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Volumn 161, Issue , 1998, Pages 129-141

Cellular carboxypeptidases

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; ANGIOTENSIN I; ARGININE; BRADYKININ; CARBOXYPEPTIDASE; CARBOXYPEPTIDASE C; ENDOTHELIN; ENZYME INHIBITOR; FORMYLMETHIONYLLEUCYLPHENYLALANINE; LYSINE; PEPTIDE HORMONE; PROLINE; PROLINE CARBOXYPEPTIDASE; SERINE; SUBSTANCE P;

EID: 0031886603     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1998.tb01577.x     Document Type: Review
Times cited : (143)

References (88)
  • 1
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen GS, Dixit VM. Caspases: Intracellular signaling by proteolysis. Cell 1997;91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 2
    • 0023690624 scopus 로고
    • Basic carboxypeptidases: Regulators of peptide hormone activity
    • Skidgel RA. Basic carboxypeptidases: regulators of peptide hormone activity. Trends Pharmacol Sci 1988;9:299-304.
    • (1988) Trends Pharmacol Sci , vol.9 , pp. 299-304
    • Skidgel, R.A.1
  • 3
    • 0027169659 scopus 로고
    • Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families
    • Tan F, Morris PW, Skidgel RA, Erdös EG. Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families. J Biol Chem 1993;268:16631-16638.
    • (1993) J Biol Chem , vol.268 , pp. 16631-16638
    • Tan, F.1    Morris, P.W.2    Skidgel, R.A.3    Erdös, E.G.4
  • 4
    • 0001995439 scopus 로고    scopus 로고
    • Structure and function of mammalian zinc carboxypeptidases
    • Hooper NM, ed. London: Taylor & Francis, Ltd.
    • Skidgel RA. Structure and function of mammalian zinc carboxypeptidases. In: Hooper NM, ed. Zinc Metalloproteases in Health and Disease. London: Taylor & Francis, Ltd. 1996. p. 241-283.
    • (1996) Zinc Metalloproteases in Health and Disease , pp. 241-283
    • Skidgel, R.A.1
  • 5
    • 84915548911 scopus 로고
    • Uber die Struktur der Protamine. I. Protaminase und die Produkte ihrer Enwirkung auf Clupein und Salmin
    • Waldschmidt-Leitz E, Ziegler F, Schäffner A, Weil L. Uber die Struktur der Protamine. I. Protaminase und die Produkte ihrer Enwirkung auf Clupein und Salmin. Z Physiol Chem 1931;197:219-236.
    • (1931) Z Physiol Chem , vol.197 , pp. 219-236
    • Waldschmidt-Leitz, E.1    Ziegler, F.2    Schäffner, A.3    Weil, L.4
  • 6
    • 0000771702 scopus 로고
    • Carboxypeptidase B.I. Purification of the zymogen and specificity of the enzyme
    • Folk JE, Gladner JA. Carboxypeptidase B.I. Purification of the zymogen and specificity of the enzyme. J Biol Chem 1958;231:379-391.
    • (1958) J Biol Chem , vol.231 , pp. 379-391
    • Folk, J.E.1    Gladner, J.A.2
  • 7
    • 0000077897 scopus 로고
    • An enzyme in human blood plasma that inactivates bradykinin and kallidins
    • Erdös EG, Sloane EM. An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem Pharmacol 1962;11:585-592.
    • (1962) Biochem Pharmacol , vol.11 , pp. 585-592
    • Erdös, E.G.1    Sloane, E.M.2
  • 8
    • 0016719394 scopus 로고
    • Plasma carboxypeptidase N, subunits and characteristics
    • Oshima G, Kato J, Erdös EG. Plasma carboxypeptidase N, subunits and characteristics. Arch Biochem Biophys 1975;170:132-138.
    • (1975) Arch Biochem Biophys , vol.170 , pp. 132-138
    • Oshima, G.1    Kato, J.2    Erdös, E.G.3
  • 9
    • 0017825437 scopus 로고
    • Human plasma carboxypeptidase N. Isolation and characterization
    • Plummer TH Jr, Hurwitz MY. Human plasma carboxypeptidase N. Isolation and characterization. J Biol Chem 1978;253:3907-3912.
    • (1978) J Biol Chem , vol.253 , pp. 3907-3912
    • Plummer Jr., T.H.1    Hurwitz, M.Y.2
  • 10
    • 0020174237 scopus 로고
    • Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I)
    • Levin Y, Skidgel RA, Erdös EG. Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I). Proc Natl Acad Sci USA 1982;79:4618-4622.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4618-4622
    • Levin, Y.1    Skidgel, R.A.2    Erdös, E.G.3
  • 11
    • 0021233813 scopus 로고
    • Purification of a human urinary carboxypeptidase (kininase) distinct from carboxypeptidase A, B, or N
    • Skidgel RA, Davis RM, Erdös EG. Purification of a human urinary carboxypeptidase (kininase) distinct from carboxypeptidase A, B, or N. Anal Biochem 1984;140:520-531.
    • (1984) Anal Biochem , vol.140 , pp. 520-531
    • Skidgel, R.A.1    Davis, R.M.2    Erdös, E.G.3
  • 12
    • 0021683271 scopus 로고
    • Hydrolysis of opioid hexapeptides by carboxypeptidase N. Presence of carboxypeptidase in cell membranes
    • Skidgel RA, Johnson AR, Erdös EG. Hydrolysis of opioid hexapeptides by carboxypeptidase N. Presence of carboxypeptidase in cell membranes. Biochem Pharmacol 1984;33:3471-3478.
    • (1984) Biochem Pharmacol , vol.33 , pp. 3471-3478
    • Skidgel, R.A.1    Johnson, A.R.2    Erdös, E.G.3
  • 13
    • 0021134710 scopus 로고
    • Enzymes in placental microvilli: Angiotensin I converting enzyme, angiotensinase A, carboxypeptidase, and neutral endopeptidase ("enkephalinase")
    • Johnson AR, Skidgel RA, Gafford JT, Erdös EG. Enzymes in placental microvilli: angiotensin I converting enzyme, angiotensinase A, carboxypeptidase, and neutral endopeptidase ("enkephalinase"). Peptides 1984;5:789-796.
    • (1984) Peptides , vol.5 , pp. 789-796
    • Johnson, A.R.1    Skidgel, R.A.2    Gafford, J.T.3    Erdös, E.G.4
  • 14
    • 0024552834 scopus 로고
    • Human carboxypeptidase M: Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones
    • Skidgel RA, Davis RM, Tan F. Human carboxypeptidase M: Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones. J Biol Chem 1989;264:2236-2241.
    • (1989) J Biol Chem , vol.264 , pp. 2236-2241
    • Skidgel, R.A.1    Davis, R.M.2    Tan, F.3
  • 15
    • 0024372894 scopus 로고
    • Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M: Comparison with carboxypeptidases A, B, H and N
    • Tan F, Chan SJ, Steiner DF, Schilling JW, Skidgel RA. Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M: Comparison with carboxypeptidases A, B, H and N. J Biol Chem 1989;264:13165-13170.
    • (1989) J Biol Chem , vol.264 , pp. 13165-13170
    • Tan, F.1    Chan, S.J.2    Steiner, D.F.3    Schilling, J.W.4    Skidgel, R.A.5
  • 17
    • 0026498950 scopus 로고
    • Carboxypeptidase M in brain and peripheral nerves
    • Nagae A, et al. Carboxypeptidase M in brain and peripheral nerves. J Neurochem 1992;59:2201-2212.
    • (1992) J Neurochem , vol.59 , pp. 2201-2212
    • Nagae, A.1
  • 18
    • 0031020560 scopus 로고    scopus 로고
    • Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B-virus binding protein
    • McGwire GB, Tan F, Michel B, Rehli M, Skidgel RA. Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B-virus binding protein. Life Sci 1997;60:715-724.
    • (1997) Life Sci , vol.60 , pp. 715-724
    • McGwire, G.B.1    Tan, F.2    Michel, B.3    Rehli, M.4    Skidgel, R.A.5
  • 19
    • 0028790290 scopus 로고
    • Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary
    • Song L, Fricker LD. Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. J Biol Chem 1995;270:25007-25013.
    • (1995) J Biol Chem , vol.270 , pp. 25007-25013
    • Song, L.1    Fricker, L.D.2
  • 20
    • 0029019153 scopus 로고
    • gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family
    • Kuroki K, Eng F, Ishikawa T, Turck C, Harada F, Ganem D. gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family. J Biol Chem 1995;270:15022-15028.
    • (1995) J Biol Chem , vol.270 , pp. 15022-15028
    • Kuroki, K.1    Eng, F.2    Ishikawa, T.3    Turck, C.4    Harada, F.5    Ganem, D.6
  • 21
    • 0030846523 scopus 로고    scopus 로고
    • Cloning and sequence analysis of cDNA encoding rat carboxypeptidase D
    • Xin X, et al. Cloning and sequence analysis of cDNA encoding rat carboxypeptidase D. DNA Cell Biol 1997;16:897-909.
    • (1997) DNA Cell Biol , vol.16 , pp. 897-909
    • Xin, X.1
  • 22
    • 0030713420 scopus 로고    scopus 로고
    • The sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains
    • Tan F, Rehli M, Krause SW, Skidgel RA. The sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains. Biochem J 1997;327:81-87.
    • (1997) Biochem J , vol.327 , pp. 81-87
    • Tan, F.1    Rehli, M.2    Krause, S.W.3    Skidgel, R.A.4
  • 23
    • 0028862371 scopus 로고
    • A eukaryotic transcriptional repressor with carboxypeptidase activity
    • He G-P, Muise A, Li AW, Ro H-S. A eukaryotic transcriptional repressor with carboxypeptidase activity. Nature 1995;378:92-96
    • (1995) Nature , vol.378 , pp. 92-96
    • He, G.-P.1    Muise, A.2    Li, A.W.3    Ro, H.-S.4
  • 24
    • 0030888061 scopus 로고    scopus 로고
    • Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase
    • Song L, Fricker LD. Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase. J Biol Chem 1997;272:10543-10550.
    • (1997) J Biol Chem , vol.272 , pp. 10543-10550
    • Song, L.1    Fricker, L.D.2
  • 25
    • 0014434136 scopus 로고
    • New enzymatic route for the inactivation of angiotensin
    • Yang HYT, Erdös EG, Chiang TS. New enzymatic route for the inactivation of angiotensin. Nature 1968;218:1224-1226.
    • (1968) Nature , vol.218 , pp. 1224-1226
    • Yang, H.Y.T.1    Erdös, E.G.2    Chiang, T.S.3
  • 26
    • 0019515695 scopus 로고
    • Prolylcarboxypeptidase (angiotensinase C) in human cultured cells
    • Kumamoto K, Stewart TA, Johnson AR, Erdos EG. Prolylcarboxypeptidase (angiotensinase C) in human cultured cells. J Clin Invest 1981;67:210-215.
    • (1981) J Clin Invest , vol.67 , pp. 210-215
    • Kumamoto, K.1    Stewart, T.A.2    Johnson, A.R.3    Erdos, E.G.4
  • 27
    • 0019771373 scopus 로고
    • Rapid radioassay for prolylcarboxypeptidase (angiotensinase C)
    • Skidgel RA, Wickstrom E, Kumamoto K. Erdös EG. Rapid radioassay for prolylcarboxypeptidase (angiotensinase C). Anal Biochem 1981;118:113-119.
    • (1981) Anal Biochem , vol.118 , pp. 113-119
    • Skidgel, R.A.1    Wickstrom, E.2    Kumamoto, K.3    Erdös, E.G.4
  • 28
    • 0029352046 scopus 로고
    • Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages
    • Jackman HL, et al. Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages. Am J Respir Cell Mol Biol 1995;13:196-204.
    • (1995) Am J Respir Cell Mol Biol , vol.13 , pp. 196-204
    • Jackman, H.L.1
  • 29
    • 0025340195 scopus 로고
    • A peptidase in human platelets that deamidates tachykinins: Probable identity with the lysosomal "protective protein."
    • Jackman HL, et al. A peptidase in human platelets that deamidates tachykinins: Probable identity with the lysosomal "protective protein." J Biol Chem 1990;265:11265-11272.
    • (1990) J Biol Chem , vol.265 , pp. 11265-11272
    • Jackman, H.L.1
  • 30
    • 0023783875 scopus 로고
    • Expression of cDNA encoding the human "protective protein" associated with lysosomal β-galactosidase and neuraminidase: Homology to yeast proteases
    • Galjart NJ, et al. Expression of cDNA encoding the human "protective protein" associated with lysosomal β-galactosidase and neuraminidase: Homology to yeast proteases. Cell 1988;54:755-764.
    • (1988) Cell , vol.54 , pp. 755-764
    • Galjart, N.J.1
  • 32
    • 0028053544 scopus 로고
    • Dominant chymotrypsin-like esterase activity in human lymphocyte granules is mediated by the serine carboxypeptidase called cathepsin A-like protective protein
    • Hanna WL, Turbov JM, Jackman HL, Tan F, Froelich CJ. Dominant chymotrypsin-like esterase activity in human lymphocyte granules is mediated by the serine carboxypeptidase called cathepsin A-like protective protein. J Immunol 1994;153:4663-4672.
    • (1994) J Immunol , vol.153 , pp. 4663-4672
    • Hanna, W.L.1    Turbov, J.M.2    Jackman, H.L.3    Tan, F.4    Froelich, C.J.5
  • 33
    • 0025024253 scopus 로고
    • Carboxypeptidase M in cultured Madin-Darby canine kidney (MDCK) cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor
    • Deddish PA, Skidgel RA, Kriho VB, Li X-Y, Becker RP, Erdös EG. Carboxypeptidase M in cultured Madin-Darby canine kidney (MDCK) cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor. J Biol Chem 1990;265:15083-15089.
    • (1990) J Biol Chem , vol.265 , pp. 15083-15089
    • Deddish, P.A.1    Skidgel, R.A.2    Kriho, V.B.3    Li, X.-Y.4    Becker, R.P.5    Erdös, E.G.6
  • 35
    • 0029934105 scopus 로고    scopus 로고
    • Membrane anchoring and release of carboxypeptidase M: Implications for extracellular hydrolysis of peptide hormones
    • Skidgel RA, McGwire GB, Li X-Y. Membrane anchoring and release of carboxypeptidase M: Implications for extracellular hydrolysis of peptide hormones. Immunopharmacology 1996;32:48-52.
    • (1996) Immunopharmacology , vol.32 , pp. 48-52
    • Skidgel, R.A.1    McGwire, G.B.2    Li, X.-Y.3
  • 36
    • 0028823576 scopus 로고
    • Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15
    • Kas K, Schoenmakers EFPM, Van de Ven WJM. Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15. Genomics 1995;30:403-405.
    • (1995) Genomics , vol.30 , pp. 403-405
    • Kas, K.1    Schoenmakers, E.F.P.M.2    Van De Ven, W.J.M.3
  • 37
    • 0029830745 scopus 로고    scopus 로고
    • Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D
    • Song L, Fricker LD. Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D. J Biol Chem 1996;271:28884-28889.
    • (1996) J Biol Chem , vol.271 , pp. 28884-28889
    • Song, L.1    Fricker, L.D.2
  • 38
    • 0000401180 scopus 로고
    • Biochemistry of angiotensin converting enzyme
    • Robertson JIS, Nicholls MG, eds. London: Gower Medical Publishing
    • Skidgel RA, Erdös EG. Biochemistry of angiotensin converting enzyme. In: Robertson JIS, Nicholls MG, eds. The Renin Angiotensin System. Vol 1. London: Gower Medical Publishing;1993. p.10.1-10.10.
    • (1993) The Renin Angiotensin System , vol.1
    • Skidgel, R.A.1    Erdös, E.G.2
  • 39
    • 0028271899 scopus 로고
    • Molecular cloning, structure, and chromosomal localization of the human inducible nitric oxide synthase gene
    • Chartrain NA, et al. Molecular cloning, structure, and chromosomal localization of the human inducible nitric oxide synthase gene. J Biol Chem 1994;269:6765-6772.
    • (1994) J Biol Chem , vol.269 , pp. 6765-6772
    • Chartrain, N.A.1
  • 41
    • 0018126802 scopus 로고
    • Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney
    • Odya CE, Marinkovic D, Hammon KJ, Stewart TA, Erdös EG. Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney. J Biol Chem 1978;253:5927-5931.
    • (1978) J Biol Chem , vol.253 , pp. 5927-5931
    • Odya, C.E.1    Marinkovic, D.2    Hammon, K.J.3    Stewart, T.A.4    Erdös, E.G.5
  • 42
    • 17344371202 scopus 로고    scopus 로고
    • URL=http://inhouse.ncbi.nlm.nih.gov/cgi-bin/UniGene/clust?ORG=Hs&CID= 75693
  • 43
    • 0028786552 scopus 로고
    • Lysosomal protective protein/cathepsin A. Role of the "linker" domain in catalytic activation
    • Bonten EJ, Galjart NJ, Willemsen R, Usmany M, Vlak JM, d'Azzo A. Lysosomal protective protein/cathepsin A. Role of the "linker" domain in catalytic activation. J Biol Chem 1995;270:26441-26445.
    • (1995) J Biol Chem , vol.270 , pp. 26441-26445
    • Bonten, E.J.1    Galjart, N.J.2    Willemsen, R.3    Usmany, M.4    Vlak, J.M.5    D'Azzo, A.6
  • 44
  • 45
    • 0025366352 scopus 로고
    • Structure of the lysosomal neuraminidase-β-galactosidase-carboxypeptidase multienzymic complex
    • Potier M, Michaud L, Tranchemontagne J, Thauvette L. Structure of the lysosomal neuraminidase-β-galactosidase-carboxypeptidase multienzymic complex. Biochem J 1990;267:197-202.
    • (1990) Biochem J , vol.267 , pp. 197-202
    • Potier, M.1    Michaud, L.2    Tranchemontagne, J.3    Thauvette, L.4
  • 46
    • 0026046389 scopus 로고
    • The gene encoding human protective protein (PPGB) is on chromosome 20
    • Wiegant J, Galjart NJ, Raap AK, d'Azzo A. The gene encoding human protective protein (PPGB) is on chromosome 20. Genomics 1991;10:345-349.
    • (1991) Genomics , vol.10 , pp. 345-349
    • Wiegant, J.1    Galjart, N.J.2    Raap, A.K.3    D'Azzo, A.4
  • 47
    • 0024473762 scopus 로고
    • 2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)
    • 2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase). Biochem J 1989;261:289-291.
    • (1989) Biochem J , vol.261 , pp. 289-291
    • Deddish, P.A.1    Skidgel, R.A.2    Erdös, E.G.3
  • 48
    • 85013504002 scopus 로고
    • Assays for arginine/lysine carboxypeptidases: Carboxypeptidase H (E; enkephalin convertase);M and N
    • Conn PM, ed. Orlando: Academic Press
    • Skidgel RA. Assays for arginine/lysine carboxypeptidases: carboxypeptidase H (E; enkephalin convertase);M and N. In: Conn PM, ed. Methods in Neurosciences: Peptide Technology. Vol 6. Orlando: Academic Press;1991. p. 373-385.
    • (1991) Methods in Neurosciences: Peptide Technology , vol.6 , pp. 373-385
    • Skidgel, R.A.1
  • 49
    • 0019890965 scopus 로고
    • A potent mercapto bi-product analogue inhibitor for human carboxypeptidase N
    • Plummer TH Jr, Ryan TJ. A potent mercapto bi-product analogue inhibitor for human carboxypeptidase N. Biochem Biophys Res Commun 1981;98: 448-454.
    • (1981) Biochem Biophys Res Commun , vol.98 , pp. 448-454
    • Plummer Jr., T.H.1    Ryan, T.J.2
  • 53
    • 0026634828 scopus 로고
    • A soluble protease identified from rat kidney degrades endothelin-1 but not proendothelin-1
    • Deng Y, Martin LL, DelGrande D, Jeng AY. A soluble protease identified from rat kidney degrades endothelin-1 but not proendothelin-1. J Biochem 1992;112:168-172.
    • (1992) J Biochem , vol.112 , pp. 168-172
    • Deng, Y.1    Martin, L.L.2    DelGrande, D.3    Jeng, A.Y.4
  • 54
    • 0028008542 scopus 로고
    • Purification and characterization of an endothelin degradation enzyme from rat kidney
    • Deng AY, Martin LL, Balwierczak JL, Jeng AY. Purification and characterization of an endothelin degradation enzyme from rat kidney. J Biochem 1994;115:120-125.
    • (1994) J Biochem , vol.115 , pp. 120-125
    • Deng, A.Y.1    Martin, L.L.2    Balwierczak, J.L.3    Jeng, A.Y.4
  • 55
    • 0028833064 scopus 로고
    • Degradation of endothelin-1 by extracts of rat lung, kidney, and liver
    • Sirviö M-L, Saijonmaa O, Metsärinne K, Fyhrquist F. Degradation of endothelin-1 by extracts of rat lung, kidney, and liver. Regul Pept 1995;55:219-225.
    • (1995) Regul Pept , vol.55 , pp. 219-225
    • Sirviö, M.-L.1    Saijonmaa, O.2    Metsärinne, K.3    Fyhrquist, F.4
  • 56
    • 0028897406 scopus 로고
    • Protective protein as an endogenous endothelin degradation enzyme in human tissues
    • Itoh K, Kase R, Shimmoto M, Satake A, Sakuraba H, Suzuki Y. Protective protein as an endogenous endothelin degradation enzyme in human tissues. J Biol Chem 1995;270:515-518.
    • (1995) J Biol Chem , vol.270 , pp. 515-518
    • Itoh, K.1    Kase, R.2    Shimmoto, M.3    Satake, A.4    Sakuraba, H.5    Suzuki, Y.6
  • 57
    • 0028295258 scopus 로고
    • A cell surface protein that binds avian hepatitis B virus particles
    • Kuroki K, Cheung R, Marion PL, Ganem D. A cell surface protein that binds avian hepatitis B virus particles. J Virol 1994;68:2091-2096.
    • (1994) J Virol , vol.68 , pp. 2091-2096
    • Kuroki, K.1    Cheung, R.2    Marion, P.L.3    Ganem, D.4
  • 60
    • 0029052676 scopus 로고
    • Distribution of carboxypeptidase-M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13
    • de Saint-Vis B, et al. Distribution of carboxypeptidase-M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13. Blood 1995;86:1098-1105.
    • (1995) Blood , vol.86 , pp. 1098-1105
    • De Saint-Vis, B.1
  • 61
    • 0029077807 scopus 로고
    • Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation
    • Rehli M, Krause SW, Kreutz M, Andreesen R. Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. J Biol Chem 1995;270:15644-15649.
    • (1995) J Biol Chem , vol.270 , pp. 15644-15649
    • Rehli, M.1    Krause, S.W.2    Kreutz, M.3    Andreesen, R.4
  • 62
    • 0025829356 scopus 로고
    • Angiotensin carboxypeptidase activity in urine from normal subjects and patients with kidney damage
    • Miller JJ, Changaris DG, Levy RS. Angiotensin carboxypeptidase activity in urine from normal subjects and patients with kidney damage. Life Sci 1991;48:1529-1535.
    • (1991) Life Sci , vol.48 , pp. 1529-1535
    • Miller, J.J.1    Changaris, D.G.2    Levy, R.S.3
  • 63
    • 0025971043 scopus 로고
    • Metabolism of substance P and bradykinin by human neutrophils
    • Skidgel RA, Jackman HL, Erdös EG. Metabolism of substance P and bradykinin by human neutrophils. Biochem Pharmacol 1991;41:1335-1344.
    • (1991) Biochem Pharmacol , vol.41 , pp. 1335-1344
    • Skidgel, R.A.1    Jackman, H.L.2    Erdös, E.G.3
  • 64
    • 0008490902 scopus 로고    scopus 로고
    • Biological roles of the non-integrin elastin/laminin receptor
    • Hinek A. Biological roles of the non-integrin elastin/laminin receptor. Biol Chem 1996;377:471-480.
    • (1996) Biol Chem , vol.377 , pp. 471-480
    • Hinek, A.1
  • 65
    • 0025248449 scopus 로고
    • Mouse "protective protein". cDNA cloning, sequence comparison, and expression
    • Galjart NJ, Gillemans N, Meijer D. d'Azzo A. Mouse "protective protein". cDNA cloning, sequence comparison, and expression. J Biol Chem 1990;265:4678-4684.
    • (1990) J Biol Chem , vol.265 , pp. 4678-4684
    • Galjart, N.J.1    Gillemans, N.2    Meijer, D.3    D'Azzo, A.4
  • 66
    • 17344369724 scopus 로고    scopus 로고
    • http://inhouse.ncbi.nlm.nih.gov/cgi-bin/UniGene/clust?ORG=Hs&CID=985
  • 67
    • 0000847126 scopus 로고
    • Kinins, paracrine hormones, in the regulation of blood flow, renal function, and blood pressure
    • Laragh JH, Brenner BM, Kaplan NM, eds. New York: Raven Press
    • Carretero OA, Scicli AG. Kinins, paracrine hormones, in the regulation of blood flow, renal function, and blood pressure. In: Laragh JH, Brenner BM, Kaplan NM, eds. Endocrine Mechanisms in Hypertension. New York: Raven Press;1989. p. 219-239.
    • (1989) Endocrine Mechanisms in Hypertension , pp. 219-239
    • Carretero, O.A.1    Scicli, A.G.2
  • 68
    • 0027051024 scopus 로고
    • Bradykinin degrading enzymes: Structure, function, distribution, and potential roles in cardiovascular pharmacology
    • Skidgel RA. Bradykinin degrading enzymes: Structure, function, distribution, and potential roles in cardiovascular pharmacology. J Cardiovasc Pharmacol 1992;20 (Suppl 9): S4-S9.
    • (1992) J Cardiovasc Pharmacol , vol.20 , Issue.9 SUPPL.
    • Skidgel, R.A.1
  • 69
    • 0026556434 scopus 로고
    • Bioregulation of kinins: Kallikreins, kininogens, and kininases
    • Bhoola KD, Figueroa CD, Worthy K. Bioregulation of kinins: Kallikreins, kininogens, and kininases. Pharmacol Rev 1992;44:1-80.
    • (1992) Pharmacol Rev , vol.44 , pp. 1-80
    • Bhoola, K.D.1    Figueroa, C.D.2    Worthy, K.3
  • 73
    • 0024564728 scopus 로고
    • Bradykinin stimulates tumor necrosis factor and interleukin-1 release from macrophages
    • Tiffany CW, Burch RM. Bradykinin stimulates tumor necrosis factor and interleukin-1 release from macrophages. FEBS Lett 1989;247:189-192.
    • (1989) FEBS Lett , vol.247 , pp. 189-192
    • Tiffany, C.W.1    Burch, R.M.2
  • 74
    • 17344368564 scopus 로고
    • Bradykinin stimulates lymphocyte movement in vitro
    • Abstract
    • MacFadden RG, Vickers K. Bradykinin stimulates lymphocyte movement in vitro. FASEB J 1988;2:1179 (Abstract).
    • (1988) FASEB J , vol.2 , pp. 1179
    • MacFadden, R.G.1    Vickers, K.2
  • 77
    • 0026029849 scopus 로고
    • Structure and biosynthesis of nerve growth factor
    • Fahnestock M. Structure and biosynthesis of nerve growth factor. Curr Top Microbiol Immunol 1991;165: 1-26.
    • (1991) Curr Top Microbiol Immunol , vol.165 , pp. 1-26
    • Fahnestock, M.1
  • 78
    • 0017229758 scopus 로고
    • Modification of the epidermal growth factor affecting the stability of its high molecular weight complex
    • Server AC, Sutter A, Shooter EM. Modification of the epidermal growth factor affecting the stability of its high molecular weight complex. J Biol Chem 1976;251:1188-1196.
    • (1976) J Biol Chem , vol.251 , pp. 1188-1196
    • Server, A.C.1    Sutter, A.2    Shooter, E.M.3
  • 79
    • 0024387018 scopus 로고
    • Down-regulation and inactivation of neutral endopeptidase 24.11 (enkephalinase) in human neutrophils
    • Erdös EG, Wagner BA, Harbury CB, Painter RG, Skidgel RA, Fa X-G. Down-regulation and inactivation of neutral endopeptidase 24.11 (enkephalinase) in human neutrophils. J Biol Chem 1989;264:14519-14523.
    • (1989) J Biol Chem , vol.264 , pp. 14519-14523
    • Erdös, E.G.1    Wagner, B.A.2    Harbury, C.B.3    Painter, R.G.4    Skidgel, R.A.5    Fa, X.-G.6
  • 80
    • 0026531241 scopus 로고
    • 1 MF-2 smooth muscle cells process internalized bradykinin via multiple degradative pathways
    • 1 MF-2 smooth muscle cells process internalized bradykinin via multiple degradative pathways. J Biol Chem 1992;267:303-309.
    • (1992) J Biol Chem , vol.267 , pp. 303-309
    • Munoz, C.M.1    Leeb-Lundberg, L.M.F.2
  • 82
    • 0029128516 scopus 로고
    • Metabolism of the anticancer peptide:H-Arg-D-Trp-NmePhe-D-Trp-Leu-Met-NHZ
    • Jones DA, et al. Metabolism of the anticancer peptide:H-Arg-D-Trp-NmePhe-D-Trp-Leu-Met-NHZ. Peptides 1995;16:777-783.
    • (1995) Peptides , vol.16 , pp. 777-783
    • Jones, D.A.1
  • 85
    • 0028560423 scopus 로고
    • Angiotensin(1-7) is an antagonist at the type 1 angiotensin II receptor
    • Mahon JM, Carr RD, Nicol AK, Henderson IW. Angiotensin(1-7) is an antagonist at the type 1 angiotensin II receptor. J Hypertens 1994;12:1377-1381.
    • (1994) J Hypertens , vol.12 , pp. 1377-1381
    • Mahon, J.M.1    Carr, R.D.2    Nicol, A.K.3    Henderson, I.W.4
  • 86
    • 0031034312 scopus 로고    scopus 로고
    • Angiotensin-(1-7) augments bradykinin-induced vasodilation by competing with ACE and releasing nitric oxide
    • Li P, Chappell MC, Ferrario CM, Brosnihan KB. Angiotensin-(1-7) augments bradykinin-induced vasodilation by competing with ACE and releasing nitric oxide. Hypertension 1997;29(Pt 2):394-400.
    • (1997) Hypertension , vol.29 , Issue.2 PT , pp. 394-400
    • Li, P.1    Chappell, M.C.2    Ferrario, C.M.3    Brosnihan, K.B.4
  • 87
    • 0031954590 scopus 로고    scopus 로고
    • N-domain specific substrate and C-domain inhibitors of angiotensin converting enzyme: Angiotensin-(1-7) and keto-ACE
    • In press
    • Deddish PA, Marcic B, Jackman HL, Wang H-Z, Skidgel RA, Erdös EG. N-domain specific substrate and C-domain inhibitors of angiotensin converting enzyme: Angiotensin-(1-7) and keto-ACE. Hypertension (In press).
    • Hypertension
    • Deddish, P.A.1    Marcic, B.2    Jackman, H.L.3    Wang, H.-Z.4    Skidgel, R.A.5    Erdös, E.G.6
  • 88
    • 0015140661 scopus 로고
    • Prolylcarboxypeptidase in biological fluids
    • Hinshaw LB, Cox BG, eds. New York: Plenum Publishing Co.
    • Sorrells K, Erdös EG. Prolylcarboxypeptidase in biological fluids. In: Hinshaw LB, Cox BG, eds. The Fundamental Mechanisms of Shock. New York: Plenum Publishing Co. 1972. p. 393-397.
    • (1972) The Fundamental Mechanisms of Shock , pp. 393-397
    • Sorrells, K.1    Erdös, E.G.2


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