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Publication : A novel murine PDGF-D splicing variant results in significant differences in peptide expression and function.

First Author  Zhuo Y Year  2003
Journal  Biochem Biophys Res Commun Volume  308
Issue  1 Pages  126-32
PubMed ID  12890490 Mgi Jnum  J:84792
Mgi Id  MGI:2670240 Doi  10.1016/s0006-291x(03)01346-9
Citation  Zhuo Y, et al. (2003) A novel murine PDGF-D splicing variant results in significant differences in peptide expression and function. Biochem Biophys Res Commun 308(1):126-32
abstractText  Platelet-derived growth factor (PDGF) is a potent mesenchymal cell mitogen and chemoattractant involved in the pathogenesis of fibroproliferative diseases. There are four known PDGF ligand isoforms designated A-D, two of which, C and D, were only recently discovered. We have identified a splicing variant in the PDGF-D isoform that occurs in mice, but not in humans. The presence of the splicing variant in murine PDGF-D appears to be due to an aberration in the splicing site at the junction of exons 5 and 6. The splicing variant results in a deletion predicted to have significant effects on peptide activity since it results in the deletion of bases within the cysteine knot domain that are important for peptide dimerization and receptor binding. It is important to appreciate differences between murine and human PDGF gene expression because PDGF is a key mitogen in the pathogenesis of fibrosis and mice are commonly employed as models for human disease.
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