PMID: 9188065May 1, 1997Paper

Detection and characterization of a protein isoaspartyl methyltransferase which becomes trapped in the extracellular space during blood vessel injury

Journal of Protein Chemistry
D J Weber, P N McFadden

Abstract

Injury to rat blood vessels in vivo was found to release intracellular pools of protein D-aspartyl/L-isoaspartyl carboxyl methyltransferase (PIMT) into the extracellular milieu, where it becomes trapped. This trapped cohort of PIMT is able to utilize radiolabeled S-adenosyl-L-methionine (AdoMet) introduced into the circulation to methylate blood vessel proteins containing altered aspartyl residues. As further shown in this study, methylated substrates are detected only at the specific site of injury. In vitro studies more fully characterized this endogenous PIMT activity in thoracic aorta and inferior vena cava. Methylation kinetics, immunoblotting, and the lability of methylated substrates at mild alkaline pH were used to demonstrate that both types of blood vessel contain an endogenous protein D-aspartyl/L-isoaspartyl carboxyl methyltransferase (PIMT). At least 50% of the PIMT activity is resistant to nonionic detergent extraction, suggesting that the enzyme activity becomes trapped within or behind the extracellular matrix (ECM). Quantities of lactate dehydrogenase (LDH), another soluble enzyme of presumed intracellular origin, were found to be similarly trapped in the extracellular space of blood vessels.

Citations

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

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