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Somatostatin pp 141-154 | Cite as

Anglerfish Pancreatic Islets Produce Two forms of Somatostatin-28

  • Joachim Spiess
  • Bryan D. Noe
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 188)

Abstract

It has been predicted on the basis of cDNA sequence analysis that anglerfish pancreatic islets contain at least two different preprosomatostatins (I and II). The C-terminal amino acid sequences of preprosomatostatin I and II were predicted to be identical to mammalian hypothalamic somatostatin-14 (SS-14) and its analog [Tyr7 ,Gly10]SS-14, respectively. That SS-14 is expressed in anglerfish pancreatic islets, has been shown earlier in pulse-chase experiments and by chemical characterization. However, it was observed that [Tyr7 ,Gly10]SS-14 was not expressed as such, but as part of larger polypeptides.

Pulse-chase experiments combined with reverse-phase high pressure liquid chromatography, amino acid analysis with two different chromatographic systems, and complete Edman degradation indicated that preprosomatostatin II is processed in anglerfish islets to two different forms of somatostatin-28 (SS-28). The primary structure of the major form containing hydroxylysine (Hyl) was determined to be:

H-Ser-Val-Asp-Ser-Thr-Asn-Asn-Leu-Pro-Pro-Arg-Glu-Arg-Lys- Ala-Gly-Cys-Lys-Asn-Phe-Tyr-Trp-Hyl-Gly-Phe-Thr-Ser-Cys-OH

The amino acid sequence of the minor form differs only at residue 23 by substitution of lysine for hydroxylysine. This is the first time that hydroxylysine, an amino acid which characteristically occurs in collagen or collagen-like structures has been identified in a potential regulatory peptide. It can be speculated that this amino acid is formed by post-translational hydroxylation of a lysine C-terminally linked to a glycine residue and thus modified at a site which has been recognized as hydroxylation site in collagen or collagen-like structures. The biological consequences of this unusual modification are being investigated.

Keywords

Amino Acid Analysis Edman Degradation Pituitary Growth Hormone Large Polypeptide Hydroxylation Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1985

Authors and Affiliations

  • Joachim Spiess
    • 1
  • Bryan D. Noe
    • 2
  1. 1.Peptide Biology LaboratoryThe Salk InstituteLa JollaUSA
  2. 2.Department of AnatomyEmory University School of MedicineAtlantaUSA

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