Abstract
We have compared the properties of a rat aorta-derived protein kinase C substrate (p75) with those of 80 kDa kinase C substrates from rat brain (MARCKS) and rabbit aorta (p80). Rat aortic p75 appeared to be closely related to rat brain MARCKS on the basis of: solubility in perchloric acid and trichloroacetic acid, heat stability, isoelectric point (pI ∼ 4.2), overall V8 protease phosphopeptide map, and immunocrossreactivity with an antibody directed against the N-terminal domain of MARCKS. However, p75 could be distinguished from rat brain MARCKS and from the rabbit aorta-derived p80 on the basis of its consistently more rapid electrophoretic mobility in SDS-containing gels, and in terms of a unique proteolytic phosphopeptide found in MARCKS but not in aortic p75. We conclude that p75 probably belongs to the family of protein kinase C substrates represented by MARCKS, and that differences in post-translational processing (glycosylation) or mRNA processing may account for the unique properties of the p75 protein in rat aortic tissue.
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Abbreviations
- p75:
-
75,000 Da protein
- MARCKS:
-
Myristoylated Alanine-Rich C Kinase Substrate
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Zhao, D., Hollenberg, M.D. & Severson, D.L. Comparison of an endogenous protein kinase C substrate in rat aorta with rat brain MARCKS. Mol Cell Biochem 116, 163–169 (1992). https://doi.org/10.1007/BF00299395
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DOI: https://doi.org/10.1007/BF00299395