Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.13 (protein kinase C)
 49,245 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A novel 78kD phosphoprotein (pp78) of BALB/c 3T3 mouse fibroblasts is reported. Its properties of appearance in late G1 phase, dependence on specific growth factors, and altered constitutive kinetics in benzo(a)pyrene-transformed (BPA31) cells suggest its role in growth and transformation. Pp78 phosphorylation is in a dynamic state and is stabilized by inhibitors of protein and mRNA synthesis, possibly because of inhibition of a labile phosphatase or protease. Its disappearance in S phase and its low level in exponential cells also indicate a dynamic control that is dependent on growth conditions. Enhancement by phorbol myristate acetate indicates that phosphorylation of pp78 is a consequence of protein kinase C activation, but it appears much later than does an 80kD phosphoprotein (pp80), which is a recognized substrate of kinase C. No simple relation between the appearance of pp78 and mitogenesis was found. Two other phosphoproteins varied with growth conditions. One is the pp80 kinase C substrate which was found in the untransformed (A31) 3T3 cells early after stimulation but was absent in BPA31 cells. The other is an 18kD phosphoprotein that appeared shortly after quiescent 3T3 cells were stimulated.
 ...
PMID:Cell cycle and growth factor-dependent phosphoprotein of 78kD differently regulated in normal and transformed mouse fibroblasts. 368 Mar 94

We have utilized several peptide specific antisera directed against the C-terminals (Wetsel et al, 1992) of several protein kinase C (PKC) isozymes (alpha, beta 1, beta 11, gamma, delta, epsilon, zeta) to delineate the cellular localization of these PKC isozymes in rat retina. Antisera against PKC beta 1, beta 11, gamma, delta and epsilon were non-reactive in frozen rat retina sections, whereas, anti PKC alpha was strongly reactive with the outer plexiform, inner plexiform and nerve fiber cell layers. The most specific localization of immunoreactivity was observed with PKC zeta, which reacted strongly and exclusively with photoreceptor inner segments, but not outer segments. Immunoblot analysis of whole rat retina homogenate showed that anti-PKC alpha recognized an antigen of approximately 80kD and anti-PKC zeta recognized a approximately 72kD protein. Immunolocalization of PKC zeta to photoreceptor inner segments and possible functional significance are discussed.
 ...
PMID:Immunolocalization of PKC zeta in rat photoreceptor inner segments. 819 61