메뉴 건너뛰기




Volumn 64, Issue 1, 2000, Pages 116-124

High molecular weight transglutaminase inhibitor produced by a microorganism (Streptomyces lavendulae Y-200)

Author keywords

Bitor; Transglutaminase; Transglutaminase inhi

Indexed keywords

CALCIUM; CASEIN; ENZYME INHIBITOR; HISTAMINE; N,N DIMETHYLCASEIN; N,N-DIMETHYLCASEIN; PRONASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRYPSIN;

EID: 0033630190     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.64.116     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0017680149 scopus 로고
    • The ε-(γ-glutamyl) lysine crosslink and the catalytic role of transglutaminases
    • Folk, J. E. and Finlayson, J. S., The ε-(γ-glutamyl) lysine crosslink and the catalytic role of transglutaminases. Advances in Protein Chemistry, 31, 1-133 (1977).
    • (1977) Advances in Protein Chemistry , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 3
    • 0023810359 scopus 로고
    • Searching for the function of tissue transglutaminase: Its possible involvement in the biochemical pathway of programmed cell death
    • Fesus, L. and Thomazy, V., Searching for the function of tissue transglutaminase: Its possible involvement in the biochemical pathway of programmed cell death. Adv. Exp. Med. Biol., 231, 119-134 (1988).
    • (1988) Adv. Exp. Med. Biol. , vol.231 , pp. 119-134
    • Fesus, L.1    Thomazy, V.2
  • 4
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C. S., Birckbichler, P. J., and Rice, R. H., Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues. FASEB J., 5, 3071-3077 (1991).
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 5
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and fluids
    • Aeschliman, D. and Paulsson, M., Transglutaminases: Protein cross-linking enzymes in tissues and fluids. Thrombosis and Haemostasis, 71, 402-415 (1994).
    • (1994) Thrombosis and Haemostasis , vol.71 , pp. 402-415
    • Aeschliman, D.1    Paulsson, M.2
  • 6
    • 0018200368 scopus 로고
    • Cellular transglutaminase, growth, and transformation
    • Birckbichler, P. J. and Patterson, M. K., Jr., Cellular transglutaminase, growth, and transformation. Ann. N. Y. Acad. Sci., 312, 354-365 (1978).
    • (1978) Ann. N. Y. Acad. Sci. , vol.312 , pp. 354-365
    • Birckbichler, P.J.1    Patterson M.K., Jr.2
  • 9
    • 0021327593 scopus 로고
    • Induction of tissue transglutaminase in human peripheral blood monocytes
    • Murtaugh, M. P., Arend, W. P., and Davies, P. J. A., Induction of tissue transglutaminase in human peripheral blood monocytes. J. Exp. Med., 159, 114-125 (1984).
    • (1984) J. Exp. Med. , vol.159 , pp. 114-125
    • Murtaugh, M.P.1    Arend, W.P.2    Davies, P.J.A.3
  • 10
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus, L., Thomazy, V., and Falus, A., Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett., 224, 104-108 (1987).
    • (1987) FEBS Lett. , vol.224 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 11
    • 0024520475 scopus 로고
    • Apoptotic hepatocytes become insoluble in detergents and chaotropic agents as a result of transglutaminase action
    • Fesus, L., Thomazy, V., Autouri, F., Ceru, M. P., Tarcsa, E., and Piacentini, M., Apoptotic hepatocytes become insoluble in detergents and chaotropic agents as a result of transglutaminase action. FEBS Lett., 245, 150-154 (1989).
    • (1989) FEBS Lett. , vol.245 , pp. 150-154
    • Fesus, L.1    Thomazy, V.2    Autouri, F.3    Ceru, M.P.4    Tarcsa, E.5    Piacentini, M.6
  • 13
    • 0029856043 scopus 로고    scopus 로고
    • Neurodegenerative diseases and transglutaminase
    • Lorand, L., Neurodegenerative diseases and transglutaminase. Proc. Natl. Acad. Sci. U.S.A., 93, 14310-14313 (1996).
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 14310-14313
    • Lorand, L.1
  • 14
    • 0030948138 scopus 로고    scopus 로고
    • In vitro neurotoxicity of amyloid β-peptide cross-linked by transglutaminase
    • Ikura, K., Takahata, K., Shinagawa, R., Masuda, S., and Sasaki, R., In vitro neurotoxicity of amyloid β-peptide cross-linked by transglutaminase. Cytotechnology, 23, 77-85 (1997).
    • (1997) Cytotechnology , vol.23 , pp. 77-85
    • Ikura, K.1    Takahata, K.2    Shinagawa, R.3    Masuda, S.4    Sasaki, R.5
  • 16
    • 0021349883 scopus 로고
    • Transglutaminase activity in human and rabbit ear comedogenesis: A histochemical study
    • Young, L. D., Ballaron, S., and Epstein, W., Transglutaminase activity in human and rabbit ear comedogenesis: a histochemical study. J. Invest. Dermatol., 82, 275-279 (1984).
    • (1984) J. Invest. Dermatol. , vol.82 , pp. 275-279
    • Young, L.D.1    Ballaron, S.2    Epstein, W.3
  • 17
    • 0022636330 scopus 로고
    • Precocious appearance of involculin and epidermal transglutaminase during differentiation of psoriatic skin
    • Bernard, B. A., Reano, A., Darmon, Y. M., and Thivolet, J., Precocious appearance of involculin and epidermal transglutaminase during differentiation of psoriatic skin. Br. J. Dermatol., 114, 279-283 (1986).
    • (1986) Br. J. Dermatol. , vol.114 , pp. 279-283
    • Bernard, B.A.1    Reano, A.2    Darmon, Y.M.3    Thivolet, J.4
  • 18
    • 0019832659 scopus 로고
    • Transglutaminase activity in normal and hereditary rat lens and its partial purification
    • Azari, P., Rahim, I., and Clarkson, D. P., Transglutaminase activity in normal and hereditary rat lens and its partial purification. Curr. Eye Res., 1, 463-469 (1981).
    • (1981) Curr. Eye Res. , vol.1 , pp. 463-469
    • Azari, P.1    Rahim, I.2    Clarkson, D.P.3
  • 19
    • 0020361280 scopus 로고
    • Transglutaminase activation: Significance with respect to immunologic phenomena
    • Fesus, L., Transglutaminase activation: significance with respect to immunologic phenomena. Surv. Immunol. Res., 1, 297-304 (1982).
    • (1982) Surv. Immunol. Res. , vol.1 , pp. 297-304
    • Fesus, L.1
  • 20
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed ε-(γ-glutamyl)lysine bond formation
    • Folk, J. E., Mechanism and basis for specificity of transglutaminase-catalyzed ε-(γ-glutamyl)lysine bond formation. Adv. Enzymol., 54, 1-56 (1983).
    • (1983) Adv. Enzymol. , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 21
    • 0016757758 scopus 로고
    • Alkyl isocyanates as active site-directed inactivators of guinea pig liver transglutaminase
    • Gross, M., Whetzel, N. K., and Folk, J. E., Alkyl isocyanates as active site-directed inactivators of guinea pig liver transglutaminase. J. Biol. Chem., 250, 7693-7699 (1975).
    • (1975) J. Biol. Chem. , vol.250 , pp. 7693-7699
    • Gross, M.1    Whetzel, N.K.2    Folk, J.E.3
  • 22
    • 0023791242 scopus 로고
    • Synthesis, chemistry, and absolute configuration of novel transglutaminase inhibitors containing a 3-halo-4,5-dihydroisoxazole
    • Castelhano, A. L., Billedeau, R., Pliura, D. H., Bonaventura, B. J., and Krantz, A., Synthesis, chemistry, and absolute configuration of novel transglutaminase inhibitors containing a 3-halo-4,5-dihydroisoxazole. Bioorg. Chem., 16, 335-340 (1988).
    • (1988) Bioorg. Chem. , vol.16 , pp. 335-340
    • Castelhano, A.L.1    Billedeau, R.2    Pliura, D.H.3    Bonaventura, B.J.4    Krantz, A.5
  • 23
    • 0027935343 scopus 로고
    • Transglutaminase inhibition by 2-[(2-oxopropyl)thio]imidazolium derivatives: Mechanism of factor XIIIa inactivation
    • Freund, K. F., Doshi, K. P., Gaul, S. L., Claremon, D. A., Remy, D. C., Baldwin, J. J., Pitzenberger, S. M., and Stern, A. M., Transglutaminase inhibition by 2-[(2-oxopropyl)thio]imidazolium derivatives: mechanism of factor XIIIa inactivation. Biochemistry, 33, 10109-10119 (1994).
    • (1994) Biochemistry , vol.33 , pp. 10109-10119
    • Freund, K.F.1    Doshi, K.P.2    Gaul, S.L.3    Claremon, D.A.4    Remy, D.C.5    Baldwin, J.J.6    Pitzenberger, S.M.7    Stern, A.M.8
  • 24
    • 0021760454 scopus 로고
    • The competitive inhibition of tissue transglutaminase by a-difluoromethylornithine
    • Delcros, J.-G., Roch, A.-M., and Quash, G., The competitive inhibition of tissue transglutaminase by a-difluoromethylornithine. FEBS Lett., 171, 221-226 (1984).
    • (1984) FEBS Lett. , vol.171 , pp. 221-226
    • Delcros, J.-G.1    Roch, A.-M.2    Quash, G.3
  • 25
    • 0022393624 scopus 로고
    • Development of selective inhibitors of transglutaminase. Phenylthiourea derivatives
    • Lee, K. N., Fesus, L., Yancey, S. T., Girard, J. E., and Chung, S. I., Development of selective inhibitors of transglutaminase. Phenylthiourea derivatives. J. Biol. Chem., 260, 14689-14694 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 14689-14694
    • Lee, K.N.1    Fesus, L.2    Yancey, S.T.3    Girard, J.E.4    Chung, S.I.5
  • 26
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • Achyuthan, A. E. and Greenberg, C. S., Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. J. Biol. Chem., 262, 1901-1906 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 1901-1906
    • Achyuthan, A.E.1    Greenberg, C.S.2
  • 28
    • 0025739051 scopus 로고
    • Inhibition of rat liver transglutaminase by nucleotides
    • Kawashima, S., Inhibition of rat liver transglutaminase by nucleotides. Experientia, 47, 709-712 (1991).
    • (1991) Experientia , vol.47 , pp. 709-712
    • Kawashima, S.1
  • 30
    • 0030268101 scopus 로고    scopus 로고
    • Analysis of catalytic action of transglutaminase induced in human promyelocytic leukemia (HL-60) and human hepatoblastoma (HepG2) cells
    • Ikura, K., Shinagawa, R., Hatano, K., Suto, N., and R. Sasaki., Analysis of catalytic action of transglutaminase induced in human promyelocytic leukemia (HL-60) and human hepatoblastoma (HepG2) cells. Biosci. Biotechnol. Biochem., 60, 1738-1739 (1996).
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1738-1739
    • Ikura, K.1    Shinagawa, R.2    Hatano, K.3    Suto, N.4    Sasaki, R.5
  • 31
    • 0001562930 scopus 로고
    • One-step purification of guinea pig liver transglutaminase using a monoclonal-antibody immunoadsorbent
    • Ikura, K., Sakurai, H., Okumura, K., Sasaki, R., and Chiba, H., One-step purification of guinea pig liver transglutaminase using a monoclonal-antibody immunoadsorbent. Agric. Biol. Chem., 49, 3527-3531 (1985).
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 3527-3531
    • Ikura, K.1    Sakurai, H.2    Okumura, K.3    Sasaki, R.4    Chiba, H.5
  • 34
    • 0000326990 scopus 로고
    • Transglutaminase (guinea pig liver)
    • Folk, J. E., Transglutaminase (guinea pig liver). Methods in Enzymology, 17, 889-894 (1970).
    • (1970) Methods in Enzymology , vol.17 , pp. 889-894
    • Folk, J.E.1
  • 35
    • 0015463837 scopus 로고
    • A filter paper assay for transamidating enzymes using radioactive amine substrates
    • Lorand, L., Campbell-Wilkes, L. K., and Cooperstein, L., A filter paper assay for transamidating enzymes using radioactive amine substrates. Anal. Biochem., 50, 623-631 (1972).
    • (1972) Anal. Biochem. , vol.50 , pp. 623-631
    • Lorand, L.1    Campbell-Wilkes, L.K.2    Cooperstein, L.3
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 84954879059 scopus 로고
    • Analysis by high-performance anion-exchange chromatography of component sugars as their fluorescent pyridylamino derivatives
    • Suzuki, J., Kondo, A., Kato, I., Hase, S., and Ikenaka, T., Analysis by high-performance anion-exchange chromatography of component sugars as their fluorescent pyridylamino derivatives. Agric. Biol. Chem., 55, 283-284 (1991).
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 283-284
    • Suzuki, J.1    Kondo, A.2    Kato, I.3    Hase, S.4    Ikenaka, T.5
  • 39
    • 0015295223 scopus 로고
    • Chromogenicity of Streptomyces
    • Arai, T. and Mikami, Y., Chromogenicity of Streptomyces. Appl. Microbiol., 23, 402-406 (1972).
    • (1972) Appl. Microbiol. , vol.23 , pp. 402-406
    • Arai, T.1    Mikami, Y.2
  • 40
  • 41
    • 0026952044 scopus 로고
    • Melanin standard method: Empirical formula 2
    • Chedekel, M. R., Ahene, A. B., and Zeise, L., Melanin standard method: Empirical formula 2. Pigment Cell Res., 5, 240-246 (1992).
    • (1992) Pigment Cell Res. , vol.5 , pp. 240-246
    • Chedekel, M.R.1    Ahene, A.B.2    Zeise, L.3
  • 42
    • 0024417118 scopus 로고
    • Bovine aortic endothelial cell transglutaminse: Enzyme characterization and regulation of activity
    • Korner, G., Schneider, D. E., Purdon, M. A., and Bjornsson, T. D., Bovine aortic endothelial cell transglutaminse: Enzyme characterization and regulation of activity. Biochem. J., 262, 633-641 (1989).
    • (1989) Biochem. J. , vol.262 , pp. 633-641
    • Korner, G.1    Schneider, D.E.2    Purdon, M.A.3    Bjornsson, T.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.