PMID: 9185174Jul 1, 1997Paper

Protein kinase C from bat brain: the enzyme from a hibernating mammal

Neurochemistry International
H Mehrani, Kenneth B Storey

Abstract

Protein kinase C (PKC) from brain of euthermic and hibernating bats (Myotis lucifugus) showed only one form as determined by hydroxylapatite chromatography, compared with three forms found in rat brain. Cross-reaction with antibodies to rabbit alpha, beta, and gamma isozymes showed that bat brain contained only PKC(gamma). During hibernation the activity of PKC in bat brain decreased to 63% of the euthermic value but the percentage that was membrane-associated did not change. Bat and rat brain PKC(gamma) were purified to homogeneity. Both enzymes phosphorylated all three of the substrates tested (FKKSFKL-NH2 peptide substrate, histone H1, protamine), the bat enzyme having significantly higher K(m) values than rat PKC for both peptide and histone. Both enzymes required phospholipids and Ca2+ for activation with rat brain PKC depending almost exclusively on phosphatidylserine. Bat PKC, however, made use of other phospholipids and showed relative activities of 100:81:33:42 for euthermic PKC and 100:91:45:35 for hibernator PKC with phosphatidylserine, phosphatidylinositol, phosphatidylcholine, and phosphatidylethanolamine (each at 50 microM), respectively. Activation of bat PKC by phosphatidylserine was temperature sensitive, being...Continue Reading

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Citations

Oct 3, 2002·Journal of Neurochemistry·Moonyong LeeKyoungsook Park
Apr 9, 2011·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·Jessica E HealyGregory L Florant
Nov 17, 2004·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Kenneth B Storey
Jul 10, 2012·Cryobiology·Khalil AbnousKenneth B Storey
Dec 5, 1998·Archives of Biochemistry and Biophysics·C P Holden, K B Storey
Oct 30, 2007·Archives of Biochemistry and Biophysics·Justin A MacDonald, Kenneth B Storey

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