PMID: 9188066May 1, 1997Paper

Injury-induced enzymatic methylation of aging collagen in the extracellular matrix of blood vessels

Journal of Protein Chemistry
D J Weber, P N McFadden

Abstract

As a result of blood vessel injury, protein D-aspartyl/L-isoaspartyl carboxyl methyltransferase (PIMT), a normally intracellular enzyme, becomes trapped within the meshwork of the vascular extracellular matrix where it can methylate substrate proteins. In this investigation we examined the distribution of such altered aspartyl-containing substrate proteins in the vascular wall. Nearly 90% of all the altered aspartyl residues were inaccessible to intracellular PIMT. Proteins of the extracellular matrix were found to be the major repository of altered aspartyl-containing polypeptides in the blood vessel wall, accounting for approximately 70% of the total amount. Proteolytic cleavage of extracellular matrix proteins with cyanogen bromide (CNBr) revealed that collagens account for most of the altered aspartyl-containing proteins of the ECM. As a consequence of blood vessel injury, both type I and type III collagen along with other proteins were found to become methylated by injury-released PIMT. It is estimated that 1 cm of vein contains on the order of 5 x 10(14) altered aspartyl residues involving between 1% and 5% of the total extracellular protein.

Citations

Oct 4, 2006·The Journal of Biological Chemistry·Flavio CurnisAngelo Corti
Jun 25, 2008·Blood·Angelo CortiRenata Pasqualini
Feb 2, 2011·Journal of Cell Science·Angelo Corti, Flavio Curnis
Jun 10, 1998·Biochemical and Biophysical Research Communications·D J WeberB Caughey
Oct 19, 2006·Clinical Biochemistry·Christopher R McCudden, Virginia B Kraus
Feb 28, 2009·Biochimica Et Biophysica Acta·Diego Ingrosso, Alessandra F Perna

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