Search: onr:"swepub:oai:DiVA.org:su-50314" >
Oligomerization and...
Oligomerization and insulin interactions of proinsulin C-peptide : Threefold relationships to properties of insulin
-
- Jornvall, Hans (author)
- Karolinska Institutet
-
Lindahl, Emma (author)
-
- Astorga-Wells, Juan (author)
- Karolinska Institutet
-
show more...
-
- Lind, Jesper (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
Holmlund, Anna (author)
-
Melles, Ermias (author)
-
- Alvelius, Gunvor (author)
- Karolinska Institutet
-
Nerelius, Charlotte (author)
-
- Mäler, Lena (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Johansson, Jan (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för anatomi, fysiologi och biokemi,Department of Anatomy, Physiology and Biochemistry (AFB)
-
show less...
-
(creator_code:org_t)
-
- Elsevier BV, 2010
- 2010
- English.
-
In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 391:3, s. 1561-1566
- Related links:
-
https://urn.kb.se/re...
-
show more...
-
https://doi.org/10.1...
-
https://res.slu.se/i...
-
http://kipublication...
-
show less...
Abstract
Subject headings
Close
- Three principally different sites of action have been reported for proinsulin C-peptide, at surface-mediated, intracellular, and extracellular locations. Following up on the latter, we now find that (i) mass spectrometric analyses reveal the presence of the C-peptide monomer in apparent equilibrium with a low-yield set of oligomers in weakly acidic or basic aqueous solutions, even at low peptide concentrations (sub-mu M). It further shows not only C-peptide to interact with insulin oligomers (known before), but also the other way around. (ii) Polyacrylamide gel electrophoresis of C-peptide shows detectable oligomers upon Western blotting. Formation of thioflavin T positive material was also detected. (iii) Cleavage patterns of analogues are compatible with C-peptide as a substrate of insulin degrading enzyme. Combined, the results demonstrate three links with insulin properties, in a manner reminiscent of amyloidogenic peptides and their chaperons in other systems. If so, peripheral C-peptide/insulin interactions, absolute amounts of both peptides and their ratios may be relevant to consider in diabetic and associated diseases.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Proinsulin C-peptide
- Insulin degrading enzyme
- Oligomerization
- Mass spectrometry
- Diabetes types 1 and 2
- Peptide deposits
- NATURAL SCIENCES
- NATURVETENSKAP
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Jornvall, Hans
-
Lindahl, Emma
-
Astorga-Wells, J ...
-
Lind, Jesper
-
Holmlund, Anna
-
Melles, Ermias
-
show more...
-
Alvelius, Gunvor
-
Nerelius, Charlo ...
-
Mäler, Lena
-
Johansson, Jan
-
show less...
- About the subject
-
- NATURAL SCIENCES
-
NATURAL SCIENCES
-
and Biological Scien ...
-
and Biochemistry and ...
- Articles in the publication
-
Biochemical and ...
- By the university
-
Stockholm University
-
Swedish University of Agricultural Sciences
-
Karolinska Institutet