Tissue-specific expression of three distinct types of rabbit protein kinase C

Ohno, Shigeo; Kawasaki, Hiroshi; Imajoh, Shinobu; Suzuki, Koichi; Inagaki, Masaki; Yokokura, Hisayuki; Sakoh, Takashi; Hidaka, Hiroyoshi

doi:10.1038/325161a0

Cited by 464 publications

(178 citation statements)

References 26 publications

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“…These early studies relied upon chromatographic elution profiles and specific activation by phospholipids, diacylglycerol and calcium [72][73][74][75]. In some cases, phorbol ester desensitization was taken as an indication of a role for specific PKC isoforms in insulin action [76].…”

Section: Pkcβiimentioning

confidence: 99%

Specific protein kinase C isoforms as transducers and modulators of insulin signaling

Sampson

Cooper

2006

Molecular Genetics and Metabolism

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Recent studies implicate specific PKC isoforms in the insulin-signaling cascade. Insulin activates PKCsα, βII, δ and ζ in several cell types. In addition, as will be documented in this review, certain members of the PKC family may also be activated and act upstream of PI3 and MAP kinases. Each of these isoforms has been shown one way or another either to mimic or to modify insulin-stimulated effects in one or all of the insulin-responsive tissues. Moreover, each of the isoforms has been shown to be activated by insulin stimulation or conditions important for effective insulin stimulation. Studies attempting to demonstrate a definitive role for any of the isoforms have been performed on different cells, ranging from appropriate model systems for skeletal muscle, liver and fat, such as primary cultures, and cell lines and even in vivo studies, including transgenic mice with selective deletion of specific PKC isoforms. In addition, studies have been done on certain expression systems such as CHO or HEK293 cells, which are far removed from the tissues themselves and serve mainly as vessels for potential protein-protein interactions. Thus, a clear picture for many of the isoforms remains elusive in spite of over two decades of intensive research. The recent intrusion of transgenic and precise molecular biology technologies into the research armamentarium has opened a wide range of additional possibilities for direct involvement of individual isoforms in the insulin signaling cascade. As we hope to discuss within the context of this review, whereas many of the long soughtafter answers to specific questions are not yet clear, major advances have been made in our understanding of precise roles for individual PKC isoforms in mediation of insulin effects. In this review, in which we shall focus our attention on isoforms in the conventional and novel categories, a clear case will be made to show that these isoforms are not only expressed but are importantly involved in regulation of insulin metabolic effects.

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Section: Pkcβiimentioning

confidence: 99%

Specific protein kinase C isoforms as transducers and modulators of insulin signaling

Sampson

Cooper

2006

Molecular Genetics and Metabolism

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“…It is now clear that the general properties used to define the enzyme are shared by a group of related proteins first identified through structural analysis [3][4][5][6][7][8][9]. Among these reports, Housey et al [8] described a partial eDNA clone, RP-16, which was only distantly related to the others.…”

Section: Introductionmentioning

confidence: 99%

Unique substrate specificity and regulatory properties of PKC‐ε: a rationale for diversity

Schaap

Parker

Bristol³

et al. 1989

FEBS Letters

224

128

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PKC-e was isolated from a murine brain eDNA library. The clone, 261PKC-e, encoded a polypeptide of 737 amino acids that is homologous to other PKCs. Northern analysis showed that the 7 kb mRNA for this eDNA is widely expressed. The protein when expressed in COS-1 cells displayed phorbol ester-binding activity. However in order to detect the kinase activity of PKC-e, it was necessary to employ a synthetic peptide substrate based upon the pseudosubstrate site. Subsequent analysis demonstrated that PKC-e, while showing certain properties characteristic of the PKC family, has a quite distinct substrate specificity and is independent of Ca 2 +.

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“…Three kinase activity peaks using chromatographic separation were first described by Huang et al (1986b), which were designated as PKC I, II, and III. A new family of PKC-related genes (a, p, and y) was identified in bovine, human, and rat genomes in 1986 (Coussens et al, 1986) and in rabbit genome in 1987 (Ohno et al, 1987). Three members of the gene family were characterized and mapped to different chromosomal locations (Coussens et al, 1986;Knopf et al, 1986).…”

Section: The Discovery Of Various Pkc Subtypesmentioning

confidence: 99%