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Separate functional features of proinsulin C-peptide
Karolinska Institutet.
Karolinska Institutet.
Karolinska Institutet.
Karolinska Institutet.
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2005 (English)In: Cellular and Molecular Life Sciences (CMLS), ISSN 1420-682X, E-ISSN 1420-9071, Vol. 62, no 15, 1772-1778 p.Article in journal (Refereed) Published
Abstract [en]

Proinsulin C-peptide influences a number of physiological parameters in addition to its well-established role in the parent proinsulin molecule. It is of interest as a candidate for future co-replacement therapy with insulin for patients with diabetes mellitus type 1, but specific receptors have not been identified and additional correlation with functional effects is desirable. Based on comparisons of 22 mammalian proinsulin variants, we have constructed analogues for activity studies, choosing phosphorylation of mitogen-activated protein kinases (MAPKs) in Swiss 3T3 fibroblasts for functional measurements. In this manner, we find that effective phosphorylation of MAPKs is promoted by the presence of conserved glutamic acid residues at positions 3, 11 and 27 of C-peptide and by the presence of helix-promoting residues in the N-terminal segment. Previous findings have ascribed functional roles to the C-terminal pentapeptide segment, and all results combined therefore now show the importance of different segments, suggesting that C-peptide interactions are complex or multiple. © Birkhäuser Verlag, 2005.

Place, publisher, year, edition, pages
2005. Vol. 62, no 15, 1772-1778 p.
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Natural Sciences
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URN: urn:nbn:se:liu:diva-29962DOI: 10.1007/s00018-005-5180-6Local ID: 15389OAI: oai:DiVA.org:liu-29962DiVA: diva2:250781
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2017-12-13

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Persson, Bengt

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