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Volumn 8, Issue 6, 2006, Pages 621-633

Catecholamine storage vesicles and the metabolic syndrome: The role of the chromogranin A fragment pancreastatin

Author keywords

Catecholamine; Chromagranin; Free fatty acid; Glucose; Hypertension; Insulin

Indexed keywords

AMINO ACID DERIVATIVE; CARBOHYDRATE; CATECHOLAMINE; CELL PROTEIN; CHROMOGRANIN A; CHROMOGRANIN B; FATTY ACID; GLUCOSE; GLYCINE; HORMONE PRECURSOR; LIPID; NEUROTRANSMITTER RECEPTOR; PANCREASTATIN; PEPTIDE FRAGMENT; SECRETOGRANIN II; SERINE;

EID: 33749464322     PISSN: 14628902     EISSN: 14631326     Source Type: Journal    
DOI: 10.1111/j.1463-1326.2006.00575.x     Document Type: Review
Times cited : (31)

References (94)
  • 1
    • 0018967377 scopus 로고
    • The molecular organization of adrenal chromaffin granules
    • Winkler H, Westhead E. The molecular organization of adrenal chromaffin granules. Neuroscience 1980; 5 (11): 1803-1823.
    • (1980) Neuroscience , vol.5 , Issue.11 , pp. 1803-1823
    • Winkler, H.1    Westhead, E.2
  • 2
    • 0017191315 scopus 로고
    • The composition of adrenal chromaffin granules: An assessment of controversial results
    • Winkler H. The composition of adrenal chromaffin granules: An assessment of controversial results. Neuroscience 1976; 1 (2): 65-80.
    • (1976) Neuroscience , vol.1 , Issue.2 , pp. 65-80
    • Winkler, H.1
  • 3
    • 0023838230 scopus 로고
    • Enkephalins in human phaeochromocytomas: Localization in immunoreactive, high molecular weight form to the soluble core of chromaffin granules
    • Parmer RJ, O'Connor DT. Enkephalins in human phaeochromocytomas: localization in immunoreactive, high molecular weight form to the soluble core of chromaffin granules. J Hypertens 1988; 6 (3): 187-198.
    • (1988) J Hypertens , vol.6 , Issue.3 , pp. 187-198
    • Parmer, R.J.1    O'Connor, D.T.2
  • 4
    • 0026783755 scopus 로고
    • Calcium and catecholamine interactions with adrenal chromogranins. Comparison of driving forces in binding and aggregation Calcium and catecholamine interactions with adrenal chromogranins. Comparison of driving forces in binding and aggregation
    • Videen JS, Mezger MS, Chang YM, O'Connor DT. Calcium and catecholamine interactions with adrenal chromogranins. Comparison of driving forces in binding and aggregation. J Biol Chem 1992; 267 (5): 3066-3073.
    • (1992) J Biol Chem , vol.267 , Issue.5 , pp. 3066-3073
    • Videen, J.S.1    Mezger, M.S.2    Chang, Y.M.3    O'Connor, D.T.4
  • 5
    • 0020602664 scopus 로고
    • Chromogranin A: Immunohistology reveals its universal occurrence in normal polypeptide hormone producing endocrine glands
    • O'Connor DT, Burton D, Deftos LJ. Chromogranin A: Immunohistology reveals its universal occurrence in normal polypeptide hormone producing endocrine glands. Life Sci 1983; 33 (17): 1657-1663.
    • (1983) Life Sci , vol.33 , Issue.17 , pp. 1657-1663
    • O'Connor, D.T.1    Burton, D.2    Deftos, L.J.3
  • 6
    • 0021361309 scopus 로고
    • Chromogranin A, the major catecholamine storage vesicle soluble protein. Multiple size forms, subcellular storage, and regional distribution in chromaffin and nervous tissue elucidated by radioimmunoassay
    • O'Connor DT, Frigon RP. Chromogranin A, the major catecholamine storage vesicle soluble protein. Multiple size forms, subcellular storage, and regional distribution in chromaffin and nervous tissue elucidated by radioimmunoassay. J Biol Chem 1984; 259 (5): 3237-3247.
    • (1984) J Biol Chem , vol.259 , Issue.5 , pp. 3237-3247
    • O'Connor, D.T.1    Frigon, R.P.2
  • 7
    • 0026340086 scopus 로고
    • Chromogranin A: Localization and stoichiometry in large dense core catecholamine storage vesicles from sympathetic nerve
    • O'Connor DT, Klein RL, Thureson-Klein AK, Barbosa JA. Chromogranin A: localization and stoichiometry in large dense core catecholamine storage vesicles from sympathetic nerve. Brain Res 1991; 567 (2): 188-196.
    • (1991) Brain Res , vol.567 , Issue.2 , pp. 188-196
    • O'Connor, D.T.1    Klein, R.L.2    Thureson-Klein, A.K.3    Barbosa, J.A.4
  • 8
    • 0013840826 scopus 로고
    • The release of protein from the stimulated adrenal medulla
    • Banks P, Helle K. The release of protein from the stimulated adrenal medulla. Biochem J 1965; 97 (3): 40C-41C.
    • (1965) Biochem J , vol.97 , Issue.3
    • Banks, P.1    Helle, K.2
  • 9
    • 0013926088 scopus 로고
    • Some chemical and physical properties of the soluble protein fraction of bovine adrenal chromaffin granules
    • Helle KB. Some chemical and physical properties of the soluble protein fraction of bovine adrenal chromaffin granules. Mol Pharmacol 1966; 2 (4): 298-310.
    • (1966) Mol Pharmacol , vol.2 , Issue.4 , pp. 298-310
    • Helle, K.B.1
  • 10
    • 0020508955 scopus 로고
    • Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase
    • Lee RW, Huttner WB. Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase. J Biol Chem 1983; 258 (18): 11326-11334.
    • (1983) J Biol Chem , vol.258 , Issue.18 , pp. 11326-11334
    • Lee, R.W.1    Huttner, W.B.2
  • 11
    • 0019511459 scopus 로고
    • Characterization of adenohypophysial polypeptides by two-dimensional gel electrophoresis. II. Sulfated and glycosylated polypeptides
    • Rosa P, Zanini A. Characterization of adenohypophysial polypeptides by two-dimensional gel electrophoresis. II. Sulfated and glycosylated polypeptides. Mol Cell Endocrinol 1981; 24 (2): 181-193.
    • (1981) Mol Cell Endocrinol , vol.24 , Issue.2 , pp. 181-193
    • Rosa, P.1    Zanini, A.2
  • 12
    • 0029035081 scopus 로고
    • Secretogranin II: Molecular properties, regulation of biosynthesis and processing to the neuropeptide secretoneurin
    • Fischer-Colbrie R, Laslop A, Kirchmair R. Secretogranin II: Molecular properties, regulation of biosynthesis and processing to the neuropeptide secretoneurin. Prog Neurobiol 1995; 46 (1): 49-70.
    • (1995) Prog Neurobiol , vol.46 , Issue.1 , pp. 49-70
    • Fischer-Colbrie, R.1    Laslop, A.2    Kirchmair, R.3
  • 13
    • 0026085275 scopus 로고
    • The granin (chromogranin/secretogranin) family
    • Huttner WB, Gerdes HH, Rosa P. The granin (chromogranin/secretogranin) family. Trends Biochem Sci 1991; 16 (1): 27-30.
    • (1991) Trends Biochem Sci , vol.16 , Issue.1 , pp. 27-30
    • Huttner, W.B.1    Gerdes, H.H.2    Rosa, P.3
  • 14
    • 0025485747 scopus 로고
    • 1B1075: A brain- and pituitary-specific mRNA that encodes a novel chromogranin/secretogranin-like component of intracellular vesicles
    • Ottiger HP, Battenberg EF, Tsou AP, Bloom FE, Sutcliffe JG. 1B1075: A brain- and pituitary-specific mRNA that encodes a novel chromogranin/ secretogranin-like component of intracellular vesicles. J Neurosci 1990; 10 (9): 3135-3147.
    • (1990) J Neurosci , vol.10 , Issue.9 , pp. 3135-3147
    • Ottiger, H.P.1    Battenberg, E.F.2    Tsou, A.P.3    Bloom, F.E.4    Sutcliffe, J.G.5
  • 15
    • 0022549618 scopus 로고
    • Monoclonal antibody HISL-19 as an immunocytochemical probe for neuroendocrine differentiation. Its application in diagnostic pathology
    • Krisch K, Buxbaum P, Horvat G et al. Monoclonal antibody HISL-19 as an immunocytochemical probe for neuroendocrine differentiation. Its application in diagnostic pathology. Am J Pathol 1986; 123 (1): 100-108.
    • (1986) Am J Pathol , vol.123 , Issue.1 , pp. 100-108
    • Krisch, K.1    Buxbaum, P.2    Horvat, G.3
  • 16
    • 0035878968 scopus 로고    scopus 로고
    • Neuroendocrine secretory protein 7B2: Structure, expression and functions
    • Mbikay M, Seidah NG, Chretien M. Neuroendocrine secretory protein 7B2: structure, expression and functions. Biochem J 2001; 357 (Pt 2): 329-342.
    • (2001) Biochem J , vol.357 , Issue.PART 2 , pp. 329-342
    • Mbikay, M.1    Seidah, N.G.2    Chretien, M.3
  • 17
    • 0030998512 scopus 로고    scopus 로고
    • Molecular cloning and characterization of NESP55, a novel chromogranin-like precursor of a peptide with 5-HT1B receptor antagonist activity
    • Ischia R, Lovisetti-Scamihorn P, Hogue-Angeletti R, Wolkersdorfer M, Winkler H, Fischer-Colbrie R. Molecular cloning and characterization of NESP55, a novel chromogranin-like precursor of a peptide with 5-HT1B receptor antagonist activity. J Biol Chem 1997; 272 (17): 11657-11662.
    • (1997) J Biol Chem , vol.272 , Issue.17 , pp. 11657-11662
    • Ischia, R.1    Lovisetti-Scamihorn, P.2    Hogue-Angeletti, R.3    Wolkersdorfer, M.4    Winkler, H.5    Fischer-Colbrie, R.6
  • 18
    • 13544253748 scopus 로고    scopus 로고
    • Role of H+-ATPase-mediated acidification in sorting and release of the regulated secretory protein chromogranin A: Evidence for a vesiculogenic function
    • Taupenot L, Harper KL, O'Connor DT. Role of H+-ATPase-mediated acidification in sorting and release of the regulated secretory protein chromogranin A: Evidence for a vesiculogenic function. J Biol Chem 2005; 280 (5): 3885-3897.
    • (2005) J Biol Chem , vol.280 , Issue.5 , pp. 3885-3897
    • Taupenot, L.1    Harper, K.L.2    O'Connor, D.T.3
  • 19
    • 0037456743 scopus 로고    scopus 로고
    • The chromogranin-secretogranin family
    • Taupenot L, Harper KL, O'Connor DT. The chromogranin-secretogranin family. N Engl J Med 2003; 348 (12): 1134-1149.
    • (2003) N Engl J Med , vol.348 , Issue.12 , pp. 1134-1149
    • Taupenot, L.1    Harper, K.L.2    O'Connor, D.T.3
  • 20
    • 0026680263 scopus 로고
    • The chromogranins A and B: The first 25 years and future perspectives
    • Winkler H, Fischer-Colbrie R. The chromogranins A and B: The first 25 years and future perspectives. Neuroscience 1992; 49 (3): 497-528.
    • (1992) Neuroscience , vol.49 , Issue.3 , pp. 497-528
    • Winkler, H.1    Fischer-Colbrie, R.2
  • 21
    • 22144495740 scopus 로고    scopus 로고
    • Hypertension from targeted ablation of chromogranin A can be rescued by the human ortholog
    • Mahapatra NR, O'Connor DT, Vaingankar SM et al. Hypertension from targeted ablation of chromogranin A can be rescued by the human ortholog. J Clin Invest 2005; 115 (7): 1942-1952.
    • (2005) J Clin Invest , vol.115 , Issue.7 , pp. 1942-1952
    • Mahapatra, N.R.1    O'Connor, D.T.2    Vaingankar, S.M.3
  • 22
    • 9644276789 scopus 로고    scopus 로고
    • The granin family of uniquely acidic proteins of the diffuse neuroendocrine system: Comparative and functional aspects
    • Helle KB. The granin family of uniquely acidic proteins of the diffuse neuroendocrine system: Comparative and functional aspects. Biol Rev Camb Philos Soc 2004; 79 (4): 769-794.
    • (2004) Biol Rev Camb Philos Soc , vol.79 , Issue.4 , pp. 769-794
    • Helle, K.B.1
  • 23
    • 0029996190 scopus 로고    scopus 로고
    • Dispersion of chromogranin/secretogranin secretory protein family loci in mammalian genomes
    • Mahata SK, Kozak CA, Szpirer J et al. Dispersion of chromogranin/ secretogranin secretory protein family loci in mammalian genomes. Genomics 1996; 33 (1): 135-139.
    • (1996) Genomics , vol.33 , Issue.1 , pp. 135-139
    • Mahata, S.K.1    Kozak, C.A.2    Szpirer, J.3
  • 24
    • 0022543388 scopus 로고
    • Chromogranins, widespread in endocrine and nervous tissue, bind Ca2+
    • Reiffen FU, Gratzl M. Chromogranins, widespread in endocrine and nervous tissue, bind Ca2+. FEBS Lett 1986; 195 (1-2): 327-330.
    • (1986) FEBS Lett , vol.195 , Issue.1-2 , pp. 327-330
    • Reiffen, F.U.1    Gratzl, M.2
  • 25
    • 0023083596 scopus 로고
    • Chromogranin A: The primary structure deduced from cDNA clones reveals the presence of pairs of basic amino acids
    • Grimes M, Iacangelo A, Eiden LE, Godfrey B, Herbert E. Chromogranin A: the primary structure deduced from cDNA clones reveals the presence of pairs of basic amino acids. Ann N Y Acad Sci 1987; 493: 351-378.
    • (1987) Ann N Y Acad Sci , vol.493 , pp. 351-378
    • Grimes, M.1    Iacangelo, A.2    Eiden, L.E.3    Godfrey, B.4    Herbert, E.5
  • 26
    • 0023555747 scopus 로고
    • The primary structure of human chromogranin A and pancreastatin
    • Konecki DS, Benedum UM, Gerdes HH, Huttner WB. The primary structure of human chromogranin A and pancreastatin. J Biol Chem 1987; 262 (35): 17026-17030.
    • (1987) J Biol Chem , vol.262 , Issue.35 , pp. 17026-17030
    • Konecki, D.S.1    Benedum, U.M.2    Gerdes, H.H.3    Huttner, W.B.4
  • 27
    • 0024440813 scopus 로고
    • Interaction of calcium with porcine adrenal chromogranin A (secretory protein-I) and chromogranin B (secretogranin I)
    • Gorr SU, Shioi J, Cohn DV. Interaction of calcium with porcine adrenal chromogranin A (secretory protein-I) and chromogranin B (secretogranin I). Am J Physiol 1989; 257 (2 Pt 1): E247-E254.
    • (1989) Am J Physiol , vol.257 , Issue.2 PART 1
    • Gorr, S.U.1    Shioi, J.2    Cohn, D.V.3
  • 28
    • 0024344257 scopus 로고
    • The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation
    • Gerdes HH, Rosa P, Phillips E et al. The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation. J Biol Chem 1989; 264 (20): 12009-12015.
    • (1989) J Biol Chem , vol.264 , Issue.20 , pp. 12009-12015
    • Gerdes, H.H.1    Rosa, P.2    Phillips, E.3
  • 29
    • 0025744980 scopus 로고
    • High capacity, low affinity Ca2+ binding of chromogranin A. Relationship between the pH-induced conformational change and Ca2+ binding property
    • Yoo SH, Albanesi JP. High capacity, low affinity Ca2+ binding of chromogranin A. Relationship between the pH-induced conformational change and Ca2+ binding property. J Biol Chem 1991; 266 (12): 7740-7745.
    • (1991) J Biol Chem , vol.266 , Issue.12 , pp. 7740-7745
    • Yoo, S.H.1    Albanesi, J.P.2
  • 30
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly RB. Pathways of protein secretion in eukaryotes. Science 1985; 230 (4721): 25-32.
    • (1985) Science , vol.230 , Issue.4721 , pp. 25-32
    • Kelly, R.B.1
  • 31
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban PA, Irminger JC. Sorting and processing of secretory proteins. Biochem J 1994; 299 (1): 1-18.
    • (1994) Biochem J , vol.299 , Issue.1 , pp. 1-18
    • Halban, P.A.1    Irminger, J.C.2
  • 32
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: Looking backward and looking forward
    • Arvan P, Castle D. Sorting and storage during secretory granule biogenesis: Looking backward and looking forward. Biochem J 1998; 332 (3): 593-610.
    • (1998) Biochem J , vol.332 , Issue.3 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 33
    • 0027441696 scopus 로고
    • pH-dependent binding of chromogranin B and secretory vesicle matrix proteins to the vesicle membrane
    • Yoo SH. pH-dependent binding of chromogranin B and secretory vesicle matrix proteins to the vesicle membrane. Biochim Biophys Acta 1993; 1179 (3): 239-246.
    • (1993) Biochim Biophys Acta , vol.1179 , Issue.3 , pp. 239-246
    • Yoo, S.H.1
  • 34
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E, Huttner WB. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J Cell Biol 1991; 115 (6): 1505-1519.
    • (1991) J Cell Biol , vol.115 , Issue.6 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 35
    • 0030976604 scopus 로고    scopus 로고
    • Carboxypeptidase E is a regulated secretory pathway sorting receptor: Genetic obliteration leads to endocrine disorders in Cpe (fat) mice
    • Cool DR, Normant E, Shen F et al. Carboxypeptidase E is a regulated secretory pathway sorting receptor: Genetic obliteration leads to endocrine disorders in Cpe (fat) mice. Cell 1997; 88 (1): 73-83.
    • (1997) Cell , vol.88 , Issue.1 , pp. 73-83
    • Cool, D.R.1    Normant, E.2    Shen, F.3
  • 36
    • 0031213595 scopus 로고    scopus 로고
    • Protein secretion: Puzzling receptors
    • Thiele C, Gerdes HH, Huttner WB. Protein secretion: Puzzling receptors. Curr Biol 1997; 7 (8): R496-R500.
    • (1997) Curr Biol , vol.7 , Issue.8
    • Thiele, C.1    Gerdes, H.H.2    Huttner, W.B.3
  • 37
    • 0032177313 scopus 로고    scopus 로고
    • Protein and lipid sorting from the trans-Golgi network to secretory granules-recent developments
    • Thiele C, Huttner WB. Protein and lipid sorting from the trans-Golgi network to secretory granules-recent developments. Semin Cell Dev Biol 1998; 9 (5): 511-516.
    • (1998) Semin Cell Dev Biol , vol.9 , Issue.5 , pp. 511-516
    • Thiele, C.1    Huttner, W.B.2
  • 38
    • 0035280141 scopus 로고    scopus 로고
    • Secretory granule biogenesis: Rafting to the SNARE
    • Tooze SA, Martens GJ, Huttner WB. Secretory granule biogenesis: Rafting to the SNARE. Trends Cell Biol 2001; 11 (3): 116-122.
    • (2001) Trends Cell Biol , vol.11 , Issue.3 , pp. 116-122
    • Tooze, S.A.1    Martens, G.J.2    Huttner, W.B.3
  • 39
    • 0037115625 scopus 로고    scopus 로고
    • Identification of a novel sorting determinant for the regulated pathway in the secretory protein chromogranin A
    • Taupenot L, Harper KL, Mahapatra NR, Parmer RJ, Mahata SK, O'Connor DT. Identification of a novel sorting determinant for the regulated pathway in the secretory protein chromogranin A. J Cell Sci 2002; 115 (Pt 24): 4827-4841.
    • (2002) J Cell Sci , vol.115 , Issue.PART 24 , pp. 4827-4841
    • Taupenot, L.1    Harper, K.L.2    Mahapatra, N.R.3    Parmer, R.J.4    Mahata, S.K.5    O'Connor, D.T.6
  • 40
    • 0027960995 scopus 로고
    • Glucocorticoid activation of chromogranin A gene expression. Identification and characterization of a novel glucocorticoid response element
    • Rozansky DJ, Wu H, Tang K, Parmer RJ, O'Connor DT. Glucocorticoid activation of chromogranin A gene expression. Identification and characterization of a novel glucocorticoid response element. J Clin Invest 1994; 94 (6): 2357-2368.
    • (1994) J Clin Invest , vol.94 , Issue.6 , pp. 2357-2368
    • Rozansky, D.J.1    Wu, H.2    Tang, K.3    Parmer, R.J.4    O'Connor, D.T.5
  • 41
    • 0027322942 scopus 로고
    • Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways
    • Chanat E, Weiss U, Huttner WB, Tooze SA. Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways. EMBO J 1993; 12 (5): 2159-2168.
    • (1993) EMBO J , vol.12 , Issue.5 , pp. 2159-2168
    • Chanat, E.1    Weiss, U.2    Huttner, W.B.3    Tooze, S.A.4
  • 42
    • 0027933035 scopus 로고
    • The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network
    • Chanat E, Weiss U, Huttner WB. The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network. FEBS Lett 1994; 351 (2): 225-230.
    • (1994) FEBS Lett , vol.351 , Issue.2 , pp. 225-230
    • Chanat, E.1    Weiss, U.2    Huttner, W.B.3
  • 43
    • 0039359126 scopus 로고    scopus 로고
    • Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis
    • Kromer A, Glombik MM, Huttner WB, Gerdes HH. Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis. J Cell Biol 1998; 140 (6): 1331-1346.
    • (1998) J Cell Biol , vol.140 , Issue.6 , pp. 1331-1346
    • Kromer, A.1    Glombik, M.M.2    Huttner, W.B.3    Gerdes, H.H.4
  • 44
    • 0344791717 scopus 로고    scopus 로고
    • The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules
    • Glombik MM, Kromer A, Salm T, Huttner WB, Gerdes HH. The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules. EMBO J 1999; 18 (4): 1059-1070.
    • (1999) EMBO J , vol.18 , Issue.4 , pp. 1059-1070
    • Glombik, M.M.1    Kromer, A.2    Salm, T.3    Huttner, W.B.4    Gerdes, H.H.5
  • 45
    • 0025017742 scopus 로고
    • Is physiologic sympathoadrenal catecholamine release exocytotic in humans?
    • Takiyyuddin MA, Cervenka JH, Sullivan PA et al. Is physiologic sympathoadrenal catecholamine release exocytotic in humans? Circulation 1990; 81 (1): 185-195.
    • (1990) Circulation , vol.81 , Issue.1 , pp. 185-195
    • Takiyyuddin, M.A.1    Cervenka, J.H.2    Sullivan, P.A.3
  • 46
    • 0022480209 scopus 로고
    • The molecular function of adrenal chromaffin granules: Established facts and unresolved topics
    • Winkler H, Apps DK, Fischer-Colbrie R. The molecular function of adrenal chromaffin granules: Established facts and unresolved topics. Neuroscience 1986; 18 (2): 261-290.
    • (1986) Neuroscience , vol.18 , Issue.2 , pp. 261-290
    • Winkler, H.1    Apps, D.K.2    Fischer-Colbrie, R.3
  • 47
    • 0023035470 scopus 로고
    • Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion
    • Tatemoto K, Efendic S, Mutt V, Makk G, Feistner GJ, Barchas JD. Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion. Nature 1986; 324 (6096): 476-478.
    • (1986) Nature , vol.324 , Issue.6096 , pp. 476-478
    • Tatemoto, K.1    Efendic, S.2    Mutt, V.3    Makk, G.4    Feistner, G.J.5    Barchas, J.D.6
  • 48
    • 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. Studies of the dysglycemic peptide, pancreastatin, using a human forearm model. Ann N Y Acad Sci 2002; 971: 528-529.
    • (2002) Ann N Y Acad Sci , vol.971 , pp. 528-529
    • Cadman, P.E.1    Rao, F.2    Mahata, S.K.3    O'Connor, D.T.4
  • 49
    • 0029956552 scopus 로고    scopus 로고
    • Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules
    • Strub JM, Goumon Y, Lugardon K et al. Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. J Biol Chem 1996; 271 (45): 28533-28540.
    • (1996) J Biol Chem , vol.271 , Issue.45 , pp. 28533-28540
    • Strub, J.M.1    Goumon, Y.2    Lugardon, K.3
  • 50
    • 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. Vasostatins, comprising the N-terminal domain of chromogranin A, suppress tension in isolated human blood vessel segments. J Neuroendocrinol 1993; 5 (4): 405-412.
    • (1993) J Neuroendocrinol , vol.5 , Issue.4 , pp. 405-412
    • Aardal, S.1    Helle, K.B.2    Elsayed, S.3    Reed, R.K.4    Serck-Hanssen, G.5
  • 51
    • 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 et al. Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist. J Clin Invest 1997; 100 (6): 1623-1633.
    • (1997) J Clin Invest , vol.100 , Issue.6 , pp. 1623-1633
    • Mahata, S.K.1    O'Connor, D.T.2    Mahata, M.3
  • 52
    • 0032889947 scopus 로고    scopus 로고
    • Neurotrophin activation of catecholamine storage vesicle protein gene expression: Signaling to chromogranin a biosynthesis
    • Mahata SK, Mahata M, Wu H, Parmer RJ, O'Connor DT. Neurotrophin activation of catecholamine storage vesicle protein gene expression: signaling to chromogranin a biosynthesis. Neuroscience 1999; 88 (2): 405-424.
    • (1999) Neuroscience , vol.88 , Issue.2 , pp. 405-424
    • Mahata, S.K.1    Mahata, M.2    Wu, H.3    Parmer, R.J.4    O'Connor, D.T.5
  • 53
    • 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 et al. 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 2004; 66 (5): 1180-1191.
    • (2004) Mol Pharmacol , vol.66 , Issue.5 , pp. 1180-1191
    • Mahata, S.K.1    Mahata, M.2    Wen, G.3
  • 54
    • 0037727654 scopus 로고    scopus 로고
    • Catestatin (CgA344-364) stimulates rat mast cell release of histamine in a manner comparable to mastoparan and other cationic charged neuropeptides
    • Kruger PG, Mahata SK, Helle KB. Catestatin (CgA344-364) stimulates rat mast cell release of histamine in a manner comparable to mastoparan and other cationic charged neuropeptides. Regul Pept 2003; 114 (1): 29-35.
    • (2003) Regul Pept , vol.114 , Issue.1 , pp. 29-35
    • Kruger, P.G.1    Mahata, S.K.2    Helle, K.B.3
  • 55
    • 14844321986 scopus 로고    scopus 로고
    • New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A
    • Briolat J, Wu SD, Mahata SK et al. New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A. Cell Mol Life Sci 2005; 62 (3): 377-385.
    • (2005) Cell Mol Life Sci , vol.62 , Issue.3 , pp. 377-385
    • Briolat, J.1    Wu, S.D.2    Mahata, S.K.3
  • 56
    • 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. Chromogranin A, an 'on/off'switch controlling dense-core secretory granule biogenesis. Cell 2001; 106 (4): 499-509.
    • (2001) Cell , vol.106 , Issue.4 , pp. 499-509
    • Kim, T.1    Tao-Cheng, J.H.2    Eiden, L.E.3    Loh, Y.P.4
  • 57
    • 22144435531 scopus 로고    scopus 로고
    • Chromogranin A: A surprising link between granule biogenesis and hypertension
    • Kim T, Loh YP. Chromogranin A: A surprising link between granule biogenesis and hypertension. J Clin Invest 2005; 115 (7): 1711-1713.
    • (2005) J Clin Invest , vol.115 , Issue.7 , pp. 1711-1713
    • Kim, T.1    Loh, Y.P.2
  • 58
    • 0029071546 scopus 로고
    • Chromogranin A in human hypertension. Influence of heredity
    • Takiyyuddin MA, Parmer RJ, Kailasam MT et al. Chromogranin A in human hypertension. Influence of heredity. Hypertension 1995; 26 (1): 213-220.
    • (1995) Hypertension , vol.26 , Issue.1 , pp. 213-220
    • Takiyyuddin, M.A.1    Parmer, R.J.2    Kailasam, M.T.3
  • 59
    • 0033507145 scopus 로고    scopus 로고
    • Catecholamine storage vesicle protein expression in genetic hypertension
    • O'Connor DT, Takiyyuddin MA, Printz MP et al. Catecholamine storage vesicle protein expression in genetic hypertension. Blood Press 1999; 8 (5-6): 285-295.
    • (1999) Blood Press , vol.8 , Issue.5-6 , pp. 285-295
    • O'Connor, D.T.1    Takiyyuddin, M.A.2    Printz, M.P.3
  • 60
    • 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. Early decline in the catecholamine release-inhibitory peptide catestatin in humans at genetic risk of hypertension. J Hypertens 2002; 20 (7): 1335-1345.
    • (2002) J Hypertens , vol.20 , Issue.7 , 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
  • 61
    • 10744224429 scopus 로고    scopus 로고
    • Both rare and common polymorphisms contribute functional variation at CHGA, a regulator of catecholamine physiology
    • Wen G, Mahata SK, Cadman P et al. Both rare and common polymorphisms contribute functional variation at CHGA, a regulator of catecholamine physiology. Am J Hum Genet 2004; 74 (2): 197-207.
    • (2004) Am J Hum Genet , vol.74 , Issue.2 , pp. 197-207
    • Wen, G.1    Mahata, S.K.2    Cadman, P.3
  • 62
    • 0023921328 scopus 로고
    • The sequence of porcine chromogranin A messenger RNA demonstrates chromogranin A can serve as the precursor for the biologically active hormone, pancreastatin
    • Iacangelo AL, Fischer-Colbrie R, Koller KJ, Brownstein MJ, Eiden LE. The sequence of porcine chromogranin A messenger RNA demonstrates chromogranin A can serve as the precursor for the biologically active hormone, pancreastatin. Endocrinology 1988; 122 (5): 2339-2341.
    • (1988) Endocrinology , vol.122 , Issue.5 , pp. 2339-2341
    • Iacangelo, A.L.1    Fischer-Colbrie, R.2    Koller, K.J.3    Brownstein, M.J.4    Eiden, L.E.5
  • 63
    • 0030059207 scopus 로고    scopus 로고
    • Pancreastatin: Further evidence for its consideration as a regulatory peptide
    • Sanchez-Margalet V, Lucas M, Goberna R. Pancreastatin: Further evidence for its consideration as a regulatory peptide. J Mol Endocrinol 1996; 16 (1): 1-8.
    • (1996) J Mol Endocrinol , vol.16 , Issue.1 , pp. 1-8
    • Sanchez-Margalet, V.1    Lucas, M.2    Goberna, R.3
  • 65
    • 0347361462 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, inhibits leptin and enhances UCP-2 expression in isolated rat adipocytes
    • Gonzalez-Yanes C, Sanchez-Margalet V. Pancreastatin, a chromogranin A-derived peptide, inhibits leptin and enhances UCP-2 expression in isolated rat adipocytes. Cell Mol Life Sci 2003; 60 (12): 2749-2756.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.12 , pp. 2749-2756
    • Gonzalez-Yanes, C.1    Sanchez-Margalet, V.2
  • 66
    • 0036930158 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, activates protein synthesis signaling cascade in rat adipocytes
    • Gonzalez-Yanes C, Sanchez-Margalet V. Pancreastatin, a chromogranin A-derived peptide, activates protein synthesis signaling cascade in rat adipocytes. Biochem Biophys Res Commun 2002; 299 (4): 525-531.
    • (2002) Biochem Biophys Res Commun , vol.299 , Issue.4 , pp. 525-531
    • Gonzalez-Yanes, C.1    Sanchez-Margalet, V.2
  • 67
    • 0032145713 scopus 로고    scopus 로고
    • Secretoneurin and chemoattractant receptor interactions
    • Kong C, Gill BM, Rahimpour R et al. Secretoneurin and chemoattractant receptor interactions. J Neuroimmunol 1998; 88 (1-2): 91-98.
    • (1998) J Neuroimmunol , vol.88 , Issue.1-2 , pp. 91-98
    • Kong, C.1    Gill, B.M.2    Rahimpour, R.3
  • 68
    • 0034473607 scopus 로고    scopus 로고
    • Vasostatins. Vascular targets
    • Helle KB. Vasostatins. Vascular targets. Adv Exp Med Biol 2000; 482: 225-238.
    • (2000) Adv Exp Med Biol , vol.482 , pp. 225-238
    • Helle, K.B.1
  • 69
    • 0034933529 scopus 로고    scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, inhibits DNA and protein synthesis by producing nitric oxide in HTC rat hepatoma cells
    • Sanchez-Margalet V, Gonzalez-Yanes C, Najib S. Pancreastatin, a chromogranin A-derived peptide, inhibits DNA and protein synthesis by producing nitric oxide in HTC rat hepatoma cells. J Hepatol 2001; 35 (1): 80-85.
    • (2001) J Hepatol , vol.35 , Issue.1 , pp. 80-85
    • Sanchez-Margalet, V.1    Gonzalez-Yanes, C.2    Najib, S.3
  • 70
    • 0033853606 scopus 로고    scopus 로고
    • Pancreastatin modulates insulin signaling in rat adipocytes: Mechanisms of cross-talk
    • Gonzalez-Yanes C, Sanchez-Margalet V. Pancreastatin modulates insulin signaling in rat adipocytes: Mechanisms of cross-talk. Diabetes 2000; 49 (8): 1288-1294.
    • (2000) Diabetes , vol.49 , Issue.8 , pp. 1288-1294
    • Gonzalez-Yanes, C.1    Sanchez-Margalet, V.2
  • 71
    • 0026615867 scopus 로고
    • Glucogenolytic and hyperglycaemic effect of 33-49 C-terminal fragment of pancreastatin in the rat in vivo
    • Sanchez-Margalet V, Calvo JR, Goberna R. Glucogenolytic and hyperglycaemic effect of 33-49 C-terminal fragment of pancreastatin in the rat in vivo. Horm Metab Res 1992; 24 (10): 455-457.
    • (1992) Horm Metab Res , vol.24 , Issue.10 , pp. 455-457
    • Sanchez-Margalet, V.1    Calvo, J.R.2    Goberna, R.3
  • 72
    • 0026654435 scopus 로고
    • Pancreastatin and its 33-49 C-terminal fragment inhibit glucagon-stimulated insulin in vivo
    • Sanchez-Margalet V, Calvo JR, Lucas M, Goberna R. Pancreastatin and its 33-49 C-terminal fragment inhibit glucagon-stimulated insulin in vivo. Gen Pharmacol 1992; 23 (4): 637-638.
    • (1992) Gen Pharmacol , vol.23 , Issue.4 , pp. 637-638
    • Sanchez-Margalet, V.1    Calvo, J.R.2    Lucas, M.3    Goberna, R.4
  • 73
    • 0028290630 scopus 로고
    • Pancreastatin inhibits insulin-stimulated glycogen synthesis but not glycolysis in rat hepatocytes
    • Sanchez-Margalet V, Goberna R. Pancreastatin inhibits insulin-stimulated glycogen synthesis but not glycolysis in rat hepatocytes. Regul Pept 1994; 51 (3): 215-220.
    • (1994) Regul Pept , vol.51 , Issue.3 , pp. 215-220
    • Sanchez-Margalet, V.1    Goberna, R.2
  • 74
    • 9944227667 scopus 로고    scopus 로고
    • eNOS, nNOS, cGMP and protein kinase G mediate the inhibitory effect of pancreastatin, a chromogranin A-derived peptide, on growth and proliferation of hepatoma cells
    • Diaz-Troya S, Najib S, Sanchez-Margalet V. eNOS, nNOS, cGMP and protein kinase G mediate the inhibitory effect of pancreastatin, a chromogranin A-derived peptide, on growth and proliferation of hepatoma cells. Regul Pept 2005; 125 (1-3): 41-46.
    • (2005) Regul Pept , vol.125 , Issue.1-3 , pp. 41-46
    • Diaz-Troya, S.1    Najib, S.2    Sanchez-Margalet, V.3
  • 75
    • 0025373848 scopus 로고
    • The importance of the C-terminal amide structure of rat pancreastatin to inhibit pancreatic exocrine secretion
    • Miyasaka K, Funakoshi A, Kitani K, Tamamura H, Fujii N, Funakoshi S. The importance of the C-terminal amide structure of rat pancreastatin to inhibit pancreatic exocrine secretion. FEBS Lett 1990; 263 (2): 279-280.
    • (1990) FEBS Lett , vol.263 , Issue.2 , pp. 279-280
    • Miyasaka, K.1    Funakoshi, A.2    Kitani, K.3    Tamamura, H.4    Fujii, N.5    Funakoshi, S.6
  • 76
    • 0028267042 scopus 로고
    • Pancreastatin, a chromogranin A-derived peptide, inhibits transcription of the parathyroid hormone and chromogranin A genes and decreases the stability of the respective messenger ribonucleic acids in parathyroid cells in culture
    • Zhang JX, Fasciotto BH, Darling DS, Cohn DV. Pancreastatin, a chromogranin A-derived peptide, inhibits transcription of the parathyroid hormone and chromogranin A genes and decreases the stability of the respective messenger ribonucleic acids in parathyroid cells in culture. Endocrinology 1994; 134 (3): 1310-1316.
    • (1994) Endocrinology , vol.134 , Issue.3 , pp. 1310-1316
    • Zhang, J.X.1    Fasciotto, B.H.2    Darling, D.S.3    Cohn, D.V.4
  • 77
    • 0027165779 scopus 로고
    • Parastatin (porcine chromogranin A347-419), a novel chromogranin A-derived peptide, inhibits parathyroid cell secretion
    • Fasciotto BH, Trauss CA, Greeley GH, Cohn DV. Parastatin (porcine chromogranin A347-419), a novel chromogranin A-derived peptide, inhibits parathyroid cell secretion. Endocrinology 1993; 133 (2): 461-466.
    • (1993) Endocrinology , vol.133 , Issue.2 , pp. 461-466
    • Fasciotto, B.H.1    Trauss, C.A.2    Greeley, G.H.3    Cohn, D.V.4
  • 78
    • 0025734203 scopus 로고
    • Structure and function of the chromogranin A gene. Clues to evolution and tissue-specific expression
    • Wu HJ, Rozansky DJ, Parmer RJ, Gill BM, O'Connor DT. Structure and function of the chromogranin A gene. Clues to evolution and tissue-specific expression. J Biol Chem 1991; 266 (20): 13130-13134.
    • (1991) J Biol Chem , vol.266 , Issue.20 , pp. 13130-13134
    • Wu, H.J.1    Rozansky, D.J.2    Parmer, R.J.3    Gill, B.M.4    O'Connor, D.T.5
  • 79
    • 24344487170 scopus 로고    scopus 로고
    • Pancreastatin: Multiple actions on human intermediary metabolism in vivo, variation in disease, and naturally occurring functional genetic polymorphism
    • O'Connor DT, Cadman PE, Smiley C et al. Pancreastatin: Multiple actions on human intermediary metabolism in vivo, variation in disease, and naturally occurring functional genetic polymorphism. J Clin Endocrinol Metab 2005; 90 (9): 5414-5425.
    • (2005) J Clin Endocrinol Metab , vol.90 , Issue.9 , pp. 5414-5425
    • O'Connor, D.T.1    Cadman, P.E.2    Smiley, C.3
  • 80
    • 0028900087 scopus 로고
    • Increased plasma pancreastatin-like immunoreactivity levels in non-obese patients with essential hypertension
    • Sanchez-Margalet V, Valle M, Lobon JA et al. Increased plasma pancreastatin-like immunoreactivity levels in non-obese patients with essential hypertension. J Hypertens 1995; 13 (2): 251-258.
    • (1995) J Hypertens , vol.13 , Issue.2 , pp. 251-258
    • Sanchez-Margalet, V.1    Valle, M.2    Lobon, J.A.3
  • 81
    • 0343527947 scopus 로고    scopus 로고
    • Characterization of pancreastatin receptor and signaling in rat HTC hepatoma cells
    • Sanchez-Margalet V, Gonzalez-Yanes C, Santos-Alvarez J, Najib S. Characterization of pancreastatin receptor and signaling in rat HTC hepatoma cells. Eur J Pharmacol 2000; 397 (2-3): 229-235.
    • (2000) Eur J Pharmacol , vol.397 , Issue.2-3 , pp. 229-235
    • Sanchez-Margalet, V.1    Gonzalez-Yanes, C.2    Santos-Alvarez, J.3    Najib, S.4
  • 83
    • 0032435902 scopus 로고    scopus 로고
    • Pancreastatin inhibits insulin action in rat adipocytes
    • Sanchez-Margalet V, Gonzalez-Yanes C. Pancreastatin inhibits insulin action in rat adipocytes. Am J Physiol 1998; 275 (6 Pt 1): E1055-E1060.
    • (1998) Am J Physiol , vol.275 , Issue.6 PART 1
    • Sanchez-Margalet, V.1    Gonzalez-Yanes, C.2
  • 85
    • 0025079968 scopus 로고
    • Elevated plasma levels of pancreastatin (PST) in patients with non-insulin-dependent diabetes mellitus (NIDDM)
    • Funakoshi A, Tateishi K, Shinozaki H, Matsumoto M, Wakasugi H. Elevated plasma levels of pancreastatin (PST) in patients with non-insulin-dependent diabetes mellitus (NIDDM). Regul Pept 1990; 30 (2): 159-164.
    • (1990) Regul Pept , vol.30 , Issue.2 , pp. 159-164
    • Funakoshi, A.1    Tateishi, K.2    Shinozaki, H.3    Matsumoto, M.4    Wakasugi, H.5
  • 86
    • 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 et al. Chromogranin A processing and secretion: Specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway. J Clin Invest 1996; 98 (1): 148-156.
    • (1996) J Clin Invest , vol.98 , Issue.1 , pp. 148-156
    • Eskeland, N.L.1    Zhou, A.2    Dinh, T.Q.3
  • 87
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
    • Prigge ST, Mains RE, Eipper BA, Amzel LM. New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function. Cell Mol Life Sci 2000; 57 (8-9): 1236-1259.
    • (2000) Cell Mol Life Sci , vol.57 , Issue.8-9 , pp. 1236-1259
    • Prigge, S.T.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 88
    • 0042924384 scopus 로고    scopus 로고
    • Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter
    • Yasothornsrikul S, Greenbaum D, Medzihradszky KF et al. Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Proc Natl Acad Sci USA 2003; 100 (16): 9590-9595.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.16 , pp. 9590-9595
    • Yasothornsrikul, S.1    Greenbaum, D.2    Medzihradszky, K.F.3
  • 90
    • 0023733506 scopus 로고
    • Isolation and primary structure of tumor-derived peptides related to human pancreastatin and chromogranin A
    • Schmidt WE, Siegel EG, Kratzin H, Creutzfeldt W. Isolation and primary structure of tumor-derived peptides related to human pancreastatin and chromogranin A. Proc Natl Acad Sci USA 1988; 85 (21): 8231-8235.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.21 , pp. 8231-8235
    • Schmidt, W.E.1    Siegel, E.G.2    Kratzin, H.3    Creutzfeldt, W.4
  • 91
    • 0024431959 scopus 로고
    • Isolation and characterization of a tumor-derived human pancreastatin-related protein
    • Funakoshi S, Tamamura H, Ohta M et al. Isolation and characterization of a tumor-derived human pancreastatin-related protein. Biochem Biophys Res Commun 1989; 164 (1): 141-148.
    • (1989) Biochem Biophys Res Commun , vol.164 , Issue.1 , pp. 141-148
    • Funakoshi, S.1    Tamamura, H.2    Ohta, M.3
  • 92
    • 0024404134 scopus 로고
    • Isolation and characterization of bovine pancreastatin
    • Nakano I, Funakoshi A, Miyasaka K et al. Isolation and characterization of bovine pancreastatin. Regul Pept 1989; 25 (2): 207-213.
    • (1989) Regul Pept , vol.25 , Issue.2 , pp. 207-213
    • Nakano, I.1    Funakoshi, A.2    Miyasaka, K.3
  • 93
    • 0025569427 scopus 로고
    • Pancreastatin: Characterization of biological activity
    • Zhang T, Mochizuki T, Kogire M et al. Pancreastatin: Characterization of biological activity. Biochem Biophys Res Commun 1990; 173 (3): 1157-1160.
    • (1990) Biochem Biophys Res Commun , vol.173 , Issue.3 , pp. 1157-1160
    • Zhang, T.1    Mochizuki, T.2    Kogire, M.3


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