메뉴 건너뛰기




Volumn 18, Issue 5, 1999, Pages 369-380

Cloning, expression, and characterization of human metalloprotease 1: A novel member of the pitrilysin family of metalloendoproteases

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; COMPLEMENTARY DNA; DIPEPTIDYL CARBOXYPEPTIDASE; HUMAN METALLOPROTEINASE 1; HYALURONIDASE; INSULINASE; LEUMORPHIN; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; PITRILYSIN; THERMOLYSIN; UNCLASSIFIED DRUG;

EID: 0032994294     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/104454999315268     Document Type: Article
Times cited : (42)

References (43)
  • 1
    • 0028879135 scopus 로고
    • Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection
    • ADAMES, N., BLUNDELL, K., ASHBY, M.N., and BOONE, C. (1995). Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science 270, 464-467.
    • (1995) Science , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 4
    • 0029022718 scopus 로고
    • Insulysin and pitrilysin: Insulin-degrading enzymes of mammals and bacteria
    • BECKER, A.B., and ROTH, R.A. (1995). Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria. Methods Enzymol. 248, 693-703.
    • (1995) Methods Enzymol. , vol.248 , pp. 693-703
    • Becker, A.B.1    Roth, R.A.2
  • 5
    • 0025762119 scopus 로고
    • PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues
    • BENJANNET, S., RONDEAU, N., DAY, R., CHRETIEN, M., and SEIDAH, N.G. (1991). PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues. Proc. Natl. Acad. Sci. USA 88, 3564-3568.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3564-3568
    • Benjannet, S.1    Rondeau, N.2    Day, R.3    Chretien, M.4    Seidah, N.G.5
  • 6
    • 0028786585 scopus 로고
    • Purification and characterization of a dynorphin processing endoprotease
    • BERMAN, Y.L., JULIANO, L., and DEVI, L.A. (1995). Purification and characterization of a dynorphin processing endoprotease. J. Biol. Chem. 270, 23845-23850.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23845-23850
    • Berman, Y.L.1    Juliano, L.2    Devi, L.A.3
  • 7
    • 2442724590 scopus 로고    scopus 로고
    • Substrate specificity of the dynorphin processing endopeptidases
    • in press
    • BERMAN, Y., JULIANO, L., and DEVI, L.A. (1998). Substrate specificity of the dynorphin processing endopeptidases. J. Neurochem. (in press).
    • (1998) J. Neurochem.
    • Berman, Y.1    Juliano, L.2    Devi, L.A.3
  • 8
    • 0025967144 scopus 로고
    • Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins
    • CHAGAS, J.R., JULIANO, L., and PRADO, E.S. (1991). Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Anal. Biochem. 192, 419-425.
    • (1991) Anal. Biochem. , vol.192 , pp. 419-425
    • Chagas, J.R.1    Juliano, L.2    Prado, E.S.3
  • 11
    • 0027979145 scopus 로고
    • Isolation and characterization of a dibasic selective metalloendopeptidase from rat testis that cleaves at the amino terminus of arginine residues
    • CHESNEAU, V., PIEROTTI, A.R., BARRE, N., CREMIAN, E., TOUGARO, C., and COHEN, P. (1994). Isolation and characterization of a dibasic selective metalloendopeptidase from rat testis that cleaves at the amino terminus of arginine residues. J. Biol. Chem. 259, 2056-2061.
    • (1994) J. Biol. Chem. , vol.259 , pp. 2056-2061
    • Chesneau, V.1    Pierotti, A.R.2    Barre, N.3    Cremian, E.4    Tougaro, C.5    Cohen, P.6
  • 12
    • 0027406156 scopus 로고
    • Tissue distribution of a dynorphin-processing endopeptidase
    • DEVI, L. (1993). Tissue distribution of a dynorphin-processing endopeptidase. Endocrinology 132, 1139-1144.
    • (1993) Endocrinology , vol.132 , pp. 1139-1144
    • Devi, L.1
  • 13
    • 0026029553 scopus 로고
    • Consensus sequence for processing of peptide precursors at monobasic sites
    • DEVI, L.A. (1991a). Consensus sequence for processing of peptide precursors at monobasic sites. FEBS Lett. 280, 189-194.
    • (1991) FEBS Lett. , vol.280 , pp. 189-194
    • Devi, L.A.1
  • 14
    • 0003149562 scopus 로고
    • Peptide processing at monobasic amino acids
    • L.D. Flicker, ed. (CRC Press, Boca Raton, FL)
    • DEVI, L.A. (1991b). Peptide processing at monobasic amino acids. In Peptide Biosynthesis and Processing. L.D. Flicker, ed. (CRC Press, Boca Raton, FL) pp. 175-198.
    • (1991) Peptide Biosynthesis and Processing , pp. 175-198
    • Devi, L.A.1
  • 15
    • 0020008342 scopus 로고
    • Post-translational proteolysis in polypeptide hormone biosynthesis
    • DOCHERTY, K., and STEINER, D.F. (1982). Post-translational proteolysis in polypeptide hormone biosynthesis. Annu. Rev. Physiol. 44, 625-638.
    • (1982) Annu. Rev. Physiol. , vol.44 , pp. 625-638
    • Docherty, K.1    Steiner, D.F.2
  • 17
    • 0023664261 scopus 로고
    • Evidence for the involvement of metalloproteases in the acrosome reaction in sea urchin sperm
    • FARACH, H.A., MUNDY, D.I., STRITTMATTER, W.J., and LENNAZ, W.J. (1987). Evidence for the involvement of metalloproteases in the acrosome reaction in sea urchin sperm. J. Biol. Chem. 262, 5483-5487.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5483-5487
    • Farach, H.A.1    Mundy, D.I.2    Strittmatter, W.J.3    Lennaz, W.J.4
  • 18
    • 0001132432 scopus 로고
    • Methods for studying carboxypeptidase E
    • FRICKER, L.D. (1995). Methods for studying carboxypeptidase E. Methods Neurosci. 23, 237-250.
    • (1995) Methods Neurosci. , vol.23 , pp. 237-250
    • Fricker, L.D.1
  • 19
    • 0345234316 scopus 로고
    • Enzymes involved in the synthesis of opioid peptides
    • L.F. Tseng, ed. (Harwood Academic Press, Amsterdam)
    • FRICKER, L.D., and DEVI, L. (1995). Enzymes involved in the synthesis of opioid peptides. In Pharmacology of Opioid Peptides. L.F. Tseng, ed. (Harwood Academic Press, Amsterdam) pp. 87-107.
    • (1995) Pharmacology of Opioid Peptides , pp. 87-107
    • Fricker, L.D.1    Devi, L.2
  • 21
    • 0024505412 scopus 로고
    • Metalloprotease inhibitors block fast axonal transport
    • HAMMERSCHLAG, P, BOLEN, F.A., and STONE, G.C. (1989). Metalloprotease inhibitors block fast axonal transport. J. Neurochem. 52, 268-273.
    • (1989) J. Neurochem. , vol.52 , pp. 268-273
    • Hammerschlag, P.1    Bolen, F.A.2    Stone, G.C.3
  • 22
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • HOOPER, N. (1994). Families of zinc metalloproteases. FEBS Lett. 354, 1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.1
  • 23
    • 0029135124 scopus 로고
    • Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor
    • JEAN, F., BOUDREAULT, A., BASAK, A., SEIDAH, N.G., and LAZURE, C. (1995). Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor. J. Biol. Chem. 270, 19225-19231.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19225-19231
    • Jean, F.1    Boudreault, A.2    Basak, A.3    Seidah, N.G.4    Lazure, C.5
  • 24
    • 0024335103 scopus 로고
    • Metalloprotease inhibitors which block the differentiation of L6 inhibit insulin degradation by the endogenous insulin-degrading enzyme
    • KALYALAR, C., and WONG, W.T. (1989). Metalloprotease inhibitors which block the differentiation of L6 inhibit insulin degradation by the endogenous insulin-degrading enzyme. J. Biol. Chem. 264, 8928-8934.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8928-8934
    • Kalyalar, C.1    Wong, W.T.2
  • 26
    • 0020616958 scopus 로고
    • Translation of insulin-related polypeptides from messenger RNAs with tandemly reiterated copies of the ribosome binding site
    • KOZAK, M. (1983). Translation of insulin-related polypeptides from messenger RNAs with tandemly reiterated copies of the ribosome binding site. Cell 34, 971-978.
    • (1983) Cell , vol.34 , pp. 971-978
    • Kozak, M.1
  • 27
    • 0027452730 scopus 로고
    • Insulin-degrading enzyme is differentially expressed and developmentally regulated in various rat tissues
    • KUO, W-L., MONTAG, A.G., and ROSNER, M.R. (1993). Insulin-degrading enzyme is differentially expressed and developmentally regulated in various rat tissues. Endocrinology 132, 604-611.
    • (1993) Endocrinology , vol.132 , pp. 604-611
    • Kuo, W.-L.1    Montag, A.G.2    Rosner, M.R.3
  • 28
    • 0021846078 scopus 로고
    • Requirement for metalloendoprotease in exocytosis: Evidence in mast cells and adrenal chromaffin cells
    • MUNDY, D.I., and STRITTMATTER, W.J. (1985). Requirement for metalloendoprotease in exocytosis: evidence in mast cells and adrenal chromaffin cells. Cell 40, 645-656.
    • (1985) Cell , vol.40 , pp. 645-656
    • Mundy, D.I.1    Strittmatter, W.J.2
  • 29
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • NEEDLEHAM, S.B., and WUNSCH, C.D. (1970). A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48, 443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleham, S.B.1    Wunsch, C.D.2
  • 30
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • NIELSEN, H., ENGELBRECHT, J., BRUNAK, S., and VON HEIJNE, G. (1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 31
    • 0020824984 scopus 로고
    • A soluble metalloendopeptidase from rat brain: Purification of the enzyme and determination of specificity with synthetic and natural peptides
    • ORLOWSKI, M., MICHAUD, C., and CHU, T.G. (1983). A soluble metalloendopeptidase from rat brain: purification of the enzyme and determination of specificity with synthetic and natural peptides. Eur. J. Biochem. 135, 81-88.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 81-88
    • Orlowski, M.1    Michaud, C.2    Chu, T.G.3
  • 32
    • 0027092035 scopus 로고
    • Sequence analysis, tissue distribution, and expression of rat cathepsin S
    • PETANCESKA, S., and DEVI, L. (1992). Sequence analysis, tissue distribution, and expression of rat cathepsin S. J. Biol. Chem. 267, 26038-26043.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26038-26043
    • Petanceska, S.1    Devi, L.2
  • 34
    • 0021007899 scopus 로고
    • Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography
    • RELTON, J.M., GEE, N.S., MATSAS, R., TURNER, A.J., and KENNY, A.J. (1983). Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography. Biochem. J. 215, 519-523.
    • (1983) Biochem. J. , vol.215 , pp. 519-523
    • Relton, J.M.1    Gee, N.S.2    Matsas, R.3    Turner, A.J.4    Kenny, A.J.5
  • 36
    • 0023801330 scopus 로고
    • Evidence for involvement of metalloendoproteases in a step in sea urchin gamete fusion
    • ROE, J.L., FARACH, H.A., STRITTMATTER, W.J., and LENNARZ, W.J. (1988). Evidence for involvement of metalloendoproteases in a step in sea urchin gamete fusion. J. Cell Biol. 107, 539-544.
    • (1988) J. Cell Biol. , vol.107 , pp. 539-544
    • Roe, J.L.1    Farach, H.A.2    Strittmatter, W.J.3    Lennarz, W.J.4
  • 37
    • 0029843563 scopus 로고    scopus 로고
    • Identification of gamma-endorphin generating enzyme as insulin-degrading enzyme
    • SAFAVI, A., MILLER, B.C., COTTAM, L., and HERSH, L.B. (1996). Identification of gamma-endorphin generating enzyme as insulin-degrading enzyme. Biochemistry 35, 14318-14325.
    • (1996) Biochemistry , vol.35 , pp. 14318-14325
    • Safavi, A.1    Miller, B.C.2    Cottam, L.3    Hersh, L.B.4
  • 38
    • 0027404880 scopus 로고
    • Gene expression of prohormone and proprotein convertases in the rat CNS: A comparative in situ hybridization analysis
    • SCHAFER, M.K.-H., DAY, R., CULLINAN, W.E., CHRETIEN, M., SEIDAH, N., and WATSON, S.J. (1993). Gene expression of prohormone and proprotein convertases in the rat CNS: a comparative in situ hybridization analysis. J. Neurosci. 13, 1258-1279.
    • (1993) J. Neurosci. , vol.13 , pp. 1258-1279
    • Schafer, M.K.-H.1    Day, R.2    Cullinan, W.E.3    Chretien, M.4    Seidah, N.5    Watson, S.J.6
  • 39
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Paris
    • SEIDAH, N.G., CHRETIEN, M., and DAY, R. (1994). The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie (Paris) 76, 197-209.
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 40
    • 0028674393 scopus 로고
    • Pro-protein convertases of subtilisin/kexin family
    • SEIDAH, N.G., and CHRETIEN, M. (1994). Pro-protein convertases of subtilisin/kexin family. Methods Enzymol. 244, 185-188.
    • (1994) Methods Enzymol. , vol.244 , pp. 185-188
    • Seidah, N.G.1    Chretien, M.2
  • 41
    • 0004354257 scopus 로고
    • The biosynthesis of biologically active peptides: A perspective
    • L.D. Fricker, ed. (CRC Press, Boca Raton, FL)
    • STEINER, D.F. (1991). The biosynthesis of biologically active peptides: a perspective. In Peptide Biosynthesis and Processing. L.D. Fricker, ed. pp. 1-16. (CRC Press, Boca Raton, FL)
    • (1991) Peptide Biosynthesis and Processing , pp. 1-16
    • Steiner, D.F.1
  • 42
    • 0024204118 scopus 로고
    • Metalloprotease inhibitors block protein synthesis, intracellular transport, and cndocytosis in hepatoma cells
    • STROUS, C.J., VAN KERKHOF, P., DEKKER, J., and SCHWARTZ, A.L. (1988). Metalloprotease inhibitors block protein synthesis, intracellular transport, and cndocytosis in hepatoma cells. J. Biol. Chem. 263, 18197-18204.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18197-18204
    • Strous, C.J.1    Van Kerkhof, P.2    Dekker, J.3    Schwartz, A.L.4
  • 43
    • 0342827897 scopus 로고
    • Thimet oligopeptidase-a review of a thiol dependent metallo-endopeptidase also known as Pz-peptidase endopeptidase 24.15 and endo-oligopeptidase
    • TISLJAR, U. (1993). Thimet oligopeptidase-a review of a thiol dependent metallo-endopeptidase also known as Pz-peptidase endopeptidase 24.15 and endo-oligopeptidase. Biol. Chem. Hoppe Seyler 374, 91-100.
    • (1993) Biol. Chem. Hoppe Seyler , vol.374 , pp. 91-100
    • Tisljar, U.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.