메뉴 건너뛰기




Volumn 48, Issue 23, 2009, Pages 5254-5262

Proteolytic fragments of chromogranins A and B represent major soluble components of chromaffin granules, illustrated by two-dimensional proteomics with NH2-terminal Edman peptide sequencing and MALDI-TOF MS

Author keywords

[No Author keywords available]

Indexed keywords

BIOACTIVE MOLECULES; CELL-CELL COMMUNICATIONS; CHROMAFFIN; CHROMOGRANIN B; CLEAVAGE SPECIFICITY; DYNAMIC STORAGE; EDMAN SEQUENCING; MALDI TOF MS; NEUROPEPTIDES; PEPTIDE SEQUENCING; PHYSIOLOGICAL FUNCTIONS; PI VALUES; PRECURSOR PROTEINS; PRO-HORMONE PROCESSING; PROTEIN SPOTS; PROTEOLYTIC FRAGMENTS; PROTEOMICS; SECRETORY VESICLES; TWO-DIMENSIONAL GELS;

EID: 67049158431     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9002953     Document Type: Article
Times cited : (18)

References (41)
  • 2
    • 45249083897 scopus 로고    scopus 로고
    • Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression
    • DOI 10.1111/j.1471-4159.2008.05408.x
    • Funkelstein, L., Toneff, T., Hwang, S.-R., Reinheckel, T., Peters, C., and 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. (Pubitemid 351840225)
    • (2008) Journal of Neurochemistry , vol.106 , Issue.1 , pp. 384-391
    • Funkelstein, L.1    Toneff, T.2    Hwang, S.-R.3    Reinheckel, T.4    Peters, C.5    Hook, V.6
  • 3
    • 56349112732 scopus 로고    scopus 로고
    • Differential activation of enkephalin, galanin, somatostatin, NPY, and VIP neuropeptide production by stimulators of protein kinases A and C in neuroendocrine chromaffin cells
    • Hook, V., Toneff, T., Baylon, S., and Sei, C. (2008) Differential activation of enkephalin, galanin, somatostatin, NPY, and VIP neuropeptide production by stimulators of protein kinases A and C in neuroendocrine chromaffin cells. Neuropeptides 42, 503-511.
    • (2008) Neuropeptides , vol.42 , pp. 503-511
    • Hook, V.1    Toneff, T.2    Baylon, S.3    Sei, C.4
  • 4
    • 0037024611 scopus 로고    scopus 로고
    • Neuropeptides and chromogranins: Session overview
    • Laslop, A., and Mahata, S. K. (2002) Neuropeptides and chromogranins: Session overview. Ann. N.Y. Acad. Sci. 971, 294-299.
    • (2002) Ann. N.Y. Acad. Sci. , vol.971 , pp. 294-299
    • Laslop, A.1    Mahata, S.K.2
  • 5
    • 0027369401 scopus 로고
    • The adrenal chromaffin granule: A model for large dense core vesicles of endocrine and nervous tissue
    • Winkler, H. (1993) The adrenal chromaffin granule: A model for large dense core vesicles of endocrine and nervous tissue. J. Anat. 183, 237-252. (Pubitemid 23299976)
    • (1993) Journal of Anatomy , vol.183 , Issue.2 , pp. 237-252
    • Winkler, H.1
  • 6
    • 3042791268 scopus 로고    scopus 로고
    • The proinflammatory cytokines tumor necrosis factor-R and interleukin-1 stimulate neuropeptide gene transcription and secretion in adrenochromaffin cells via activation of extracellularly regulated kinase 1/2 and p38 protein kinases, and activator protein-1 transcription factors
    • Ait-Ali, D., Turquier, V., Grumolato, L., Yon, L., Jourdain, M., Alexandre, D., Eiden, L. E., Vaudry, H., and Anouar, Y. (2004) The proinflammatory cytokines tumor necrosis factor-R and interleukin-1 stimulate neuropeptide gene transcription and secretion in adrenochromaffin cells via activation of extracellularly regulated kinase 1/2 and p38 protein kinases, and activator protein-1 transcription factors. Mol. Endocrinol. 18, 1721-1739.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1721-1739
    • Ait-Ali, D.1    Turquier, V.2    Grumolato, L.3    Yon, L.4    Jourdain, M.5    Alexandre, D.6    Eiden, L.E.7    Vaudry, H.8    Anouar, Y.9
  • 7
    • 10944250163 scopus 로고    scopus 로고
    • A dynamic pool of calcium in catecholamine storage vesicles. Exploration in living cells by a novel vesicle-targeted chromogranin A-aequorin chimeric photoprotein
    • Mahapatra, N. R., Mahata, M., Hazra, P. P., McDonough, P. M., O'Connor, D. T., and Mahat, S. K. (2004) A dynamic pool of calcium in catecholamine storage vesicles. Exploration in living cells by a novel vesicle-targeted chromogranin A-aequorin chimeric photoprotein. J. Biol. Chem. 279, 51107-51121.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51107-51121
    • Mahapatra, N.R.1    Mahata, M.2    Hazra, P.P.3    McDonough, P.M.4    O'Connor, D.T.5    Mahat, S.K.6
  • 8
    • 0026783755 scopus 로고
    • Calcium and catecholamine interactions with adrenal chromogranins. Comparison of driving forces in binding and aggregation
    • Videen, J. S., Mezger, M. S., Chang, Y. M., O'Connor, D. T., Mezger, M. S., Chang, Y. M., and O'Connor, D. T. (1992) Calcium and catecholamine interactions with adrenal chromogranins. Comparison of driving forces in binding and aggregation. J. Biol. Chem. 267, 3066-3073.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3066-3073
    • Videen, J.S.1    Mezger, M.S.2    Chang, Y.M.3    O'Connor, D.T.4    Mezger, M.S.5    Chang, Y.M.6    O'Connor, D.T.7
  • 9
    • 0029119333 scopus 로고
    • Mechanisms of catecholamine secretion from adrenal chromaffin cells
    • Burgoyne, R. D. (1995) Mechanisms of catecholamine secretion from adrenal chromaffin cells. J. Physiol. Pharmacol. 46, 273-283.
    • (1995) J. Physiol. Pharmacol. , vol.46 , pp. 273-283
    • Burgoyne, R.D.1
  • 10
    • 0023802985 scopus 로고
    • Control of exocytosis from adrenal chromaffin cells
    • Holz, R. W. (1988) Control of exocytosis from adrenal chromaffin cells. Cell. Mol. Neurobiol. 8, 259-268.
    • (1988) Cell. Mol. Neurobiol. , vol.8 , pp. 259-268
    • Holz, R.W.1
  • 11
    • 0037470083 scopus 로고    scopus 로고
    • Neuroendocrine pharmacology of stress
    • Carrasco, G. A., and Van de Kar, L. D. (2003) Neuroendocrine pharmacology of stress. Eur. J. Pharmacol. 463, 235-272.
    • (2003) Eur. J. Pharmacol. , vol.463 , pp. 235-272
    • Carrasco, G.A.1    Van De Kar, L.D.2
  • 13
    • 0029554361 scopus 로고
    • A novel sympathetic stress hormone and more
    • Zukowska-Grojec, Z. (1995) A novel sympathetic stress hormone and more. Ann. N.Y. Acad. Sci. 771, 219-233.
    • (1995) Ann. N.Y. Acad. Sci. , vol.771 , pp. 219-233
    • Zukowska-Grojec, Z.1
  • 14
    • 38549131692 scopus 로고    scopus 로고
    • Diseases of the adrenal medulla
    • DOI 10.1111/j.1748-1716.2007.01809.x
    • Fung, M. M., Viveros, O. H., and O'Connor, D. T. (2008) Diseases of the adrenal medulla. Acta Physiol. 192, 325-335. (Pubitemid 351160993)
    • (2008) Acta Physiologica , vol.192 , Issue.2 , pp. 325-335
    • Fung, M.M.1    Viveros, O.H.2    O'Connor, D.T.3
  • 17
    • 0038394566 scopus 로고    scopus 로고
    • Precursor convertases in the secretory pathway, cytosol and extracellular milieu
    • Seidah, N. G., and Prat, A. (2002) Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem. 38, 79-94. (Pubitemid 36589196)
    • (2002) Essays in Biochemistry , vol.38 , pp. 79-94
    • Seidah, N.G.1    Prat, A.2
  • 18
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou, A., Webb, G., Zhu, X., and Steiner, D. F. (1999) Proteolytic processing in the secretory pathway. J. Biol. Chem. 274, 20745-20748.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 19
    • 0031982551 scopus 로고    scopus 로고
    • Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: Relevance to prohormone processing
    • Yasothornsrikul, S., Toneff, T., Hwang, S.-R., and Hook, V. Y. H. (1998) Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: Relevance to prohormone processing. J. Neurochem. 70, 153-163. (Pubitemid 28020839)
    • (1998) Journal of Neurochemistry , vol.70 , Issue.1 , pp. 153-163
    • Yasothornsrikul, S.1    Toneff, T.2    Hwang, S.-R.3    Hook, V.Y.H.4
  • 20
    • 0038131826 scopus 로고    scopus 로고
    • Primary sequence characterization of catestatin intermediates and peptides defines proteolytic cleavage sites utilized for converting chromogranin a into active catestatin secreted from neuroendocrine chromaffin cells
    • DOI 10.1021/bi0300433
    • Lee, J. C., Taylor, C. V., Gaucher, S. P., Toneff, T., Taupenot, L., Yasothornsrikul, S., Mahata, S. K., Sei, C., Parmer, R. J., Neveu, J. M., Lane, W. S., Gibson, B. W., O'Connor, D. T., and Hook, V. Y. H. (2003) Primary sequence characterization of catestatin intermediates and peptides defines proteolytic cleavage sites utilized for converting chromogranin A into active catestatin secreted from neuroendocrine chromaffin cells. Biochemistry 42, 6938-6946. (Pubitemid 36706476)
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 6938-6946
    • Lee, J.C.1    Taylor, C.V.2    Gaucher, S.P.3    Toneff, T.4    Taupenot, L.5    Yasothornsrikul, S.6    Mahata, S.K.7    Sei, C.8    Parmer, R.J.9    Neveu, J.M.10    Lane, W.S.11    Gibson, B.W.12    O'Connor, D.T.13    Hook, V.Y.H.14
  • 21
    • 0036211823 scopus 로고    scopus 로고
    • RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database
    • DOI 10.1002/1615-9861(200201)2:1<36::AID-PROT36>3.0.CO;2-W
    • Field, H. I., Fenyo, D., and Beavis, R. C. (2002) RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database. Proteomics 2, 36-47. (Pubitemid 34273097)
    • (2002) Proteomics , vol.2 , Issue.1 , pp. 36-47
    • Field, H.I.1    Fenyo, D.2    Beavis, R.C.3
  • 22
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567. (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 23
    • 0029053727 scopus 로고
    • Rapid mass spectrometric peptide sequencing and mass matching for characterization of human melanoma proteins isolated by two-dimensional PAGE
    • Clauser, K. R., Hall, S. C., Smith, D. M., Webb, J. W., Andrew, L. E., Tran, H. M., Epstein, L. B., and Burlingame, A. (1995) Rapid mass spectrometric peptide sequencing and mass matching for characterization of human melanoma proteins isolated by two-dimensional PAGE. Proc. Natl. Acad. Sci. U.S.A. 92, 5072-5076.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5072-5076
    • Clauser, K.R.1    Hall, S.C.2    Smith, D.M.3    Webb, J.W.4    Andrew, L.E.5    Tran, H.M.6    Epstein, L.B.7    Burlingame, A.8
  • 24
    • 0020046010 scopus 로고
    • A carboxypeptidase processing enzyme for enkephalin precursors
    • Hook, V. Y. H., Eiden, L. E., and Brownstein, M. J. (1982) A carboxypeptidase processing enzyme for enkephalin precursors. Nature 295, 341-342. (Pubitemid 12159271)
    • (1982) Nature , vol.295 , Issue.5847 , pp. 341-342
    • Hook, V.Y.H.1    Eiden, L.E.2    Brownstein, M.J.3
  • 26
    • 0023655990 scopus 로고
    • Production inhibition of carboxypeptidase H
    • Hook, V. Y. H., and LaGamma, E. F. (1987) Production inhibition of carboxypeptidase H. J. Biol. Chem. 262, 12583-12588.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12583-12588
    • Hook, V.Y.H.1    LaGamma, E.F.2
  • 27
    • 0021803993 scopus 로고
    • Selective regulation of carboxypeptidase peptide hormone-processing enzyme during enkephalin biosynthesis in cultured bovine adrenomedullary chromaffin cells
    • Hook, V. Y. H., Eiden, L. E., and Pruss, R. M. (1985) Selective regulation of carboxypeptidase peptide hormone-processing enzyme during enkephalin biosynthesis in cultured bovine adrenomedullary chromaffin cells. J. Biol. Chem. 260, 5991-5997.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5991-5997
    • Hook, V.Y.H.1    Eiden, L.E.2    Pruss, R.M.3
  • 28
    • 0023864209 scopus 로고
    • Carboxypeptidase E
    • Fricker, L. D. (1988) Carboxypeptidase E. Annu. Rev. Physiol. 50, 309-321.
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 309-321
    • Fricker, L.D.1
  • 31
    • 0026537856 scopus 로고
    • Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour
    • Curry, W. J., Shaw, C., Johnston, C. F., Thim, L., and Buchanan, K. D. (1992) Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour. FEBS Lett. 301, 319-321.
    • (1992) FEBS Lett. , vol.301 , pp. 319-321
    • Curry, W.J.1    Shaw, C.2    Johnston, C.F.3    Thim, L.4    Buchanan, K.D.5
  • 32
    • 0025690249 scopus 로고
    • A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in the bovine adrenomedullary chromaffin vesicle
    • Flanagan, T., Taylor, L., Poulter, L., Viveros, O. H., and Diliberto, E. J. (1990) A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in the bovine adrenomedullary chromaffin vesicle. Cell. Mol. Neurobiol. 10, 507-523.
    • (1990) Cell. Mol. Neurobiol. , vol.10 , pp. 507-523
    • Flanagan, T.1    Taylor, L.2    Poulter, L.3    Viveros, O.H.4    Diliberto, E.J.5
  • 33
    • 85047690831 scopus 로고
    • Processing of chromogranin B in bovine adrenal medulla, identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity
    • Strub, J. M., Garcia-Sabone, P., Lonning, K., Taupenot, L., Hubert, P., Van Dorsselaer, A., Aunis, D., and Metz-Boutique, M. H. (1995) Processing of chromogranin B in bovine adrenal medulla, identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity. Eur. J. Biochem. 229, 356-368.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 356-368
    • Strub, J.M.1    Garcia-Sabone, P.2    Lonning, K.3    Taupenot, L.4    Hubert, P.5    Van Dorsselaer, A.6    Aunis, D.7    Metz-Boutique, M.H.8
  • 34
    • 0034825159 scopus 로고    scopus 로고
    • Identification and characterization of novel chromogranin B-derived peptides from porcine chromaffin granules by liquid chromatography/electrospray tandem MS
    • Wang, Z., Vandenberghe, I., Depreitere, J., Devreese, B., Clerens, S., Nouwen, E. J., Van Beeumen, J., and de Potter, W. (2001) Identification and characterization of novel chromogranin B-derived peptides from porcine chromaffin granules by liquid chromatography/electrospray tandem MS. Eur. J. Biochem. 268, 235-242.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 235-242
    • Wang, Z.1    Vandenberghe, I.2    Depreitere, J.3    Devreese, B.4    Clerens, S.5    Nouwen, E.J.6    Van Beeumen, J.7    De Potter, W.8
  • 35
    • 0035943417 scopus 로고    scopus 로고
    • Chromogranin A, an "on/off" switch controlling dense core secreotry granule biogenesis
    • Kim, T., Tao-Chen, J. H., Eiden, L. E., and Loh, Y. P. (2001) Chromogranin A, an "on/off" switch controlling dense core secreotry granule biogenesis. Cell 106, 499-509.
    • (2001) Cell , vol.106 , pp. 499-509
    • Kim, T.1    Tao-Chen, J.H.2    Eiden, L.E.3    Loh, Y.P.4
  • 36
    • 0037024652 scopus 로고    scopus 로고
    • Large dense core secretory granule biogensis is under the control of chromogranin a in neuroendocrine cells
    • Kim, T., Tao-Cheng, J. H., Eiden, L. E., and Loh, Y. P. (2002) Large dense core secretory granule biogensis is under the control of chromogranin A in neuroendocrine cells. Ann. N.Y. Acad. Sci. 971, 323-331.
    • (2002) Ann. N.Y. Acad. Sci. , vol.971 , pp. 323-331
    • Kim, T.1    Tao-Cheng, J.H.2    Eiden, L.E.3    Loh, Y.P.4
  • 37
    • 23044488803 scopus 로고    scopus 로고
    • Chromogranin a deficiency in transgenic mice leads to aberrant chromaffin granule biogenesis
    • DOI 10.1523/JNEUROSCI.1058-05.2005
    • Kim, T., Zhang, C. F., Sun, Z., Wu, H., and Loh, Y. P. (2005) Chromogranin A deficiency in transgenic mice leads to aberrant chromaffin granule biogenesis. J. Neurosci. 25, 6958-6961. (Pubitemid 41077003)
    • (2005) Journal of Neuroscience , vol.25 , Issue.30 , pp. 6958-6961
    • Kim, T.1    Zhang, C.-F.2    Sun, Z.3    Wu, H.4    Loh, Y.P.5
  • 38
    • 34249295158 scopus 로고    scopus 로고
    • Proteomics of neuroendocrine secretory vesicles reveal distinct functional systems for biosynthesis and exocytosis of peptide hormones and neurotransmitters
    • DOI 10.1021/pr060503p
    • Wegrzyn, J., Lee, J., Neveu, J. M., Lane, W. S., and Hook, V. (2007) Proteomics of neuroendocrine secretory vesicles reveal distinct functional systems for biosynthesis and exocytosis of peptide hormones and neurotransmitters. J. Proteome Res. 6, 1652-1665. (Pubitemid 46814490)
    • (2007) Journal of Proteome Research , vol.6 , Issue.5 , pp. 1652-1665
    • Wegrzyn, J.1    Lee, J.2    Neveu, J.M.3    Lane, W.S.4    Hook, V.5
  • 41


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.