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 Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sánchez-Margalet, V Articles by Goberna, R Search for Related Content PubMed PubMed Citation Articles by Sánchez-Margalet, V Articles by Goberna, R

Pancreastatin is a 49 amino acid peptide first isolated, purified and characterized from the porcine pancreas, and whose biological activity in different tissues can be assigned to the C-terminal part of the molecule. Pancreastatin has a prohormonal precursor, chromogranin A (CGA), which is a glycoprotein present in neuroendocrine cells, including the endocrine pancreas. Both intracellular and extracellular processing of CGA can yield pancreastatin. This processing is tissue-specific, with the pancreatic islet and antral gastric endocrine cells being the major source of fully processed pancreastatin. Most of the circulating CGA is secreted by chromaffin tissue. Therefore, peripheral processing of CGA is probably the major indirect source of pancreastatin. Pancreastatin seems to have a general modulatory control on endocrine (insulin, glucagon, parathormone) and exocrine (pancreatic, gastric) secretion from tissues close to the source of production. This has led to the assumption that pancreastatin may be a peptide with an autocrine and paracrine function. It has recently been revealed to be a peptide with a metabolic function counter-regulatory to insulin action. This effect, in conjunction with the inhibitory effect on insulin and pancreatic exocrine secretion, points to a role in the physiology of stress. The molecular mechanism of the glycogenolytic effect of pancreastatin is better known, although further work is still needed. In general, more studies should be carried out at the molecular level to investigate the mechanism of action of pancreastatin and thus to clarify its physiological role in the neuroendocrine system.

This article has been cited by other articles:

				L. Taupenot, K. L. Harper, and D. T. O'Connor The Chromogranin-Secretogranin Family N. Engl. J. Med., March 20, 2003; 348(12): 1134 - 1149. [Full Text] [PDF]

				L. Taupenot, K. L. Harper, N. R. Mahapatra, R. J. Parmer, S. K. Mahata, and D. T. O'Connor Identification of a novel sorting determinant for the regulated pathway in the secretory protein chromogranin A J. Cell Sci., March 14, 2003; 115(24): 4827 - 4841. [Abstract] [Full Text] [PDF]

				A. Kirschenbaum, D. R. Liotta, S. Yao, X.-H. Liu, A. P. Klausner, P. Unger, E. Shapiro, I. Leav, and A. C. Levine Immunohistochemical Localization of Cyclooxygenase-1 and Cyclooxygenase-2 in the Human Fetal and Adult Male Reproductive Tracts J. Clin. Endocrinol. Metab., September 1, 2000; 85(9): 3436 - 3441. [Abstract] [Full Text]

				V. Sanchez-Margalet and C. Gonzalez-Yanes Pancreastatin inhibits insulin action in rat adipocytes Am J Physiol Endocrinol Metab, December 1, 1998; 275(6): E1055 - E1060. [Abstract] [Full Text] [PDF]

				V. Sanchez-Margalet and J. Santos-Alvarez Solubilization and Molecular Characterization of Active Pancreastatin Receptors from Rat Liver Membranes Endocrinology, April 1, 1997; 138(4): 1712 - 1718. [Abstract] [Full Text] [PDF]