HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Patel, Y. C. Articles by O'Neil, W. Search for Related Content PubMed PubMed Citation Articles by Patel, Y. C. Articles by O'Neil, W. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 2, 745-751, 01, 1988

Peptides derived from cleavage of prosomatostatin at carboxyl- and amino-terminal segments. Characterization of tissue and secreted forms in the rat

YC Patel and W O'Neil
Fraser Laboratories, McGill University, Department of Medicine, Royal Victoria Hospital, Montreal, Quebec, Canada.

Tissue and secreted forms of rat prosomatostatin and its cleavage products were characterized immunochemically using high performance liquid chromatography and sequence-specific radioimmunoassays directed against somatostatin-14 (S-14), S-28-(1-12), and S-28-(1-14). Acetic or hydrochloric acid extracts of hypothalamus, pancreas, stomach, and jejunum contained seven molecular forms of Mr = 10,400 (corresponding to prosomatostatin (pro-S], Mr = 6,800 (7-kDa peptide, consisting of an NH2-terminally truncated form of pro-S), Mr = 7,600 (8-kDa peptide, corresponding to pro-S-(1-76), i.e. pro-S minus the COOH-terminal -Arg- Lys-S-14), Mr = 5,600 (5-kDa peptide, corresponding to pro-S-(33-76)) and three peptides co-chromatographing with synthetic S-14, S-28, and S- 28-(1-12). Acid/ethanol extracts of these tissues contained pro-S, 8- kDa peptide, S-28, S-14, and S-28-(1-12) forms, but not the 7- and 5- kDa species. Pepstatin inhibited 7- and 5-kDa peptide formation in acetic acid extracts of tissues. The secreted forms consisted of the same five forms present in acid/ethanol or acetic acid plus pepstatin tissue extracts. The 7- and 5-kDa peptides were not secreted and appeared to be derived artifactually, presumably through the action of renin- and cathepsin D-like acid proteases. Accurate quantitation of the 8-kDa peptide by acid/ethanol extraction revealed a variable tissue distribution. Since the presence of the 8-kDa form provides evidence for direct processing of pro-S----S-14 + 8-kDa peptide, the present data suggest that pro-S----S-14 conversion is important for S-14 synthesis in the hypothalamus and pancreas, tissues rich in the 8-kDa form, but not in the stomach and jejunal mucosa, which contain low concentrations of this peptide.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. Scanlan, L. Dufourny, and D. C. Skinner Somatostatin-14 Neurons in the Ovine Hypothalamus: Colocalization with Estrogen Receptor {alpha} and Somatostatin-28(1-12) Immunoreactivity, and Activation in Response to Estradiol Biol Reprod, October 1, 2003; 69(4): 1318 - 1324. [Abstract] [Full Text] [PDF]

				J. W. Ensinck, D. G. Baskin, T. P. Vahl, R. E. Vogel, E. C. Laschansky, B. H. Francis, R. C. Hoffman, J. D. Krakover, M. R. Stamm, M. J. Low, et al. Thrittene, Homologous with Somatostatin-28(1-13), Is a Novel Peptide in Mammalian Gut and Circulation Endocrinology, July 1, 2002; 143(7): 2599 - 2609. [Abstract] [Full Text] [PDF]

				M. A. Sheridan, J. D. Kittilson, and B. J. Slagter Structure-Function Relationships of the Signaling System for the Somatostatin Peptide Hormone Family Integr. Comp. Biol., April 1, 2000; 40(2): 269 - 286. [Abstract] [Full Text] [PDF]

				R. Mouchantaf, U. Kumar, T. Sulea, and Y. C. Patel A Conserved alpha -Helix at the Amino Terminus of Prosomatostatin Serves as a Sorting Signal for the Regulated Secretory Pathway J. Biol. Chem., July 6, 2001; 276(28): 26308 - 26316. [Abstract] [Full Text] [PDF]