AJP - Cell Physiology, Vol 264, Issue 4 C1029-C1036, Copyright © 1993 by American Physiological Society

ARTICLES

Distribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes

L. M. Matovcik, B. Haimowitz, J. R. Goldenring, A. J. Czernik and F. S. Gorelick
Department of Surgery, Department of Veterans Affairs Hospital, West Haven, Connecticut 06516.

Ca2+/calmodulin (CaM)-dependent protein kinase II is a major effector of the Ca2+ signaling pathway. It has a wide tissue distribution and phosphorylates multiple substrates. Villus enterocytes from rat ileum contain a Ca2+/CaM-dependent kinase activity that phosphorylates the exogenous neural substrate synapsin I. This phosphorylation is blocked by a specific peptide inhibitor. Antibodies made to rat brain Ca2+/CaM-dependent protein kinase II label a single band with a relative molecular mass of approximately 50 kDa in isolated rat enterocytes by immunoblot. Almost one-half of this immunoreactive protein is preferentially found in a particulate compared with a soluble subcellular fraction of the enterocytes. Virtually all of the 50-kDa band in the particulate fraction is insoluble in nonionic detergent, suggesting that the kinase is associated with the enterocyte cytoskeleton. Antibodies to Ca2+/CaM-dependent protein kinase II immunocytochemically detect fibrillar structures concentrated in the terminal web region of intestinal epithelial cells that colocalized with myosin II. This enzyme may have a role in regulating the intestinal epithelial cytoskeleton.

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