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Endocrinology, Vol 130, 3427-3432, Copyright © 1992 by Endocrine Society

ARTICLES

Purification and sequencing of molluscan insulin-related peptide II from the neuroendocrine light green cells in Lymnaea stagnalis

KW Li, WP Geraerts and J Joosse
Faculty of Biology, Vrije Universiteit, Amsterdam, The Netherlands.

The growth-controlling neuroendocrine light green cells of the freshwater snail, Lymnaea stagnalis, express a family of genes encoding structurally related, yet distinct, molluscan insulin-related peptides (MIPs). In the present study one of these peptides, MIP II, has been isolated and structurally identified. MIP II is a heterodimer of A and B chains connected by disulfide bonds. Both chains are N-terminally blocked with pyroglutamate. After cleaving of the A and B chains and deblocking with pyroglutamate amino-peptidase their sequences have been determined as: A chain: pQRTTNLVCECCFNYCTPDVVRKYCY and B chain: pQSSCSLSSRPHPRGICGSNLAGFRAFICSNQNSPS. In comparison with the MIP II sequence based on complementary DNA studies, it is clear that the two C- terminal amino acid residues of the B chain are posttranslationally removed. In addition, the glutamic acid residue in A chain was recovered in very low yields during Edman degradation, suggesting that the residue may be posttranslationally modified.


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K Hamano, M Awaji, and H Usuki
cDNA structure of an insulin-related peptide in the Pacific oyster and seasonal changes in the gene expression
J. Endocrinol., October 1, 2005; 187(1): 55 - 67.
[Abstract] [Full Text] [PDF]


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