Abstract
Anglerfish (Lophius piscatorius) Brockmann organs contain a form of somatostatin-14, identical to the hypothalamic tetradecapeptide, and two distinct forms of somatostatin-28, which can be separated by reversed-phase high-pressure liquid chromatography (HPLC). Analysis of the NH2-terminal amino acid sequence and comparison of the ability to incorporate 125I indicate that one of these forms corresponds to an octacosapeptide including in its sequence the (Tyr-7, Gly-10) derivative of somatostatin-14 (somatostatin II). Exposure of this somatostatin-28 species to an endopeptidase activity from the rat brain cortex generates a peptide immunologically related to somatostatin and undistinguishable from synthetic (Tyr-7, Gly-10) somatostatin-14 II by HPLC. This somatostatin-28 II exhibits a potent inhibitory effect on growth hormone release by rat anterior pituitary cells, comparable to the other somatostatin-28 form. Since (Tyr-7, Gly-10) somatostatin-14 II cannot be detected in anglerfish pancreatic islets, these results indicate that somatostatin-28 II represents the terminal active product of prosomatostatin II processing, whose structure was predicted from the cDNA nucleotide sequence corresponding to the second mRNA cloned from anglerfish Brockmann organs [Hobart, P., Crawford, R., Shen, L. P., Pictet, R. & Rutter, W. J. (1980) Nature (London) 288, 137-141].
Full text
PDF



Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Brazeau P., Vale W., Burgus R., Ling N., Butcher M., Rivier J., Guillemin R. Hypothalamic polypeptide that inhibits the secretion of immunoreactive pituitary growth hormone. Science. 1973 Jan 5;179(4068):77–79. doi: 10.1126/science.179.4068.77. [DOI] [PubMed] [Google Scholar]
- Brown M., Rivier J., Vale W. Somatostatin-28: selective action on the pancreatic beta-cell and brain. Endocrinology. 1981 Jun;108(6):2391–2396. doi: 10.1210/endo-108-6-2391. [DOI] [PubMed] [Google Scholar]
- Esch F., Böhlen P., Ling N., Benoit R., Brazeau P., Guillemin R. Primary structure of ovine hypothalamic somatostatin-28 and somatostatin-25. Proc Natl Acad Sci U S A. 1980 Nov;77(11):6827–6831. doi: 10.1073/pnas.77.11.6827. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gluschankof P., Morel A., Gomez S., Nicolas P., Fahy C., Cohen P. Enzymes processing somatostatin precursors: an Arg-Lys esteropeptidase from the rat brain cortex converting somatostatin-28 into somatostatin-14. Proc Natl Acad Sci U S A. 1984 Nov;81(21):6662–6666. doi: 10.1073/pnas.81.21.6662. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gomez S., Morel A., Nicolas P., Cohen P. Regional distribution of the Mr 15,000 somatostatin precursor, somatostatin-28 and somatostatin-14 in the rat brain suggests a differential intracellular processing of the high molecular weight species. Biochem Biophys Res Commun. 1983 Apr 15;112(1):297–305. doi: 10.1016/0006-291x(83)91830-2. [DOI] [PubMed] [Google Scholar]
- Hobart P., Crawford R., Shen L., Pictet R., Rutter W. J. Cloning and sequence analysis of cDNAs encoding two distinct somatostatin precursors found in the endocrine pancreas of anglerfish. Nature. 1980 Nov 13;288(5787):137–141. doi: 10.1038/288137a0. [DOI] [PubMed] [Google Scholar]
- Lauber M., Camier M., Cohen P. Higher molecular weight forms of immunoreactive somatostatin in mouse hypothalamic extracts: evidence of processing in vitro. Proc Natl Acad Sci U S A. 1979 Nov;76(11):6004–6008. doi: 10.1073/pnas.76.11.6004. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mandarino L., Stenner D., Blanchard W., Nissen S., Gerich J., Ling N., Brazeau P., Bohlen P., Esch F., Guillemin R. Selective effects of somatostatin-14, -25 and -28 on in vitro insulin and glucagon secretion. Nature. 1981 May 7;291(5810):76–77. doi: 10.1038/291076a0. [DOI] [PubMed] [Google Scholar]
- Marchalonis J. J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem J. 1969 Jun;113(2):299–305. doi: 10.1042/bj1130299. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meyers C. A., Murphy W. A., Redding T. W., Coy D. H., Schally A. V. Synthesis and biological actions of prosomatostatin. Proc Natl Acad Sci U S A. 1980 Oct;77(10):6171–6174. doi: 10.1073/pnas.77.10.6171. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meyers C. A., Murphy W. A., Redding T. W., Coy D. H., Schally A. V. Synthesis and biological actions of prosomatostatin. Proc Natl Acad Sci U S A. 1980 Oct;77(10):6171–6174. doi: 10.1073/pnas.77.10.6171. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morel A., Chang J. Y., Cohen P. The complete amino-acid sequence of anglerfish somatostatin-28 II. A new octacosapeptide containing the (Tyr7, Gly10) derivative of somatostatin-14 I. FEBS Lett. 1984 Sep 17;175(1):21–24. doi: 10.1016/0014-5793(84)80561-x. [DOI] [PubMed] [Google Scholar]
- Morel A., Lauber M., Cohen P. Selective processing of the 15 000 Mr prosomatostatin by mouse hypothalamic extracts releases the tetradecapeptide. FEBS Lett. 1981 Dec 28;136(2):316–318. doi: 10.1016/0014-5793(81)80643-6. [DOI] [PubMed] [Google Scholar]
- Morel A., Nicolas P., Cohen P. Evidence for a predominant form of Mr = 15,000 prosomatostatin in the mouse hypothalamus. Relationship with somatostatin-14 and -28. J Biol Chem. 1983 Jul 10;258(13):8273–8276. [PubMed] [Google Scholar]
- Noe B. D., Spiess J. Evidence fore biosynthesis and differential post-translational proteolytic processing of different (pre)prosomatostatins in pancreatic islets. J Biol Chem. 1983 Jan 25;258(2):1121–1128. [PubMed] [Google Scholar]
- Noe B. D., Spiess J., Rivier J. E., Vale W. Isolation and characterization of somatostatin from anglerfish pancreatic islet. Endocrinology. 1979 Dec;105(6):1410–1415. doi: 10.1210/endo-105-6-1410. [DOI] [PubMed] [Google Scholar]
- Noe B. D. Synthesis of one form of pancreatic islet somatostatin predominates. J Biol Chem. 1981 Sep 25;256(18):9397–9400. [PubMed] [Google Scholar]
- Pradayrol L., Jörnvall H., Mutt V., Ribet A. N-terminally extended somatostatin: the primary structure of somatostatin-28. FEBS Lett. 1980 Jan 1;109(1):55–58. doi: 10.1016/0014-5793(80)81310-x. [DOI] [PubMed] [Google Scholar]
- Spiess J., Villarreal J., Vale W. Isolation and sequence analysis of a somatostatin-like polypeptide from ovine hypothalamus. Biochemistry. 1981 Mar 31;20(7):1982–1988. doi: 10.1021/bi00510a038. [DOI] [PubMed] [Google Scholar]
- Vale W., Grant G., Amoss M., Blackwell R., Guillemin R. Culture of enzymatically dispersed pituitary cells: functional validation of a method. Endocrinology. 1972 Aug;91(2):562–572. doi: 10.1210/endo-91-2-562. [DOI] [PubMed] [Google Scholar]
- Warren T. G., Shields D. Cell-free biosynthesis of somatostatin precursors: Evidence for multiple forms of preprosomatostatin. Proc Natl Acad Sci U S A. 1982 Jun;79(12):3729–3733. doi: 10.1073/pnas.79.12.3729. [DOI] [PMC free article] [PubMed] [Google Scholar]




