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Proinsulin and somatostatin from the islet organ of the southern-hemisphere lamprey Geotria australis

Conlon, J.M., Nielsen, P.F., Youson, J.H. and Potter, I.C. (1995) Proinsulin and somatostatin from the islet organ of the southern-hemisphere lamprey Geotria australis. General and Comparative Endocrinology, 100 (3). pp. 413-422.

Link to Published Version: http://dx.doi.org/10.1006/gcen.1995.1172
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Abstract

An extract of the islet organ of the southern-hemisphere lamprey Geotria australis contained a high concentration of somatostatin like immunoreactivity (34 nmol/g) but only trace amounts of insulin-like immunoreactivity. The primary structure of Geotria somatostatin-33 (AVQEAGGAAM10PPPGQRDRKA20 GCKNFFWKTF30SSC) shows almost no similarity to somatostatins from the holarctic lampreys Petromyzon marinus and Lampetra fluviatilis in the N-terminal region but the functionally important C-terminal region, including the substitution Thr31 → Ser, is the same. Insulin was not identified in the extract but proinsulin and an incompletely processed form with an intact A-chain/C-peptide junction were purified and partially characterized. The primary structure of the insulin region of Geotria proinsulin was established as A-chain; GIVEKCCHNR10CSIYQ MESYC20N; B-chain: SALTGSGGNY10LCGSYLVDAL20YLACGPRGFF30YTSTPV. This sequence contains 17 amino acid substitutions compared with the identical insulins from P. marinus and L. fluviatilis but the unusual extension to the N-terminus of the B-chain (SALTG) is present. Compared with mammalian insulins, Geotria insulin contains several substitutions of strongly conserved residues such as GinA5 → Lys in the putative receptor-binding region, GluB26 → Pro important in dimerization, and LeuA13 → Ile, HisB10 → Tyr, and HisB21 → Tyr important in hexamerization. Geotria proinsulin contains an Arg-Arg processing site at the B-chain/C-peptide junction but we speculate either that the Lys-Arg processing site at the C-peptide/A-chain junction is absent or that the Geotria pancreas is unable to synthesize a SPC2-type prohormone convertase. Our results are consistent with the view that G. australis and holarctic lampreys arose from a common stock but have been separated for a considerable period.

Item Type: Journal Article
Murdoch Affiliation(s): School of Biological and Environmental Sciences
Publisher: Academic Press Inc.
Copyright: © 1995 Academic Press
URI: http://researchrepository.murdoch.edu.au/id/eprint/19652
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