Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway

doi:10.1083/jcb.101.5.1999

This Article

	Full Text (PDF, 2192K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Rosa, P.
	Articles by Huttner, W. B.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Rosa, P.
	Articles by Huttner, W. B.


Social Bookmarking

	What's this?

ARTICLES

Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway

P Rosa, A Hille, RW Lee, A Zanini, P De Camilli and WB Huttner

We report on the biochemical and immunological properties as well as on the cellular and subcellular distribution of two proteins, called secretogranins I and II. These proteins specifically occur in a wide variety of endocrine and neuronal cells that package and sort regulatory peptides into secretory granules. Both secretogranins take the same intracellular route as the peptides and are also sorted into secretory granules. Secretogranins I and II are biochemically and immunologically distinct proteins and differ from chromogranin A. Yet, these three proteins are similar to each other in many respects and therefore constitute one class of proteins. A remarkable feature of this protein class is a very acidic pI, brought about by a high content of acidic amino acids as well as by phosphorylation on serine and sulfation on tyrosine and O-linked carbohydrate. As a result, this class of proteins has a high net negative charge even at the acidic pH of the trans Golgi cisternae. We discuss the possibility that this property of the proteins may point to a role in the packaging of regulatory peptides into secretory granules.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Lu, H., Yang, Y., Allister, E. M., Wijesekara, N., Wheeler, M. B. (2008). The Identification of Potential Factors Associated with the Development of Type 2 Diabetes: A Quantitative Proteomics Approach. Mol. Cell. Proteomics 7: 1434-1451 [Abstract] [Full Text]
Mishiro, E., Sakakibara, Y., Liu, M.-C., Suiko, M. (2006). Differential Enzymatic Characteristics and Tissue-Specific Expression of Human TPST-1 and TPST-2. J Biochem 140: 731-737 [Abstract] [Full Text]
Lee, S.-N., Hwang, J. R., Lindberg, I. (2006). Neuroendocrine Protein 7B2 Can Be Inactivated by Phosphorylation within the Secretory Pathway. J. Biol. Chem. 281: 3312-3320 [Abstract] [Full Text]
Silverman, M. A., Johnson, S., Gurkins, D., Farmer, M., Lochner, J. E., Rosa, P., Scalettar, B. A. (2005). Mechanisms of Transport and Exocytosis of Dense-Core Granules Containing Tissue Plasminogen Activator in Developing Hippocampal Neurons. J. Neurosci. 25: 3095-3106 [Abstract] [Full Text]
Greenwood, T. A., Cadman, P. E., Stridsberg, M., Nguyen, S., Taupenot, L., Schork, N. J., O'Connor, D. T. (2004). Genome-wide linkage analysis of chromogranin B expression in the CEPH pedigrees: implications for exocytotic sympathochromaffin secretion in humans. Physiol. Genomics 18: 119-127 [Abstract] [Full Text]
Beuret, N., Stettler, H., Renold, A., Rutishauser, J., Spiess, M. (2004). Expression of Regulated Secretory Proteins Is Sufficient to Generate Granule-like Structures in Constitutively Secreting Cells. J. Biol. Chem. 279: 20242-20249 [Abstract] [Full Text]
Macchi, P., Hemraj, I., Goetze, B., Grunewald, B., Mallardo, M., Kiebler, M. A. (2003). A GFP-based System to Uncouple mRNA Transport from Translation in a Single Living Neuron. Mol. Biol. Cell 14: 1570-1582 [Abstract] [Full Text]
Coco, S., Calegari, F., Pravettoni, E., Pozzi, D., Taverna, E., Rosa, P., Matteoli, M., Verderio, C. (2003). Storage and Release of ATP from Astrocytes in Culture. J. Biol. Chem. 278: 1354-1362 [Abstract] [Full Text]
Yoo, S. H., You, S. H., Kang, M. K., Huh, Y. H., Lee, C. S., Shim, C. S. (2002). Localization of the Secretory Granule Marker Protein Chromogranin B in the Nucleus. POTENTIAL ROLE IN TRANSCRIPTION CONTROL. J. Biol. Chem. 277: 16011-16021 [Abstract] [Full Text]
Osamura, R. Y., Tahara, S., Kurotani, R., Sanno, N., Matsuno, A., Teramoto, A. (2000). Contributions of Immunohistochemistry and In Situ Hybridization to the Functional Analysis of Pituitary Adenomas. J. Histochem. Cytochem. 48: 445-458 [Abstract] [Full Text]
Calegari, F., Coco, S., Taverna, E., Bassetti, M., Verderio, C., Corradi, N., Matteoli, M., Rosa, P. (1999). A Regulated Secretory Pathway in Cultured Hippocampal Astrocytes. J. Biol. Chem. 274: 22539-22547 [Abstract] [Full Text]
Borglum Jensen, T., Hilsted, L., Rehfeld, J. F. (1999). Library of Sequence-specific Radioimmunoassays for Human Chromogranin A. Clin. Chem. 45: 549-560 [Abstract] [Full Text]
Dannies, P. S. (1999). Protein Hormone Storage in Secretory Granules: Mechanisms for Concentration and Sorting. Endocr. Rev. 20: 3-21 [Abstract] [Full Text]
Mahata, S. K., Mahata, M., Livsey, C. V., Gerdes, H.-H., Huttner, W. B., O’Connor, D. T. (1999). Neuroendocrine Cell Type-Specific and Inducible Expression of the Secretogranin II Gene: Crucial Role of Cyclic Adenosine Monophosphate and Serum Response Elements. Endocrinology 140: 739-749 [Abstract] [Full Text]
Rowe, J, Corradi, N, Malosio, M., Taverna, E, Halban, P, Meldolesi, J, Rosa, P (1999). Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells: prevention by rbSEC1. J. Cell Sci. 112: 1865-1877 [Abstract]
Kiebler, M. A., Hemraj, I., Verkade, P., Kohrmann, M., Fortes, P., Marion, R. M., Ortin, J., Dotti, C. G. (1999). The Mammalian Staufen Protein Localizes to the Somatodendritic Domain of Cultured Hippocampal Neurons: Implications for Its Involvement in mRNA Transport. J. Neurosci. 19: 288-297 [Abstract] [Full Text]
Borgonovo, B., Racchetti, G., Malosio, M., Benfante, R., Podini, P., Rosa, P., Meldolesi, J. (1998). Neurosecretion Competence, an Independently Regulated Trait of the Neurosecretory Cell Phenotype. J. Biol. Chem. 273: 34683-34686 [Abstract] [Full Text]
Watanabe, T., Banno, T., Jeziorowski, T., Ohsawa, Y., Waguri, S., Grube, D., Uchiyama, Y. (1998). Effects of Sex Steroids on Secretory Granule Formation in Gonadotropes of Castrated Male Rats with Respect to Granin Expression. Endocrinology 139: 2765-2773 [Abstract] [Full Text]
Jeng, C.-J., McCarroll, S. A., Martin, T. F.�J., Floor, E., Adams, J., Krantz, D., Butz, S., Edwards, R., Schweitzer, E. S. (1998). Thy-1 Is a Component Common to Multiple Populations of Synaptic Vesicles. JCB 140: 685-698 [Abstract] [Full Text]
Strub, J.-M., Sorokine, O., Van Dorsselaer, A., Aunis, D., Metz-Boutigue, M.-H. (1997). Phosphorylation and O-Glycosylation Sites of Bovine Chromogranin A from Adrenal Medullary Chromaffin Granules and Their Relationship with Biological Activities. J. Biol. Chem. 272: 11928-11936 [Abstract] [Full Text]
Kahler, C. M., Kirchmair, R., Kaufmann, G., Kahler, S. T., Reinisch, N., Fischer-Colbrie, R., Hogue-Angeletti, R., Winkler, H., Wiedermann, C. J. (1997). Inhibition of Proliferation and Stimulation of Migration of Endothelial Cells by Secretoneurin In Vitro. Arterioscler. Thromb. Vasc. Bio. 17: 932-939 [Abstract] [Full Text]
Passafaro, M., Rosa, P., Sala, C., Clementi, F., Sher, E. (1996). N-type Ca2+ Channels Are Present in Secretory Granules and Are Transiently Translocated to the Plasma Membrane during Regulated Exocytosis. J. Biol. Chem. 271: 30096-30104 [Abstract] [Full Text]
Strub, J.-M., Goumon, Y., Lugardon, K., Capon, C., Lopez, M., Moniatte, M., Van Dorsselaer, A., Aunis, D., Metz-Boutigue, M.-H. (1996). Antibacterial Activity of Glycosylated and Phosphorylated Chromogranin A-derived Peptide 173-194 from Bovine Adrenal Medullary Chromaffin Granules. J. Biol. Chem. 271: 28533-28540 [Abstract] [Full Text]
Corradi, N., Borgonovo, B., Clementi, E., Bassetti, M., Racchetti, G., Consalez, G. G., Huttner, W. B., Meldolesi, J., Rosa, P. (1996). Overall Lack of Regulated Secretion in a PC12 Variant Cell Clone. J. Biol. Chem. 271: 27116-27124 [Abstract] [Full Text]
Yanagihara, N., Oishi, Y., Yamamoto, H., Tsutsui, M., Kondoh, J., Sugiura, T., Miyamoto, E., Izumi, F. (1996). Phosphorylation of Chromogranin A and Catecholamine Secretion Stimulated by Elevation of Intracellular Ca2+ in Cultured Bovine Adrenal Medullary Cells. J. Biol. Chem. 271: 17463-17468 [Abstract] [Full Text]
Saito, Y., Maruyama, K., Kawano, H., Hagino-Yamagishi, K., Kawamura, K., Saido, T. C., Kawashima, S. (1996). Molecular Cloning and Characterization of a Novel Form of Neuropeptide Gene as a Developmentally Regulated Molecule. J. Biol. Chem. 271: 15615-15622 [Abstract] [Full Text]
Weber, E., Jilling, T.�s, Kirk, K. L. (1996). Distinct Functional Properties of Rab3A and Rab3B in PC12 Neuroendocrine Cells. J. Biol. Chem. 271: 6963-6971 [Abstract] [Full Text]
Gorr, S.-U., Gorr, S. U. (1996). Differential Storage of Prolactin, Granins (Chromogranin B and Secretogranin II), and Constitutive Secretory Markers in Rat Pituitary GH(4)C(1) Cells. J. Biol. Chem. 271: 3575-3580 [Abstract] [Full Text]
Thomas, J., Stieber, A, Gonatas, N (1994). Two proteins associated with secretory granule membranes identified in chicken regulated secretory cells. J. Cell Sci. 107: 1297-1308 [Abstract]