not appear to have any particular role in the enzyme's catalytic function. (C) 1995 Academic Press, Inc., ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS
Arch. Biochem. Biophys., Feb. 1995, [Reviewed]

Production and epitope specificity of monoclonal antibodies against mouse peptidylarginine deiminase type II
Hiroko Koike、Khoich Sase; Hiroyuki Uchida; Tadashi Sudo; Masakazu Shiraiwa; Kiyoshi Sugawara; Hidenari Takahara, Peptidylarginine deiminase catalyzes the conversion of arginyl residues in proteins to citrullyl residues in the presence of Ca2+. We described the preparation of monoclonal antibody (subclass type IgG(1)) specific to mouse peptidylarginine deiminase type II. The antibody had no effect on the enzyme activity and its specific epitope was localized in the eight-residue segment at the amino-terminal portion of the enzyme., TAYLOR & FRANCIS LTD
Biosci. Biotech. Biochem., Dec. 1994, [Reviewed]

Proteins deiminated by peptidylarginine deiminase in mouse uterus and their charge during estrous cycle
Masakazu Shiraiwa; Kazunobu Idota; Tomoji Arai; Hidenari Takahara; Kiyoshi Sugawara, Peptidylarginine deiminase (PAD) catalyzes the formation of citrullyl residues by deimination of arginyl residues of proteins in the presence of Ca2+. We found several deiminated proteins in mouse uterus using antibodies recognizing the citrulline residue. The levels of these proteins changed during the estrous cycle in parallel with PAD activity. © 1994 Taylor &
Francis Group LLC.
Biosci. Biotech. Biochem., Jul. 1994, [Reviewed]

An active-site peptide containing the second essential carboxyl group of dextransucrase from Leuconostoc mesenteroides by chemical modifications
Kazumi Funane; Masakazu Shiraiwa; Kenya Hashimoto; Eiji Ichishima; Mikihiko Kobayashi, The treatment of Leuconostoc mesenteroides B-512F dextransucrase with 10 mM 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC) and glycine ethyl ester (GEE) inactivated the enzyme almost completely within 24 min where the modification of one carboxyl group/mol of the enzyme by EDC was attained. Though 30 mM diethyl pyrocarbonate (DEP) also inactivated the enzyme, about 35% of the activity remained during a 36-min incubation. When 10 mol of imidazole residues/mol of the enzyme was modified by DEP, 50% of the activity was still retained. The addition of the substrate sucrose greatly retarded the enzyme inactivation by EDC. However, the addition of dextran slightly protected the inactivation of the glucosyl-transferring activity and accelerated the inactivation of the sucrose-cleaving activity. In the case of DEP, the addition of sucrose or dextran gave no influence on the inactivation of the enzyme. Therefore, the carboxyl group seemed to play a more important role in the substrate binding and in the catalytic activity of the dextransucrase than the imidazolium group. Differential labeling of Leuconostoc dextransucrase by EDC was conducted in the presence of a sucrose analog, sucrose monocaprate. The fluorescent probe N-(1-naphthyl)ethylenediamine (EDAN) was used as the nucleophile instead of GEE. A fluorescent labeled peptide was isolated from a trypsin digest of the EDC-EDAN modified enzyme. The amino acid sequence of the isolated peptide was Leu-Gln-Glu-Asp-Asn-Ser-Asn-Val-Val-Val-Glu-Ala. The sequence had about 58% homology to those of streptococcal glucosyltransferases GTF-S and GTF-I producing soluble and insoluble dextrans. Those peptides were distinguished from the active-site peptides of GTF-S and GTF-I from S. mutans, which contained catalytic aspartic acid residues of Asp465 and Asp451, respectively. They were located at 30-45 amino acids toward the amino terminal from the catalytic aspartic acid. Therefore, the isolated peptide seemed to contain the second essential carboxyl group for the catalytic activity., AMER CHEMICAL SOC
Biochemistry, Dec. 1993, [Reviewed]

Solubilities of soybean saponins and their solubilization with a bisdesmoside saponin
Makoto Shimoyamada; Yoshihumi Osugi; Masakazu Shiraiwa; Kazuyoshi Okubo; Kenji Watanabe, The solubilities of Bb (soyasaponin I), one of the major monodesmoside saponins in soybean seeds, were measured in aqueous ethanol and buffer. Bb showed the highest solubility in 60% ethanol, and was more soluble in alkaline region in buffers prepared at various pHs. On the other hand, Bb' (soyasaponin III) and B-G (3-O-beta-D-glucuronopyranosyl soyasapogenol B) were almost insoluble in buffer. Solubilities of Bb, Bb' and B-G in buffer were increased by the addition of Ab (acetyl-soyasaponin A1), which is one of the major bisdesmoside saponins in soybean seed hypocotyl. The solubilizing effects of bisdesmoside saponins on monodesmosides, which are responsible for some physiological effects in soybean, may be important for processing beneficial foods using saponins for human consumpution., JAPAN SOC FOOD SCIENCE TECHNOLOGY
Nippon Shokuhin Kogyo Gakkaishi, Mar. 1993, [Reviewed]

Composition and structure of "group B saponin" in soybean seed
Masakazu Shiraiwa; Kyuya Harada; Kazuyoshi Okubo, The composition of "group B saponin" in soybean seed was analyzed by HPLC, and six kinds of "group B saponin," named Ba, Bb, Bb', Bc, Bd and Be according to elution order from HPLC, were detected. Of these saponins, Ba, Bb, Bb' and Bc were identified with soyasaponin V, I, III and II, respectively. Bd and Be were novel saponins possessing soyasapogenol E as the aglycone and the same sugar chain as Ba and Bb, respectively. These saponins were very unstable in the isolated state and had a tendency to form Ba and Bb, respectively. From these results, Bd and Be are presumed to be the precursors of Ba and Bb in soybean seed., JAPAN SOC BIOSCI BIOTECHN AGROCHEM
Agric. Biol. Chem., Apr. 1991, [Reviewed]

Composition and structure of "group A saponin" in soybean seed
Masakazu Shiraiwa; Shigemitu Kudo; Makoto Shimoyamada; Kazuyoshi Okubo, The composition of "group A saponin" in the seed hypocotyl of soybean was analyzed, and six kinds of "group A saponins," named Aa, Ab, Ac, Ad, Ae and Af according to their elution order from HPLC, were detected. On the basis of chemical and physicochemical evidence, Aa, Ab, Ae and Af are shown to be identical with the known saponins,-soyasponins acetyl-soyasaponins A4, A1, ?A5, and 52, respectivity, whilst Ac and Ad were novel saponins possessing different sugar chains. In all these saponins, the terminal sugar of the oligosaccharide chain attached to C-22 of an aglycone (soyasapogenol A) was acetylated in the soybean seed., JAPAN SOC BIOSCI BIOTECHN AGROCHEM
Agric. Biol. Chem., Feb. 1991, [Reviewed]

Composition and content of saponin in soybean seed according to variety, cultivation year and maturity
Masakazu Shiraiwa; Kyuya Harada; Kazuyoshi Okubo, There was a remarkable varietal difference in regard to the composition of "group A saponin" in seed hypocotyls of 457 varieties of soybeans. It was observed that the saponin composition in soybean seed was not affected by the difference in the year of cultivation of the seed, but was peculiar to the variety. The content of total saponin in the seed hypocotyl fraction of soybean ranged from 0.62-6.16%. The content of saponin in soybean seed was more greatly dependent on the variety than on the cultivation year. In soybean seeds harvested at different degrees of maturity, the saponin content varied with the maturity of seed, although the nature of this variation was insufficient to exert an influence upon the varietal difference., JAPAN SOC BIOSCI BIOTECHN AGROCHEM
Agric. Biol. Chem., Feb. 1991, [Reviewed]

Soybean saponin ; Structure and physiological properties, especially antiviral activity on HIV in vitro　　　　　　　　　　　　　　　
Masakazu Shiraiwa; Hideki Nakashima; Naoki Yamamoto; Tsutomu Tamura; Satoshi Matsuda; Kazuyoshi Okubo
International Conference of Soybean Processing and Utilization Proceeding, 1991

Inheritance of "group A saponin" in soybean seed
Masakazu Shiraiwa; Fumio Yamauchi; Kyuya Harada; Kazuyoshi Okubo, JAPAN SOC BIOSCI BIOTECHN AGROCHEM
Agric. Biol. Chem., Jun. 1990, [Reviewed]

Effect of glycosides like saponin on vegetable food processing (Part I). Chemical structures of soybean saponins　　　　　　　　　　　　　　　
Masakazu Shiraiwa; Makoto Shimoyamada; Kazuyoshi Okubo; Fumio Yamauchi; Masayuki Yoshikawa; Isao Kitagawa
International Symposium on New Technology of Vegetable Proteins Oils and Starch Processing, Nov. 1987

Effect of glycosides like saponin on vegetable food processing (Part III) Distribution of glycosides like saponin on vegetable plant　　　　　　　　　　　　　　　
Makoto Shimoyamada; Masakazu Shiraiwa; Shigemitu kudou; Yoshihiro Kamata; Kazuyoshi Okubo; Fumio Yamauchi; kyuya Harada
International Symposium on New Technology of Vegetable Proteins Oils and Starch Processing, Nov. 1987

低不快味大豆育種を目的としたAグループサポニンの生合成に関与する水酸化酵素に関する研究　　　　　　　　　　　　　　　
白岩雅和; 橋浦淳
大豆たん白質研究, Oct. 2006

低不快味大豆育種を目的としたAグループサポニン生合成酵素に関する研究　　　　　　　　　　　　　　　
白岩雅和
大豆たん白質研究, Oct. 2005

低不快味大豆育種を目的とした大豆サポニン生合成酵素に関する研究　　　　　　　　　　　　　　　
白岩雅和; 安田一美
大豆たん白質研究, Oct. 2004

ストレス耐性作物の作出を目的としたライ麦における新しい活性酸素消去機構の解明　　　　　　　　　　　　　　　
白岩雅和
タカノ農芸化学研究助成財団平成１４年度助成研究報告書, Sep. 2003

生理活性グルクロン酸含有糖鎖合成のための新規酵素の検索と反応特性の解明　　　　　　　　　　　　　　　
白岩雅和; 高原英成
糖質の構造改変による高機能性素材の開発に関する総合研究研究成果集, Mar. 2003

大豆サポニンの生理的役割の解明および付加価値の高い大豆品種の育種を目的としたグルクロン酸転移酵素の精製と性質性質の解明　　　　　　　　　　　　　　　
白岩雅和; 黒澤康紀
大豆たん白質研究, Oct. 2001

納豆の研究法（第５章 機能性成分分析法 ４.サポニン）　　　　　　　　　　　　　　　
白岩雅和, Joint work
株式会社恒星社恒星閣, 10 Mar. 2010

種子の科学とバイオテクノロジー （第３章 種子成分の生合成と生化学 10.種子の二次代謝（ダイズサポニン））　　　　　　　　　　　　　　　
白岩雅和, Joint work
学会出版センター, Mar. 2009

機能性糖質素材の開発と食品への応用（【配糖体・糖誘導体・その他】第９章 大豆サポニンの機能性）　　　　　　　　　　　　　　　
白岩雅和, Joint work
シーエムシー出版, 31 Aug. 2005

コーヒー豆に含まれる成分の変化がコーヒーの味に及ぼす影響　　　　　　　　　　　　　　　
菊地 歩実、 飯髙 亘、白岩 雅和
日本農芸化学会関東支部2022年度大会, 27 Aug. 2022

大豆サポニンの抗炎症活性とその活性発現メカニズムの解析　　　　　　　　　　　　　　　
大窪 まどか、白岩 雅和
日本農芸化学会関東支部2021年度大会, 24 Aug. 2021

キクイモの塊茎および葉抽出液の抗酸化能に関する研究　　　　　　　　　　　　　　　
中島 理沙; 白岩 雅和
日本農芸化学会関東支部2020年度大会, 28 Nov. 2020

キクイモ塊茎に含まれる白血病細胞増殖抑制成分の同定と他の抗ガン活性成分との併 用効果　　　　　　　　　　　　　　　
太田 圭佑; 山崎 桜; 白岩 雅和
日本農芸化学会関東支部2020年度大会, 28 Nov. 2020

製造工程による納豆中の大豆サポニンの含量と組成の制御に関する研究　　　　　　　　　　　　　　　
山口加奈
日本食品科学工学会2019年度大会, 31 Aug. 2019

各種大豆サポニンのヒト結腸ガン細胞に対する増殖抑制効果　　　　　　　　　　　　　　　
井川大暉; 白岩雅和
日本食品科学工学会2018年度大会, 24 Aug. 2018

マウスマクロファージ細胞RAW264における各種大豆サポニンの抗炎症活性　　　　　　　　　　　　　　　
森本可菜子
日本食品科学工学会2018年度大会, 24 Aug. 2018

Research on anti-inflammatory compounds contained in Jerusalem artichoke tuber　　　　　　　　　　　　　　　
Shugo KUROSAWA; Yuri SHITOU; Chika MITSUMORI; Masakazu SHIRAIWA
日本農芸化学会2017年度大会, 18 Mar. 2017

Elucidation of the compounds which inhibit the proliferation of leukemia cells from a Jerusalem artichoke tuber　　　　　　　　　　　　　　　
小林 悠生; 高橋 優佳; 五十嵐 大輔; 白岩 雅和
日本農芸化学会2016年度大会, 28 Mar. 2016

キクイモ塊茎に含まれる前立腺ガン細胞増殖抑制成分の探索　　　　　　　　　　　　　　　
柴田祥平; 竹花駿平; 白岩雅和
日本農芸化学会2014年度大会, 30 Mar. 2014

発芽大豆根におけるDDMPグループサポニンの活性酸素種代謝制御による根伸長メカニズム　　　　　　　　　　　　　　　
永井華澄; 八木絵美; 小牧香里; 石川佳奈子; 伊藤慧; 佐々木由香里; 白岩雅和
日本農芸化学会2014年度大会, 29 Mar. 2014

Aグループサポニンの大豆種子発芽における生理機能の解明　　　　　　　　　　　　　　　
松本剣; 白岩雅和
日本農芸化学会2014年度大会, 29 Mar. 2014

発芽期大豆種子からクローニングされた転移酵素遺伝子の特徴付け　　　　　　　　　　　　　　　
河上茉奈実; 市村悠子; 御園久代; 佐藤光朗; 小島俊雄; 高原英成; 白岩雅和
日本農芸化学会2014年度大会, 28 Mar. 2014

大豆サポニン生合成の活性化メカニズムとサポニン生合成を活性化させた大豆種子における機能性　　　　　　　　　　　　　　　
日本農芸化学会2013年度大会, 26 Mar. 2013

キクイモ塊茎に含まれる抗ガン活性成分に関する研究　　　　　　　　　　　　　　　
竹花駿平; 白岩雅和
日本農芸化学会2012年度大会, 24 Mar. 2012, 日本農芸化学会

大豆サポニンの抗肥満活性に関する研究　　　　　　　　　　　　　　　
飯塚正浩; 白岩雅和
日本農芸化学会2012年度大会, 23 Mar. 2012, 日本農芸化学会

大豆種子の栽培および保存条件の制御によるサポニン含量の変化　　　　　　　　　　　　　　　
斉藤哲史; 白岩雅和; 窪田真子; 常楽真由美; 石川佳奈子; 深澤厚子
日本農芸化学会2012年度大会, 23 Mar. 2012, 日本農芸化学会

大豆サポニン生合成に関与するグルクロン酸転移酵素遺伝子の探索　　　　　　　　　　　　　　　
市村悠子; 御園久代; 橋浦淳; 小島俊雄; 高原英成; 白岩雅和
日本農芸化学会2011年度大会, 28 Mar. 2011, 日本農芸化学会

ヒトPeptidylarginine deiminase Type I 遺伝子の第１イントロンにはエンハンサー活性が存在する　　　　　　　　　　　　　　　
応士波; 董四君; 小島俊雄; 白岩雅和; 川田暁; 高原英成
日本農芸化学会2008年度大会, 27 Mar. 2008

ヒトPeptidylarginine deiminase Type 4のN末端ドメインの構造と機能に関する研究　　　　　　　　　　　　　　　
青木香絵; 小島俊雄; 白岩雅和; 高原英成
日本農芸化学会2008年度大会, 27 Mar. 2008

大豆サポニン生合成におよぼすジャスモン酸メチルおよび過酸化水素の影響　　　　　　　　　　　　　　　
橋浦淳; 曽根日和; 窪田真子; 小島俊雄; 高原英成; 白岩雅和
日本農芸化学会2008年度大会, 27 Mar. 2008

新規ダイズ遺伝子GmTDF-5を過剰発現する形質転換植物の耐塩性評価　　　　　　　　　　　　　　　
牧山太樹; 木下美幸; 山田知恵; 小島俊雄; 白岩雅和; 高原英成
日本農芸化学会2008年度大会, 27 Mar. 2008

ダイズOxysterol-binding proteinに結合する脂質の探索　　　　　　　　　　　　　　　
北川貴規; 高橋暢維; 小島俊雄; 白岩雅和; 高原英成
日本農芸化学会2008年度大会, 27 Mar. 2008

ヒトPeptidylarginine deiminase Type I遺伝子の基本的転写調節領域及び基本転写因子の解明　　　　　　　　　　　　　　　
応士波; 董四君; 小島俊雄; 白岩雅和; 川田暁; 高原英成
日本農芸化学会2007年度大会, 2007

ダイズ塩ストレス応答性遺伝子GmTDF-5の過剰発現が及ぼす植物耐塩性への影響　　　　　　　　　　　　　　　
牧山 太樹; 高橋 亜理沙; 兼上 明美; 小島 俊雄; 白岩 雅和; 高原 英成
第２５回日本植物細胞分子生物学会大会, 2007

発芽大豆におけるDDMPグループサポニンの生理機能の解明　　　　　　　　　　　　　　　
八木絵美; 安田一美; 黒澤康紀; 高原英成; 白岩雅和
日本農芸化学会2006年度大会, 2006

ヒト表皮・毛嚢で発現するPeptidylarginine deiminase遺伝子群の発現制御機構　　　　　　　　　　　　　　　
董四君; 小島俊雄; 白岩雅和; 川田暁; 高原英成
日本農芸化学会2006年度大会, 2006

ダイズPR-5蛋白質群における遺伝子構造とストレス応答性の比較解析　　　　　　　　　　　　　　　
舘裕之; 福田久美子; 小島俊雄; 白岩雅和; 高原英成
日本農芸化学会2006年度大会, 2006

ライ麦のルテオリン代謝に関与するβ-グルクロニダーゼの分離と精製　　　　　　　　　　　　　　　
村上智史; 根本絵美; 高原英成; 白岩雅和
第２４回日本植物細胞分子生物学会大会, 2006

大豆栽培条件の制御によるAグループサポニンとDDMPグループサポニンの組成改変　　　　　　　　　　　　　　　
白岩雅和; 曽根日和; 安田一美; 高原英成
第２７回種子生理生化学研究会年会, 2006

機能性食品としての納豆について　　　　　　　　　　　　　　　
白岩雅和
平成１７年度茨城農業改革実践ミニシンポジウム「茨城の納豆を考える」, 27 Oct. 2005, [Invited]

低不快味、高機能性大豆の開発を目的とした大豆サポニン生合成経路と生理機能の解明　　　　　　　　　　　　　　　
白岩雅和
国立遺伝学研究所研究集会プログラム「ダイズのバイオリソースとゲノミクスの進展」, 2005, [Invited]

塩ストレスに応答するダイズオキシステロール結合蛋白質の遺伝子単離と構造解析　　　　　　　　　　　　　　　
井上速見
第２８回日本分子生物学会大会, 2005

ストレス／非ストレス環境におけるダイズオキシステロール結合蛋白質の遺伝子発現制御解析　　　　　　　　　　　　　　　
高橋暢維
第２８回日本分子生物学会大会, 2005

大豆配糖体（サポニン）の機能研究最前線　　　　　　　　　　　　　　　
白岩雅和
食品開発展2004記念セミナー, 07 Oct. 2004, [Invited]

DDMPグループサポニンによる発芽大豆の根の伸長促進メカニズムの解明　　　　　　　　　　　　　　　
八木絵美; 安田一美; 黒澤康紀; 高原英成; 白岩雅和
日本農芸化学会2004年度大会, 2004

ルテオリン配糖体を基質とするライ麦初期葉中のペルオキシダーゼアイソザイムの精製と性質の比較および反応生成物の解析　　　　　　　　　　　　　　　
村上智史; 高原英成; 白岩雅和
日本農芸化学会2004年度大会, 2004

ダイズにおける塩ストレス誘導性遺伝子GmTDF-5の解析　　　　　　　　　　　　　　　
兼上明美; 青木亜矢子; 小島俊雄; 白岩雅和; 高原英成
日本農芸化学会2004年度大会, 2004

大豆サポニンの生合成と生理機能およびその応用　　　　　　　　　　　　　　　
白岩雅和
第５１回日本食品科学工学会大会シンポジウム, 2004, [Invited]

塩ストレス応答における新規ダイズ遺伝子GmTDF-5の機能解析　　　　　　　　　　　　　　　
兼上明美
第２７回日本分子生物学会大会, 2004

塩ストレスに対する新規ダイズ遺伝子GmTDF-5の転写制御機構　　　　　　　　　　　　　　　
三原迪子
第２７回日本分子生物学会大会, 2004

ダイズPR-5蛋白質群の遺伝子構造とストレス応答性の比較　　　　　　　　　　　　　　　
舘裕之
第２７回日本分子生物学会大会, 2004

大豆植物体におけるサポニンの生理的役割と生理機能発現メカニズムの解明　　　　　　　　　　　　　　　
白岩雅和; 安田一美; 八木絵美; 黒澤康紀; 高原英成
第２５回種子生理生化学研究会年会, 2004

過酸化水素処理によるライ麦初期葉中のペルオキシダーゼの活性変動および過酸化水素感受性ペルオキシダーゼの精製と性質の解明　　　　　　　　　　　　　　　
村上智史; 鈴木麻由子; 高原英成; 白岩雅和
日本農芸化学会2003年度大会, 2003

大豆種子登熟期のサポニン生合成に関与するグルクロン酸転移酵素の変動と性質の解明　　　　　　　　　　　　　　　
安田一美; 高原英成; 白岩雅和
日本農芸化学会2003年度大会, 2003

組換え型ヒトpeptidylarginine deiminase type Iの大量発現ベクターの構築並びに同組換え型酵素の精製及び酵素化学的性質　　　　　　　　　　　　　　　
槐正明; 原田一明; 川田暁; 白岩雅和; 高原英成
日本農芸化学会2003年度大会, 2003

塩ストレスに応答するダイズ由来PR-5タンパク質、GmOLPの遺伝子解析　　　　　　　　　　　　　　　
小島俊雄; 大西真理; 白岩雅和; 高原英成
日本植物細胞分子生物学会2003年度大会, 2003

ダイズにおける塩ストレス応答性β-グルコシダーゼ遺伝子の単離および遺伝子発現解析　　　　　　　　　　　　　　　
小椋真紀; 小島俊雄; 白岩雅和; 高原英成
日本分子生物学会2003年度大会, 2003

ダイズプロリン代謝関連酵素遺伝子群の発現解析　　　　　　　　　　　　　　　
前田良彦; 小島俊雄; 白岩雅和; 高原英成
日本分子生物学会2003年度大会, 2003

発芽大豆におけるmonodesmosidic saponinの糖鎖生合成酵素群の精製と性質　　　　　　　　　　　　　　　
黒澤康紀; 高原英成; 白岩雅和
日本農芸化学会2002年度大会, 2002

発芽大豆におけるサポニンの生合成と根の伸長に及ぼすサポニンの影響　　　　　　　　　　　　　　　
白岩雅和; 黒澤康紀; 安田一美; 高原英成
日本農芸化学会2002年度大会, 2002

ダイズにおける塩ストレス誘導性オスモチン遺伝子の単離と発現解析　　　　　　　　　　　　　　　
大西真理; 青木亜矢子; 小島俊雄; 白岩雅和; 高原英成
日本農芸化学会2002年度大会, 2002

Molecular Cloning of two soybean cysteine proteinase genes in senescing cotyledon by cDNA representational difference analysis　　　　　　　　　　　　　　　
Jianqun Ling; Toshio Kojima; Masakazu Shiraiwa; Hidenari Takahara
日本農芸化学会2002年度大会, 2002

過酸化水素処理したライ麦初期葉におけるルテオリン配糖体およびその代謝酵素群の動態　　　　　　　　　　　　　　　
鈴木麻由子; 村上智史; 根本絵美; 高原英成; 白岩雅和
日本植物細胞分子生物学会2002年度大会, 2002

ルテオリン配糖体を基質とする過酸化水素消去反応を触媒するペルオキシダーゼの精製と性質の解明　　　　　　　　　　　　　　　
村上智史; 鈴木麻由子; 根本絵美; 高原英成; 白岩雅和
日本植物細胞分子生物学会2002年度大会, 2002

発芽大豆の根におけるAグループサポニンとDDMPグループサポニンの生合成と根の伸長におよぼす影響　　　　　　　　　　　　　　　
安田一美; 黒澤康紀; 野田香織; 高原英成; 白岩雅和
日本植物細胞分子生物学会2002年度大会, 2002

Peptidylarginine deiminase Type IおよびType III遺伝子の転写制御機構の解析　　　　　　　　　　　　　　　
董四君; 小島俊雄; 白岩雅和; 川田暁; 高原英成
日本分子生物学会2002年度大会, 2002

マウスPeptidylarginine deiminase Type II遺伝子の発現調節機構の解析　　　　　　　　　　　　　　　
後藤梨香; 小島俊雄; 白岩雅和; 高原英成
2002

CysP1 and CysP2, encoding two cysteine proteinases with C-terminal KDEL motif, are soybean cotyledon senescence-associated genes　　　　　　　　　　　　　　　
Ling JQ; T Kojima; M.Shiraiwa; H takahara
日本分子生物学会2002年度大会, 2002

ダイズオスモチン遺伝子のストレス応答性とその発現制御機構　　　　　　　　　　　　　　　
大西真理; 小島俊雄; 白岩雅和; 高原英成
日本分子生物学会2002年度大会, 2002

ダイズOSBP遺伝子の単離とその遺伝子解析　　　　　　　　　　　　　　　
李東艶; 小島俊雄; 白岩雅和; 高原英成
日本分子生物学会2002年度大会, 2002

ライ麦初期葉におけるフラボノイド代謝が関与する新しい活性酸素消去機構の解明　　　　　　　　　　　　　　　
白岩雅和; 鈴木麻由子; 村上智史; 根本絵美; 高原英成
第２３回種子生理生化学研究会年会, 2002

ダイズおける塩ストレス応答性遺伝子群のcDNA-AFLP解析　　　　　　　　　　　　　　　
小島俊雄; 青木亜矢子; 白岩雅和; 高原英成
第２３回種子生理生化学研究会年会, 2002

ダイズ塩ストレス誘導性オスモチン遺伝子の単離とスチレス応答性解析　　　　　　　　　　　　　　　
大西真理; 小島俊雄; 白岩雅和; 高原英成
第２３回種子生理生化学研究会年会, 2002

ライ麦初期葉中におけるルテオリン代謝に関与するグルクロン酸転移酵素の精製とその性質　　　　　　　　　　　　　　　
鈴木麻由子; 黒澤康紀; 高原英成; 白岩雅和
日本農芸化学会2001年度大会, 2001

発芽大豆におけるサポニンの生合成経路と生理機能の解明　　　　　　　　　　　　　　　
白岩雅和; 黒澤康紀; 安田一美; 高原英成
第２２回種子生理生化学研究会年会, 2001

塩ストレスに対するダイズプロリン生合成関連酵素の遺伝子解析　　　　　　　　　　　　　　　
小島俊雄; 緒形沙百合; 大西真理; 前田良彦; 青木亜矢子; 白岩雅和; 高原英成
第２２回種子生理生化学研究会年会, 2001

exo-β-グルクロニダーゼによるグルクロン酸転移反応　　　　　　　　　　　　　　　
望月毅; 高原英成; 白岩雅和
日本農芸化学会1999年度大会, 1999

Peptidylarginine deiminase遺伝子の組織特異的発現調節機構に関する研究　　　　　　　　　　　　　　　
日本農芸化学会1999年度大会, 1999

ヒトPeptidylarginine deiminase Type IIIの大腸菌発現系の構築と精製およびヒト毛嚢蛋白質トリコヒアリンに対する反応特性　　　　　　　　　　　　　　　
日本農芸化学会1999年度大会, 1999

組換え型ヒトPeptidylarginine deiminase Type IIIのヒト毛嚢蛋白質トリコヒアリンに対する反応特性　　　　　　　　　　　　　　　
菅野拓也; 川田暁; STEINERT PM; 白岩雅和; 高原英成
日本生化学会1999年度大会, 1999

大豆サポニン生合成に関与するグルクロン酸転移酵素の精製　　　　　　　　　　　　　　　
黒澤康紀; 高原英成; 白岩雅和
第２０回種子生理生化学研究会年会, 1999

大豆サポニングルクロン酸転移酵素の可溶化と精製　　　　　　　　　　　　　　　
黒澤康紀; 高原英成; 白岩雅和
日本農芸化学会1998年度大会, 1998

Peptidylarginine deiminaseの活性中心構造に関する研究 –活性発現に関与するCys残基の同定及び活性中心構造の解明-　　　　　　　　　　　　　　　
小松ひとみ; 白岩雅和; 高原英成
日本農芸化学会1998年度大会, 1998

マウス表皮細胞由来新規peptidylarginine deiminase Type αのcDNAクローニングと構造解析　　　　　　　　　　　　　　　
小野博之; 白岩雅和; 高原英成
日本農芸化学会1998年度大会, 1998

Molecular Cloning and Characterization of cDNA of Murine Peptidylarginine deiminase Type III　　　　　　　　　　　　　　　
Ahmed Abu Rus’; Sayaka Kanematu; Masakazu Shiraiwa; Hidenari Takahara
日本農芸化学会1998年度大会, 1998

ヒトPeptidylarginine deiminaseType IIIのクローニングと発現調節機構の解明　　　　　　　　　　　　　　　
山木綾子; 菅野拓也; 川田暁; 白岩雅和; 高原英成
日本生化学会1998年度大会, 1998

ヒトPeptidylarginine deiminase Type IIIの大腸菌発現系の構築　　　　　　　　　　　　　　　
菅野拓也; 川田暁; 白岩雅和; 高原英成
日本生化学会1998年度大会, 1998

マウスPeptidylarginine deiminase Type Iと推定されるcDNAのクローニングと組織特異的発現　　　　　　　　　　　　　　　
池尻泰子; RUS’D Ahmed Abu; 小野博之; 白岩雅和; 高原英成
日本生化学会1998年度大会, 1998

Peptidylarginine deiminaseの活性中心構造に関する研究 –活性発現に関与すると推測される２つHis残基の機能解析-　　　　　　　　　　　　　　　
小松ひとみ; 高原英成; 白岩雅和
日本農芸化学会1997年度大会, 1997

大豆サポニングルクロン酸転移酵素の精製とその性質　　　　　　　　　　　　　　　
黒澤康紀; 高原英成; 白岩雅和
日本農芸化学会1997年度大会, 1997

大豆サポニングルクロン酸転移酵素の性質と発芽大豆における分布　　　　　　　　　　　　　　　
黒澤康紀; 高原英成; 白岩雅和
第１８回種子生理生化学研究会年会, 1997

大豆植物体におけるサポニングルクロン酸転移酵素の分布　　　　　　　　　　　　　　　
黒澤康紀; 高原英成; 白岩雅和
日本農芸化学会1996年度大会, 1996

ヒト正常培養表皮角化細胞由来Peptidylarginine deiminaseType IIIのcDNAクローニングと構造解析　　　　　　　　　　　　　　　
菅野拓也; 土田衛; 土井浩; 鴨田博伸; 川田暁; 小野博之; 白岩雅和; 高原英成
日本生化学会1996年度大会, 1996

マウスpeptidylarginine deiminaseType II遺伝子構造と染色体マッピング　　　　　　　　　　　　　　　
高原英成; 一井正城; 辻本弘昭; 奥村克純; 篭谷和弘; 田口寛; 小野博之; RUS’D Ahmed Abu; 白岩雅和
日本生化学会1996年度大会, 1996

正常ヒト表皮角化培養細胞よりクローニングされた新規Ca2+結合性PDI様蛋白質（EP52）の構造と機能に関する研究　　　　　　　　　　　　　　　
渡邉聡; 白岩雅和; Kimie Fukuyama; 小山洋一; 入江伸吉; 高原英成
日本農芸化学会1995年度大会, 1995

妊娠期マウス子宮におけるpeptidylarginine deiminaseの標的蛋白質の検索　　　　　　　　　　　　　　　
白岩雅和; 西川正晃; 高原英成
日本農芸化学会1995年度大会, 1995

マウスpeptidylarginine deiminaseの化学修飾および部位指定変異法による活性中心残基の同定　　　　　　　　　　　　　　　
神谷貴則; 小山誠司; 白岩雅和; 高原英成
日本農芸化学会1995年度大会, 1995

ラット表皮細胞から見出された新規peptidylarginine deiminase様タンパク質のcDNAクローニングと構造解析　　　　　　　　　　　　　　　
山越敦司; 西条孝幸; 白岩雅和; 高原英成
日本生化学会1995年度大会, 1995

部位指定変異法によるマウスpeptidylarginine deiminaseの活性中心システイン残基の同定と触媒機構に関する研究　　　　　　　　　　　　　　　
成田葉子; 白岩雅和; 国分友邦; 大箸信一; 高原英成
日本生化学会1995年度大会, 1995

非妊娠期マウス子宮におけるpeptidylarginine deiminaseの標的蛋白質の同定　　　　　　　　　　　　　　　
井戸田一伸; 白岩雅和; 高原英成
日本生化学会1995年度大会, 1995

Peptidylarginine deiminaseの阻害剤に関する研究　　　　　　　　　　　　　　　
矢走敦; 白岩雅和; 高原英成; 菅原潔
日本農芸化学会1994年度大会, 1994

ニワトリ脳由来Peptidylarginine deiminaseの精製と構造解析　　　　　　　　　　　　　　　
繁田賢治; 白岩雅和; 菅原潔; 高原英成
日本生化学会1994年度大会, 1994

Peptidylarginine deiminaseの生理機能に関する研究 –非妊娠期マウス子宮における同上酵素標的蛋白質の解析-　　　　　　　　　　　　　　　
井戸田一伸; 白岩雅和; 菅原潔; 高原英成
日本生化学会1994年度大会, 1994

Peptidylarginine deiminase type IIIに関する研究　　　　　　　　　　　　　　　
西条孝幸; 白岩雅和; 菅原潔; Seung-Hoon Cha; Kimie Fukuyama; 高原英成
日本生化学会1994年度大会, 1994

Peptidylarginine deiminaseに関する研究 –同上酵素の性ホルモン誘導時に標的となる蛋白質の同定-　　　　　　　　　　　　　　　
白岩雅和; 井戸田一伸; 吉田真紀; 高原英成; 菅原潔
日本農芸化学会1993年度大会, 1993

Peptidylarginine deiminaseに関する研究 –シトルリン残基特異認識抗体によるマウス同上酵素の標的蛋白質の検索-　　　　　　　　　　　　　　　
吉田真紀; 白岩雅和; 高原英成; 菅原潔
日本農芸化学会1993年度大会, 1993

Peptidylarginine deiminaseに関する研究 –マウスにおけるオルニチン残基の存在と組織間分布-　　　　　　　　　　　　　　　
白岩雅和; 佐々明; 高原英成; 菅原潔
日本農芸化学会1992年度大会, 1992

Peptidylarginine deiminaseに関する研究 –シトルリン残基のHMGタンパク質における存在-　　　　　　　　　　　　　　　
森下繁徳; 白岩雅和; 高原英成; 菅原潔
日本農芸化学会1992年度大会, 1992

大豆種子サポニンの組成と含量における品種間および栽培年度間の差異　　　　　　　　　　　　　　　
白岩雅和; 大久保一良; 山内文男; 原田久也
日本農芸化学会1989年度大会, 1989

大豆サポニンの化学構造とそのAグループ成分における品種間の差異　　　　　　　　　　　　　　　
白岩雅和; 大久保一良; 山内文男; 原田久也; 谷山登志男; 吉川雅之; 北川勲
日本農芸化学会1987年度大会, 1987

胚軸にみられる未確認大豆サポニン成分の組成　　　　　　　　　　　　　　　
下山田真; 吉越昌樹; 白岩雅和; 大久保一良; 山内文男
日本農芸化学会1986年度大会, 1986

Soyasaponin Aaの単離・精製、およびその構造解析　　　　　　　　　　　　　　　
白岩雅和; 吉越昌樹; 大久保一良; 山内文男; 鈴木建夫; 目黒熙
日本農芸化学会1986年度大会, 1986

大豆サポニン（Soyasaponin）の構造解析　　　　　　　　　　　　　　　
白岩雅和; 吉越昌樹; 大久保一良; 山内文男; 鈴木建夫; 目黒熙; 五十嵐正倫; 北川勲; 吉川雅之
日本農芸化学会 1985年度大会, 1985

大豆サ ポニンのHPLCによる定　　　　　　　　　　　　　　　
五十嵐正倫; 吉越昌樹; 白岩雅和; 大久保一良; 山内文男; 斎尾恭子
日本農芸化学会1985年度大会, 1985

大豆サポニンの組成とその呈味性　　　　　　　　　　　　　　　
吉越昌樹; 白岩雅和; 浅野三夫; 大久保一良; 山内文男; 五十嵐正倫; 広野治
日本農芸化学会1985年度大会, 1985

大豆サ,ポニンのHPLCによる定　　　　　　　　　　　　　　　
五十嵐正倫、吉越昌樹、白岩雅和、大久保一良、山内文男、斎尾恭子
日本農芸化学会1985年度大会, 1985