Douglas Sawyer
Faculty Member
Last active: 7/21/2014

26S proteasome regulation of Ankrd1/CARP in adult rat ventricular myocytes and human microvascular endothelial cells.

Samaras SE, Chen B, Koch SR, Sawyer DB, Lim CC, Davidson JM
Biochem Biophys Res Commun. 2012 425 (4): 830-5

PMID: 22892129 · PMCID: PMC3460693 · DOI:10.1016/j.bbrc.2012.07.162

Ankyrin repeat domain 1 protein (Ankrd1), also known as cardiac ankyrin repeat protein (CARP), increases dramatically after tissue injury, and its overexpression improves aspects of wound healing. Reports that Ankrd1/CARP protein stability may affect cardiovascular organization, together with our findings that the protein is crucial to stability of the cardiomyocyte sarcomere and increased in wound healing, led us to compare the contribution of Ankrd1/CARP stability to its abundance. We found that the 26S proteasome is the dominant regulator of Ankrd1/CARP degradation, and that Ankrd1/CARP half-life is significantly longer in cardiomyocytes (h) than endothelial cells (min). In addition, higher endothelial cell density decreased the abundance of the protein without affecting steady state mRNA levels. Taken together, our data and that of others indicate that Ankrd1/CARP is highly regulated at multiple levels of its expression. The striking difference in protein half-life between a muscle and a non-muscle cell type suggests that post-translational proteolysis is correlated with the predominantly structural versus regulatory role of the protein in the two cell types.

Published by Elsevier Inc.

MeSH Terms (15)

Animals Cell Count Cells, Cultured Endothelium, Vascular Half-Life Heart Ventricles Humans Microvessels Muscle Proteins Myocytes, Cardiac Nuclear Proteins Proteasome Endopeptidase Complex Proteolysis Rats Repressor Proteins

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