메뉴 건너뛰기




Volumn 150, Issue 8, 2009, Pages 3547-3557

Cathepsin L colocalizes with chromogranin A in chromaffin vesicles to generate active peptides

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOLAMINE; CATHEPSIN L; CHROMOGRANIN A; GLYCINE; LEUCINE; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; NICOTINE; PROLINE; PROPROTEIN CONVERTASE 1; PROPROTEIN CONVERTASE 2; SERINE;

EID: 67651174537     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2008-1613     Document Type: Article
Times cited : (61)

References (63)
  • 1
    • 0026680263 scopus 로고
    • The chromogranins A and B: The first 25 years and future perspectives
    • Winkler H, Fischer-Colbrie R 1992 The chromogranins A and B: the first 25 years and future perspectives. Neuroscience 49:497-528
    • (1992) Neuroscience , vol.49 , pp. 497-528
    • Winkler, H.1    Fischer-Colbrie, R.2
  • 2
    • 0037456743 scopus 로고    scopus 로고
    • Mechanisms of disease: The chromogranin-secretogranin family
    • Taupenot L, Harper KL, O'Connor DT 2003 Mechanisms of disease: the chromogranin-secretogranin family. N Engl J Med 348:1134-1149
    • (2003) N Engl J Med , vol.348 , pp. 1134-1149
    • Taupenot, L.1    Harper, K.L.2    O'Connor, D.T.3
  • 4
    • 0025253581 scopus 로고    scopus 로고
    • Takiyyuddin MA, Cervenka JH, Hsiao RJ, Barbosa JA, Parmer RJ, O'Connor DT 1990 Chromogranin A. Storage and release in hypertension. Hypertension 15:237-246
    • Takiyyuddin MA, Cervenka JH, Hsiao RJ, Barbosa JA, Parmer RJ, O'Connor DT 1990 Chromogranin A. Storage and release in hypertension. Hypertension 15:237-246
  • 6
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly RB 1985 Pathways of protein secretion in eukaryotes. Science 230:25-32
    • (1985) Science , vol.230 , pp. 25-32
    • Kelly, R.B.1
  • 7
    • 0035943417 scopus 로고    scopus 로고
    • Chromogranin A, an "on/off" switch controlling dense-core secretory granule biogenesis
    • Kim T, Tao-Cheng JH, Eiden LE, Loh YP 2001 Chromogranin A, an "on/off" switch controlling dense-core secretory granule biogenesis. Cell 106:499-509
    • (2001) Cell , vol.106 , pp. 499-509
    • Kim, T.1    Tao-Cheng, J.H.2    Eiden, L.E.3    Loh, Y.P.4
  • 8
    • 23044488803 scopus 로고    scopus 로고
    • Chromogranin A deficiency in transgenic mice leads to aberrant chromaffin granule biogenesis
    • Kim T, Zhang CF, Sun Z, Wu H, Loh YP 2005 Chromogranin A deficiency in transgenic mice leads to aberrant chromaffin granule biogenesis. J Neurosci 25:6958-6961
    • (2005) J Neurosci , vol.25 , pp. 6958-6961
    • Kim, T.1    Zhang, C.F.2    Sun, Z.3    Wu, H.4    Loh, Y.P.5
  • 9
    • 33846029499 scopus 로고    scopus 로고
    • Secretory granule biogenesis in sympathoadrenal cells: Identification of a granulogenic determinant in the secretory prohormone chromogranin A
    • Courel M, Rodemer C, Nguyen ST, Pance A, Jackson AP, O'connor DT, Taupenot L 2006 Secretory granule biogenesis in sympathoadrenal cells: identification of a granulogenic determinant in the secretory prohormone chromogranin A. J Biol Chem 281:38038-38051
    • (2006) J Biol Chem , vol.281 , pp. 38038-38051
    • Courel, M.1    Rodemer, C.2    Nguyen, S.T.3    Pance, A.4    Jackson, A.P.5    O'connor, D.T.6    Taupenot, L.7
  • 11
    • 0037024637 scopus 로고    scopus 로고
    • Studies of the dysglycemic peptide, pancreastatin, using a human forearm model
    • Cadman PE, Rao F, Mahata SK, O'Connor DT 2002 Studies of the dysglycemic peptide, pancreastatin, using a human forearm model. Ann NY Acad Sci 971:528-529
    • (2002) Ann NY Acad Sci , vol.971 , pp. 528-529
    • Cadman, P.E.1    Rao, F.2    Mahata, S.K.3    O'Connor, D.T.4
  • 12
    • 0027302614 scopus 로고
    • Vasostatins, comprising the N-terminal domain of chromogranin A, suppress tension in isolated human blood vessel segments
    • Aardal S, Helle KB, Elsayed S, Reed RK, Serck-Hanssen G 1993 Vasostatins, comprising the N-terminal domain of chromogranin A, suppress tension in isolated human blood vessel segments. J Neuroendocrinol 5:405-412
    • (1993) J Neuroendocrinol , vol.5 , pp. 405-412
    • Aardal, S.1    Helle, K.B.2    Elsayed, S.3    Reed, R.K.4    Serck-Hanssen, G.5
  • 13
    • 0030803637 scopus 로고    scopus 로고
    • Novel autocrine feedback control of catecholamine release. A discrete chromogranin A fragment is a noncompetitive nicotinic cholinergic antagonist
    • Mahata SK, O'Connor DT, Mahata M, Yoo SH, Taupenot L, Wu H, Gill BM, Parmer RJ 1997 Novel autocrine feedback control of catecholamine release. A discrete chromogranin A fragment is a noncompetitive nicotinic cholinergic antagonist. J Clin Invest 100:1623-1633
    • (1997) J Clin Invest , vol.100 , pp. 1623-1633
    • Mahata, S.K.1    O'Connor, D.T.2    Mahata, M.3    Yoo, S.H.4    Taupenot, L.5    Wu, H.6    Gill, B.M.7    Parmer, R.J.8
  • 15
    • 0033768870 scopus 로고    scopus 로고
    • Primary structure and function of the catecholamine release inhibitory peptide catestatin (chromogranin A344-364): Identification of amino acid residues crucial for activity
    • Mahata SK, Mahata M, Wakade AR, O'Connor DT 2000 Primary structure and function of the catecholamine release inhibitory peptide catestatin (chromogranin A344-364): Identification of amino acid residues crucial for activity. Mol Endocrinol 14:1525-1535
    • (2000) Mol Endocrinol , vol.14 , pp. 1525-1535
    • Mahata, S.K.1    Mahata, M.2    Wakade, A.R.3    O'Connor, D.T.4
  • 16
    • 4344600532 scopus 로고    scopus 로고
    • Catestatin - the catecholamine release inhibitory peptide: A structural and functional overview
    • Mahata SK 2004 Catestatin - the catecholamine release inhibitory peptide: a structural and functional overview. Curr Med Chem Immun Endocr Metab Agents 4:221-234
    • (2004) Curr Med Chem Immun Endocr Metab Agents , vol.4 , pp. 221-234
    • Mahata, S.K.1
  • 18
    • 0036628754 scopus 로고    scopus 로고
    • Early decline in the catecholamine release-inhibitory peptide catestatin in humans at genetic risk of hypertension
    • O'Connor DT, Kailasam MT, Kennedy BP, Ziegler MG, Yanaihara N, Parmer RJ 2002 Early decline in the catecholamine release-inhibitory peptide catestatin in humans at genetic risk of hypertension. J Hypertens 20:1335-1345
    • (2002) J Hypertens , vol.20 , pp. 1335-1345
    • O'Connor, D.T.1    Kailasam, M.T.2    Kennedy, B.P.3    Ziegler, M.G.4    Yanaihara, N.5    Parmer, R.J.6
  • 21
    • 0028968096 scopus 로고
    • Processing of secretogranin II by prohormone convertases: Importance of PC1 in generation of secretoneurin
    • Hoflehner J, Eder U, Laslop A, Seidah NG, Fischer-Colbrie R, Winkler H 1995 Processing of secretogranin II by prohormone convertases: importance of PC1 in generation of secretoneurin. FEBS Lett 360:294-298
    • (1995) FEBS Lett , vol.360 , pp. 294-298
    • Hoflehner, J.1    Eder, U.2    Laslop, A.3    Seidah, N.G.4    Fischer-Colbrie, R.5    Winkler, H.6
  • 22
    • 0030016321 scopus 로고    scopus 로고
    • Chromogranin A processing and secretion: Specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway
    • Eskeland NL, Zhou A, Dinh TQ, Wu H, Parmer RJ, Mains RE, O'Connor DT 1996 Chromogranin A processing and secretion: specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway. J Clin Invest 98:148-156
    • (1996) J Clin Invest , vol.98 , pp. 148-156
    • Eskeland, N.L.1    Zhou, A.2    Dinh, T.Q.3    Wu, H.4    Parmer, R.J.5    Mains, R.E.6    O'Connor, D.T.7
  • 23
    • 0032524834 scopus 로고    scopus 로고
    • Precursor convertases: An evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins
    • Seidah NG, Day R, Marcinkiewicz M, Chrétien M 1998 Precursor convertases: an evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins. Ann NY Acad Sci 839:9-24
    • (1998) Ann NY Acad Sci , vol.839 , pp. 9-24
    • Seidah, N.G.1    Day, R.2    Marcinkiewicz, M.3    Chrétien, M.4
  • 25
    • 0038394566 scopus 로고    scopus 로고
    • Precursor convertases in the secretory pathway, cytosol and extracellular milieu
    • Seidah NG, Prat A 2002 Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem 38:79-94
    • (2002) Essays Biochem , vol.38 , pp. 79-94
    • Seidah, N.G.1    Prat, A.2
  • 26
    • 0037471347 scopus 로고    scopus 로고
    • Proteolytic processing of chromogranin A by the prohormone convertase PC2
    • Doblinger A, Becker A, Seidah NG, Laslop A 2003 Proteolytic processing of chromogranin A by the prohormone convertase PC2. Regul Pept 111:111-116
    • (2003) Regul Pept , vol.111 , pp. 111-116
    • Doblinger, A.1    Becker, A.2    Seidah, N.G.3    Laslop, A.4
  • 29
    • 0035816635 scopus 로고    scopus 로고
    • Proteolytic cleavage of chromogranin A (CgA) by plasmin: Selective liberation of a specific bioactive CgA fragment that regulates catecholamine release
    • Jiang Q, Taupenot L, Mahata SK, Mahata M, O'Connor DT, Miles LA, Parmer RJ 2001 Proteolytic cleavage of chromogranin A (CgA) by plasmin: selective liberation of a specific bioactive CgA fragment that regulates catecholamine release. J Biol Chem 276:25022-25029
    • (2001) J Biol Chem , vol.276 , pp. 25022-25029
    • Jiang, Q.1    Taupenot, L.2    Mahata, S.K.3    Mahata, M.4    O'Connor, D.T.5    Miles, L.A.6    Parmer, R.J.7
  • 30
    • 38549159125 scopus 로고    scopus 로고
    • Proteolytic cleavage of human chromogranin a containing naturally occurring catestatin variants: Differential processing at catestatin region by plasmin
    • Biswas N, Vaingankar SM, Mahata M, Das M, Gayen JR, Taupenot L, Torpey JW, O'Connor DT, Mahata SK 2008 Proteolytic cleavage of human chromogranin a containing naturally occurring catestatin variants: differential processing at catestatin region by plasmin. Endocrinology 149:749-757
    • (2008) Endocrinology , vol.149 , pp. 749-757
    • Biswas, N.1    Vaingankar, S.M.2    Mahata, M.3    Das, M.4    Gayen, J.R.5    Taupenot, L.6    Torpey, J.W.7    O'Connor, D.T.8    Mahata, S.K.9
  • 32
    • 34248177365 scopus 로고    scopus 로고
    • Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion
    • Hwang SR, Garza C, Mosier C, Toneff T, Wunderlich E, Goldsmith P, Hook V 2007 Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion. J Biol Chem 282:9556-9563
    • (2007) J Biol Chem , vol.282 , pp. 9556-9563
    • Hwang, S.R.1    Garza, C.2    Mosier, C.3    Toneff, T.4    Wunderlich, E.5    Goldsmith, P.6    Hook, V.7
  • 33
    • 45249083897 scopus 로고    scopus 로고
    • Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression
    • Funkelstein L, Toneff T, Hwang SR, Reinheckel T, Peters C, Hook V 2008 Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression. J Neurochem 106:384-391
    • (2008) J Neurochem , vol.106 , pp. 384-391
    • Funkelstein, L.1    Toneff, T.2    Hwang, S.R.3    Reinheckel, T.4    Peters, C.5    Hook, V.6
  • 36
    • 0020503983 scopus 로고
    • Identification of a 31,500 molecular weight islet cell protease as cathepsin B
    • Docherty K, Carroll R, Steiner DF 1983 Identification of a 31,500 molecular weight islet cell protease as cathepsin B. Proc Natl Acad Sci USA 80:3245-3249
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 3245-3249
    • Docherty, K.1    Carroll, R.2    Steiner, D.F.3
  • 37
    • 0021250798 scopus 로고
    • Cathepsin B-related proteases in the insulin secretory granule
    • Docherty K, Hutton JC, Steiner DF 1984 Cathepsin B-related proteases in the insulin secretory granule. J Biol Chem 259:6041-6044
    • (1984) J Biol Chem , vol.259 , pp. 6041-6044
    • Docherty, K.1    Hutton, J.C.2    Steiner, D.F.3
  • 38
    • 0037077262 scopus 로고    scopus 로고
    • Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis
    • Kukor Z, Mayerle J, Krüger B, Tóth M, Steed PM, Halangk W, Lerch MM, Sahin-Tóth M 2002 Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis. J Biol Chem 277:21389-21396
    • (2002) J Biol Chem , vol.277 , pp. 21389-21396
    • Kukor, Z.1    Mayerle, J.2    Krüger, B.3    Tóth, M.4    Steed, P.M.5    Halangk, W.6    Lerch, M.M.7    Sahin-Tóth, M.8
  • 39
    • 0029883537 scopus 로고    scopus 로고
    • Cathepsin B is a prorenin processing enzyme
    • Neves FA, Duncan KG, Baxter JD 1996 Cathepsin B is a prorenin processing enzyme. Hypertension 27:514-517
    • (1996) Hypertension , vol.27 , pp. 514-517
    • Neves, F.A.1    Duncan, K.G.2    Baxter, J.D.3
  • 40
    • 0032969486 scopus 로고    scopus 로고
    • Prorenin processing by cathepsin B in vitro and in transfected cells
    • Jutras I, Reudelhuber TL 1999 Prorenin processing by cathepsin B in vitro and in transfected cells. FEBS Lett 443:48-52
    • (1999) FEBS Lett , vol.443 , pp. 48-52
    • Jutras, I.1    Reudelhuber, T.L.2
  • 41
    • 0023780065 scopus 로고
    • An acid protease secreted by transformed cells interferes with antigen processing
    • McCoy K, Gal S, Schwartz RH, Gottesman MM 1988 An acid protease secreted by transformed cells interferes with antigen processing. J Cell Biol 106: 1879-1884
    • (1988) J Cell Biol , vol.106 , pp. 1879-1884
    • McCoy, K.1    Gal, S.2    Schwartz, R.H.3    Gottesman, M.M.4
  • 42
  • 43
    • 0027337988 scopus 로고
    • Proenzyme from of cathepsin L produced by thymic epithelial cells promotes proliferation of immature thymocytes in the presence of IL-1, IL-7, and anti-CD3 antibody
    • Kasai M, Shirasawa T, Kitamura M, Ishido K, Kominami E, Hirokawa K 1993 Proenzyme from of cathepsin L produced by thymic epithelial cells promotes proliferation of immature thymocytes in the presence of IL-1, IL-7, and anti-CD3 antibody. Cell Immunol 150:124-136
    • (1993) Cell Immunol , vol.150 , pp. 124-136
    • Kasai, M.1    Shirasawa, T.2    Kitamura, M.3    Ishido, K.4    Kominami, E.5    Hirokawa, K.6
  • 46
    • 57649183693 scopus 로고    scopus 로고
    • Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
    • Li W, Kornmark L, Jonasson L, Forssell C, Yuan XM 2009 Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis. Atherosclerosis 202:92-102
    • (2009) Atherosclerosis , vol.202 , pp. 92-102
    • Li, W.1    Kornmark, L.2    Jonasson, L.3    Forssell, C.4    Yuan, X.M.5
  • 47
    • 0029839705 scopus 로고    scopus 로고
    • Vesicular monoamine transport inhibitors. Novel action at calcium channels to prevent catecholamine secretion
    • Mahata M, Mahata SK, Parmer RJ, O'Connor DT 1996 Vesicular monoamine transport inhibitors. Novel action at calcium channels to prevent catecholamine secretion. Hypertension 28:414-420
    • (1996) Hypertension , vol.28 , pp. 414-420
    • Mahata, M.1    Mahata, S.K.2    Parmer, R.J.3    O'Connor, D.T.4
  • 48
    • 0028926843 scopus 로고
    • Recombinant human chromogranin A: Expression, purification and characterization of the N-terminal derived peptides
    • Taupenot L, Remacle JE, Helle KB, Aunis D, Bader MF 1995 Recombinant human chromogranin A: expression, purification and characterization of the N-terminal derived peptides. Regul Pept 56:71-88
    • (1995) Regul Pept , vol.56 , pp. 71-88
    • Taupenot, L.1    Remacle, J.E.2    Helle, K.B.3    Aunis, D.4    Bader, M.F.5
  • 49
    • 45549095065 scopus 로고    scopus 로고
    • Sorting of the neuroendocrine secretory protein secretogranin II into the regulated secretory pathway: Role of N- and C-terminal α-helical domains
    • Courel M, Vasquez MS, Hook VY, Mahata SK, Taupenot L 2008 Sorting of the neuroendocrine secretory protein secretogranin II into the regulated secretory pathway: role of N- and C-terminal α-helical domains. J Biol Chem 283:11807-11822
    • (2008) J Biol Chem , vol.283 , pp. 11807-11822
    • Courel, M.1    Vasquez, M.S.2    Hook, V.Y.3    Mahata, S.K.4    Taupenot, L.5
  • 50
    • 0034945881 scopus 로고    scopus 로고
    • Cysteine proteinases mediate extracellular prohormone processing in the thyroid
    • Brix K, Linke M, Tepel C, Herzog V 2001 Cysteine proteinases mediate extracellular prohormone processing in the thyroid. Biol Chem 382:717-725
    • (2001) Biol Chem , vol.382 , pp. 717-725
    • Brix, K.1    Linke, M.2    Tepel, C.3    Herzog, V.4
  • 51
    • 2242491791 scopus 로고    scopus 로고
    • Cleavage of chromogranin A N-terminal domain by plasmin provides a new mechanism for regulating cell adhesion
    • Colombo B, Longhi R, Marinzi C, Magni F, Cattaneo A, Yoo SH, Curnis F, Corti A 2002 Cleavage of chromogranin A N-terminal domain by plasmin provides a new mechanism for regulating cell adhesion. J Biol Chem 277: 45911-45919
    • (2002) J Biol Chem , vol.277 , pp. 45911-45919
    • Colombo, B.1    Longhi, R.2    Marinzi, C.3    Magni, F.4    Cattaneo, A.5    Yoo, S.H.6    Curnis, F.7    Corti, A.8
  • 52
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel C, Brömme D, Herzog V, Brix K 2000 Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J Cell Sci 113 Pt 24:4487-4498
    • (2000) J Cell Sci , vol.113 , Issue.PART 24 , pp. 4487-4498
    • Tepel, C.1    Brömme, D.2    Herzog, V.3    Brix, K.4
  • 53
    • 0027436425 scopus 로고
    • Intracellular and extracellular processing of chromogranin A. Determination of cleavage sites
    • Metz-Boutigue MH, Garcia-Sablone P, Hogue-Angeletti R, Aunis D 1993 Intracellular and extracellular processing of chromogranin A. Determination of cleavage sites. Eur J Biochem 217:247-257
    • (1993) Eur J Biochem , vol.217 , pp. 247-257
    • Metz-Boutigue, M.H.1    Garcia-Sablone, P.2    Hogue-Angeletti, R.3    Aunis, D.4
  • 54
    • 0036859443 scopus 로고    scopus 로고
    • The spectrum of endogenous human chromogranin A-derived peptides identified using a modified proteomic strategy
    • Orr DF, Chen T, Johnsen AH, Chalk R, Buchanan KD, Sloan JM, Rao P, Shaw C 2002 The spectrum of endogenous human chromogranin A-derived peptides identified using a modified proteomic strategy. Proteomics 2:1586-1600
    • (2002) Proteomics , vol.2 , pp. 1586-1600
    • Orr, D.F.1    Chen, T.2    Johnsen, A.H.3    Chalk, R.4    Buchanan, K.D.5    Sloan, J.M.6    Rao, P.7    Shaw, C.8
  • 55
    • 58149101263 scopus 로고    scopus 로고
    • Major role of cathepsin L for producing the peptide hormones ACTH, β-endorphin, and α-MSH, illustrated by protease gene knockout and expression
    • Funkelstein L, Toneff T, Mosier C, Hwang SR, Beuschlein F, Lichtenauer UD, Reinheckel T, Peters C, Hook V 2008 Major role of cathepsin L for producing the peptide hormones ACTH, β-endorphin, and α-MSH, illustrated by protease gene knockout and expression. J Biol Chem 283:35652-35659
    • (2008) J Biol Chem , vol.283 , pp. 35652-35659
    • Funkelstein, L.1    Toneff, T.2    Mosier, C.3    Hwang, S.R.4    Beuschlein, F.5    Lichtenauer, U.D.6    Reinheckel, T.7    Peters, C.8    Hook, V.9
  • 57
    • 0033535927 scopus 로고    scopus 로고
    • Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: Activation by glutathione localized to secretory vesicles
    • Yasothornsrikul S, Aaron W, Toneff T, Hook VY 1999 Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: activation by glutathione localized to secretory vesicles. Biochemistry 38:7421-7430
    • (1999) Biochemistry , vol.38 , pp. 7421-7430
    • Yasothornsrikul, S.1    Aaron, W.2    Toneff, T.3    Hook, V.Y.4
  • 59
    • 49649094763 scopus 로고    scopus 로고
    • Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment
    • Abboud-Jarrous G, Atzmon R, Peretz T, Palermo C, Gadea BB, Joyce JA, Vlodavsky I 2008 Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment. J Biol Chem 283:18167-18176
    • (2008) J Biol Chem , vol.283 , pp. 18167-18176
    • Abboud-Jarrous, G.1    Atzmon, R.2    Peretz, T.3    Palermo, C.4    Gadea, B.B.5    Joyce, J.A.6    Vlodavsky, I.7
  • 61
    • 6944221313 scopus 로고    scopus 로고
    • The catecholamine release-inhibitory "catestatin" fragment of chromogranin A: Naturally occurring human variants with different potencies for multiple chromaffin cell nicotinic cholinergic responses
    • Mahata SK, Mahata M, Wen G, Wong WB, Mahapatra NR, Hamilton BA, O'Connor DT 2004 The catecholamine release-inhibitory "catestatin" fragment of chromogranin A: naturally occurring human variants with different potencies for multiple chromaffin cell nicotinic cholinergic responses. Mol Pharmacol 66:1180-1191
    • (2004) Mol Pharmacol , vol.66 , pp. 1180-1191
    • Mahata, S.K.1    Mahata, M.2    Wen, G.3    Wong, W.B.4    Mahapatra, N.R.5    Hamilton, B.A.6    O'Connor, D.T.7
  • 63
    • 0025788842 scopus 로고
    • Purification and characterization of a novel thiol protease involved in processing the enkephalin precursor
    • Krieger TJ, Hook VY 1991 Purification and characterization of a novel thiol protease involved in processing the enkephalin precursor. J Biol Chem 266: 8376-8383
    • (1991) J Biol Chem , vol.266 , pp. 8376-8383
    • Krieger, T.J.1    Hook, V.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.