Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 20 November 1987:
Vol. 238. no. 4830, pp. 1126 - 1129
DOI: 10.1126/science.2891188
Prev | Table of Contents | Next

Articles

Science, Vol 238, Issue 4830, 1126-1129
Copyright © 1987 by American Association for the Advancement of Science

articles

A new prosomatostatin-derived peptide reveals a pattern for prohormone cleavage at monobasic sites

R Benoit, N Ling, and F Esch

Montreal General Hospital Research Institute, Department of Medicine, McGill University, Quebec, Canada.

Cleavage of the peptide bonds of preprosomatostatin at basic residues near the carboxyl terminus yields somatostatin-14, somatostatin-28, and somatostatin-28 (1-12). However, little is known about the molecular forms derived from the amino terminal portion of the precursor, even though this part of the prohormone is highly conserved through evolution. By using an antibody against the amino terminus of prosomatostatin, a decapeptide with the structure Ala-Pro-Ser-Asp-Pro-Arg-Leu-Arg-Gln-Phe, corresponding to preprosomatostatin (25-34), was isolated from the endocrine portion of the rat stomach, the gastric antrum. The antral decapeptide may represent a bioactive product generated from prosomatostatin after a monobasic cleavage similar to that involved in the formation of somatostatin-28. In fact, a monobasic cleavage requires two basic residues and a domain containing nonpolar amino acids such as alanine or leucine, or both.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Neuronostatin Encoded by the Somatostatin Gene Regulates Neuronal, Cardiovascular, and Metabolic Functions.
W. K. Samson, J. V. Zhang, O. Avsian-Kretchmer, K. Cui, G. L. C. Yosten, C. Klein, R.-M. Lyu, Y. X. Wang, X. Q. Chen, J. Yang, et al. (2008)
J. Biol. Chem. 283, 31949-31959
   Abstract »    Full Text »    PDF »
Disparate Intracellular Processing of Human IL-12 Preprotein Subunits: Atypical Processing of the P35 Signal Peptide.
F. J. Murphy, M. P. Hayes, and P. R. Burd (2000)
J. Immunol. 164, 839-847
   Abstract »    Full Text »    PDF »
Tissue Distribution, Cellular Source, and Structural Analysis of Rat Immunoreactive Uroguanylin.
M. Nakazato, H. Yamaguchi, Y. Date, M. Miyazato, K. Kangawa, M. F. Goy, N. Chino, and S. Matsukura (1998)
Endocrinology 139, 5247-5254
   Abstract »    Full Text »    PDF »
The Mechanism of Inhibition of Ryanodine Receptor Channels by Imperatoxin I, a Heterodimeric Protein from the Scorpion Pandinus imperator.
F. Z. Zamudio, R. Conde, C. Arevalo, B. Becerril, B. M. Martin, H. H. Valdivia, and L. D. Possani (1997)
J. Biol. Chem. 272, 11886-11894
   Abstract »    Full Text »    PDF »
Cloning and Expression of the Chick Anti-Müllerian Hormone Gene.
D.èl. C. Eusèbe, N. di Clemente, R. Rey, C. Pieau, B. Vigier, N. Josso, and J.-Y. Picard (1996)
J. Biol. Chem. 271, 4798-4804
   Abstract »    Full Text »    PDF »
A Conserved alpha -Helix at the Amino Terminus of Prosomatostatin Serves as a Sorting Signal for the Regulated Secretory Pathway.
R. Mouchantaf, U. Kumar, T. Sulea, and Y. C. Patel (2001)
J. Biol. Chem. 276, 26308-26316
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)