| Expression of IGF-binding protein-1 phosphoisoforms in fasted rat skin and its role in regulation of collagen biosynthesis. | |
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MedLine Citation:
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PMID: 12670795 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Insulin-like growth factor-I (IGF-I) is an important stimulator of collagen and glycosaminoglycan (GAG) biosynthesis in tissues. IGF-I activity is modulated by a family of IGF-binding proteins (IGFBPs) with different IGF-I binding affinities. At least IGFBP-1 and IGFBP-2 are known as inhibitors of IGF functions. Some IGFBPs (IGFBP-1, IGFBP-3 and IGFBP-5) may undergo phosphorylation that dramatically increase their affinity for IGF. During fasting of animals there is a significant decrease of the collagen and GAG content of the skin, accompanied by a reduction of plasma IGF-I levels. However, in previous studies we showed that in the skin of fasted rats IGF-I as well as IGFBP-1 and IGFBP-2 expressions were not different, compared to control rat skin, although collagen content was significantly decreased. In the present study we show that fasted rat skin contains similar amounts of IGF-I, IGFBP-3 and IGFBP-1, although extract from fasted rat skin induced inhibition of collagen biosynthesis in cultured fibroblasts, compared to control rat skin extract. Western immunoblot analysis of control and fasted rat skin extracts, using anti-phosphoserine antibodies for immunoprecipitated IGFBP-1 and IGFBP-3, revealed that both proteins are present in phosphorylated form. Although no differences were found in the expression of phosphorylated IGFBP-3 between control and fasted rat skins, that of phosphorylated IGFBP-1 in fasted rat skin extract was higher than in control one. We suggest that there is an increased level of IGFBP-1 phosphoisoform in fasted rat skin, associated with increased affinity for IGF-I. The increase of phosphorylated IGFBP-1 in fasted rat skin tissue may augment IGF-I binding affinity for IGF and decrease its bioavailability for receptor interaction. This mechanism may prevent IGF-I dependent stimulation of fibroblasts to produce extracellular matrix components. The specific expression of IGFBPs and their phosphoisoforms in tissues may play an important role in regulation of IGF-I action during physiologic and pathologic responses. |
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Authors:
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Marzanna Cechowska-Pasko; Jerzy Pałka |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology Volume: 134 ISSN: 1096-4959 ISO Abbreviation: Comp. Biochem. Physiol. B, Biochem. Mol. Biol. Publication Date: 2003 Apr |
Date Detail:
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Created Date: 2003-04-02 Completed Date: 2004-03-08 Revised Date: 2004-11-17 |
Medline Journal Info:
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Nlm Unique ID: 9516061 Medline TA: Comp Biochem Physiol B Biochem Mol Biol Country: England |
Other Details:
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Languages: eng Pagination: 703-11 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Medical Academy of Białystok, 15-230, Białystok, Poland. m.pasko@poczta.fm |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cells, Cultured Child Collagen / biosynthesis* Fasting Fibroblasts / metabolism Gene Expression Regulation* Humans Insulin-Like Growth Factor Binding Protein 1 / analysis*, biosynthesis, physiology* Insulin-Like Growth Factor Binding Protein 3 / analysis Insulin-Like Growth Factor I / analysis Male Phosphorylation Protein Isoforms / analysis, physiology Rats Rats, Wistar Skin / chemistry* |
| Chemical | |
Reg. No./Substance:
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0/Insulin-Like Growth Factor Binding Protein 1; 0/Insulin-Like Growth Factor Binding Protein 3; 0/Protein Isoforms; 67763-96-6/Insulin-Like Growth Factor I; 9007-34-5/Collagen |
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