Expression of protein kinase C isozymes in primary neuronal cultures of the rat cerebellum

Shimohama, Shun; Uehara-Kunugi, Yukiko; Terai, Kazuhiro; Taniguchi, Takashi; Kimura, Jun; Saitoh, Tsunao

doi:10.1002/jnr.490290217

Cited by 21 publications

(17 citation statements)

References 42 publications

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“…The isoforms a, b1, c, e, d, and f have been previously detected in cerebellum and in cerebellar granule cells (Huang et al. 1988;Shimohama et al 1991;Linden et al 1992;Lin et al 1997;Yang and Kodavanti 2001). PKC c has also been detected in cerebellar granule cells (Lin et al 1997) and the low expression of this isoform in our study is in agreement with the report of Yang and Kodavanti (2001).…”

Section: Discussionsupporting

confidence: 92%

Chronic exposure to ammonia induces isoform‐selective alterations in the intracellular distribution and NMDA receptor‐mediated translocation of protein kinase C in cerebellar neurons in culture

Giordano

Sánchez-Pérez

Burgal

et al. 2004

Journal of Neurochemistry

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Hyperammonemia is responsible for most neurological alterations in patients with hepatic encephalopathy by mechanisms that remain unclear. Hyperammonemia alters phosphorylation of neuronal protein kinase C (PKC) substrates and impairs NMDA receptor-associated signal transduction. The aim of this work was to analyse the effects of hyperammonemia on the amount and intracellular distribution of PKC isoforms and on translocation of each isoform induced by NMDA receptor activation in cerebellar neurons. Chronic hyperammonemia alters differentially the intracellular distribution of PKC isoforms. The amount of all isoforms (except PKC f) was reduced (17-50%) in the particulate fraction. The contents of a, b1, and e isoforms decreased similarly in cytosol (65-78%) and membranes (66-83%), whereas c, d, and h isoforms increased in cytosol but decreased in membranes, and f isoform increased in membranes and decreased in cytosol. Chronic hyperammonemia also affects differentially NMDA-induced translocation of PKC isoforms. NMDA-induced translocation of PKC a and b is prevented by ammonia, whereas PKC c, d, e, or h translocation is not affected. Inhibition of phospholipase C did not affect PKC a translocation but reduced significantly PKC c translocation, indicating that NMDA-induced translocation of PKC a is mediated by Ca 2+ , whereas PKC c translocation is mediated by diacylglycerol. Chronic hyperammonemia reduces Ca +2 -mediated but not diacylglycerol-mediated translocation of PKC isoforms induced by NMDA.

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Section: Discussionsupporting

confidence: 92%

Chronic exposure to ammonia induces isoform‐selective alterations in the intracellular distribution and NMDA receptor‐mediated translocation of protein kinase C in cerebellar neurons in culture

Giordano

Sánchez-Pérez

Burgal

et al. 2004

Journal of Neurochemistry

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“…However, this in vitro observation contrasts with the in vivo situation of the adult hippocampus, where a defined subcellular localization exists for each PKC isozyme [17][18][19]45]. Similar puzzling results have been obtained before in primary cultures of rat cerebellum where neither the expression of different isozymes to different cell populations nor the subcellular localization observed in adult cerebellum is achieved in vitro [46]. It may be that additional signals, probably of extracellular origin, are needed to determine PKC isozyme subcellular localization.…”

Section: Phase Contrastmentioning

confidence: 52%

Expression of protein kinase C isozymes in hippocampal neurones in culture

1995

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Several protein kinase C (PKC) isozymes were analyzed by immunoblot and immunocytochemistry in cultures of hippocampal neurones at several stages of differentiation. Our findings reveal the existence of two distinct patterns of expression. Firstly, conventional PKC isozymes a, /3 and % that are expressed at very low levels during the initial stages and then increase continuously with time of culture. Secondly, novel PKC isozymes 6, ~ and 5, whose contents increase very early to reach a maximum after three days of culture and then progressively decline. Specific proteolysis for PKC isozymes i~ and y was observed throughout the period studied. The developmental profile obtained for the different PKC isozymes is discussed in relation to the differentiation of hippocampal neurones in culture.

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“…PKC for example is largely conWned to brain and neuronal tissue (Cardell et al 1998;Shimohama et al 1991) and a shortened transcript of PKC , PKM to brain as well (Hernandez et al 2003). According to earlier reports PKC was restricted to testis and insulin secreting cells (Selbie et al 1993) and PKC to skeletal muscle and T cells (Berry and Nishizuka 1990;Czerwinski et al 2005;Osada et al 1992).…”

Section: Tissue Distributionmentioning

confidence: 91%

Protein kinase C family: On the crossroads of cell signaling in skin and tumor epithelium

Breitkreutz

Braiman-Wiksman²,

Daum

et al. 2007

J Cancer Res Clin Oncol

128

121

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The protein kinase C (PKC) family represents a large group of phospholipid dependent enzymes catalyzing the covalent transfer of phosphate from ATP to serine and threonine residues of proteins. Phosphorylation of the substrate proteins induces a conformational change resulting in modification of their functional properties. The PKC family consists of at least ten members, divided into three subgroups: classical PKCs (alpha, betaI, betaII, gamma), novel PKCs (delta, epsilon, eta, theta), and atypical PKCs (zeta, iota/lambda). The specific cofactor requirements, tissue distribution, and cellular compartmentalization suggest differential functions and fine tuning of specific signaling cascades for each isoform. Thus, specific stimuli can lead to differential responses via isoform specific PKC signaling regulated by their expression, localization, and phosphorylation status in particular biological settings. PKC isoforms are activated by a variety of extracellular signals and, in turn, modify the activities of cellular proteins including receptors, enzymes, cytoskeletal proteins, and transcription factors. Accordingly, the PKC family plays a central role in cellular signal processing. Accumulating data suggest that various PKC isoforms participate in the regulation of cell proliferation, differentiation, survival and death. These findings have enabled identification of abnormalities in PKC isoform function, as they occur in several cancers. Specifically, the initiation of squamous cell carcinoma formation and progression to the malignant phenotype was found to be associated with distinct changes in PKC expression, activation, distribution, and phosphorylation. These studies were recently further extended to transgenic and knockout animals, which allowed a more direct analysis of individual PKC functions. Accordingly, this review is focused on the involvement of PKC in physiology and pathology of the skin.

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Expression of protein kinase C isozymes in primary neuronal cultures of the rat cerebellum

Cited by 21 publications

References 42 publications

Chronic exposure to ammonia induces isoform‐selective alterations in the intracellular distribution and NMDA receptor‐mediated translocation of protein kinase C in cerebellar neurons in culture

Chronic exposure to ammonia induces isoform‐selective alterations in the intracellular distribution and NMDA receptor‐mediated translocation of protein kinase C in cerebellar neurons in culture

Expression of protein kinase C isozymes in hippocampal neurones in culture

Protein kinase C family: On the crossroads of cell signaling in skin and tumor epithelium

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