Publication Date:
1987-11-20
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benoit, R -- Ling, N -- Esch, F -- AM I88II/AM/NIADDK NIH HHS/ -- HD 09690/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1126-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Montreal General Hospital Research Institute, Department of Medicine, McGill University, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2891188" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Hydrolysis
;
Immunologic Techniques
;
Peptide Fragments/physiology
;
Protein Precursors/immunology/*physiology
;
Protein Processing, Post-Translational
;
Rats
;
Somatostatin/immunology/*physiology
;
Stomach/*physiology
;
Structure-Activity Relationship
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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