A novel phorbol ester receptor/protein kinase, nPKC, distantly related to the protein kinase C family

Ohno, Shigeo; Akita, Yoshiko; Konno, Yasuhiko; Imajoh, Shinobu; Suzuki, Koichi

doi:10.1016/0092-8674(88)90091-8

Cited by 408 publications

(191 citation statements)

References 45 publications

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“…This mRNA species corresponds to that identified with an RP16 probe [8] and more recently with rat [10] and rabbit [11] PKC-• cDNAs (see below).…”

Section: Tissue Distribution Of Pkc-esupporting

confidence: 73%

“…In order to define the relationship of this gene product to the PKC family of proteins and determine its biochemical properties, we have isolated a eDNA of this clone. The sequence of this clone is highly homologous to two recently published PKC-e eDNA clones [10,11], and is therefore also named PKC-e. By using a synthetic peptide as a substrate, based upon the putative pseudosubstrate site of PKC-e, we have been able to partially purify PKC-E. The initial characteristics of this kinase are shown to be different from PKC-~, -B1, -/32, and…”

Section: Introductionmentioning

confidence: 81%

“…The authors conclude from these studies that PKC-E shows completely different regulatory features compared to other PKC subtypes; this is clearly at variance with the data reported here for the murine clone. Also recently Ohno et al [11] reported the cDNA cloning of PKC-e from rabbit. These authors also find a PKC-e protein that essentially co-elutes with the endogenous PKC-a on anionexchange chromatography.…”

Section: Tdvcngrki Ela~ I G~'ddfvanct I Qfeellqngsrrfedwi Dlepe ~ Idlmentioning

confidence: 99%

See 2 more Smart Citations

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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“…This mRNA species corresponds to that identified with an RP16 probe [8] and more recently with rat [10] and rabbit [11] PKC-• cDNAs (see below).…”

Section: Tissue Distribution Of Pkc-esupporting

confidence: 73%

Section: Introductionmentioning

confidence: 81%

Section: Tdvcngrki Ela~ I G~'ddfvanct I Qfeellqngsrrfedwi Dlepe ~ Idlmentioning

confidence: 99%

See 1 more Smart Citation

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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“…Initially, PKC was described as a Ca 2+-and phospholipid-dependent serine/threonine kinase [4,5], and later it was shown to be the major intracellular receptor for the tumorpromoting phorbol esters [6,7]. cDNA cloning and careful examination of the encoded proteins has revealed that the members of the PKC family can be classified into three major groups, namely, classical, cPKCs-c~, -/31, -1~II and -y, [8]; novel, nPKCs-~, -e, -/7, -0, and -¢t [9][10][11][12][13][14][15]; and atypical, aPKCs -5 and -t (the human counterpart of mouse aPKC-2) [10,1618]. Only the cPKCs require Ca 2+ for activity.…”

Section: Introductionmentioning

confidence: 99%

Identification of the primary growth response gene, ST2/T1, as a gene whose expression is differentially regulated by different protein kinase C isozymes

Kieser¹,

Goodnight²,

Kölch³

et al. 1995

FEBS Letters

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kbstract Individual protein kinase C isozymes have been shown Io play different roles in mediating proliferation, differentiation and transformation, but it is not known to what extent these effects involve induction of expression of particular genes. To explore the differential gene expression that might be induced by activation of different PKC isozymes, we stably transfected NIH 3T3 cells with expression vectors that encode the isozymes PKC-~, -Eli, -V, -~i, -c, -~ and -~l. Using differential display-reverse transcription-polymerase chain reaction we isolated a small eDNA that encodes a portion of the primary response gene, ST2 (also referred to as T1 or DER4), and we confirmed by RNA blot studies that ST2fYI expression is differentially regulated by PKC isozymes. ST2/TI mRNA is undetectable in the unstimulated parental NIH 3T3 cells that express only the a isozyme of PKC, but it can be induced by phorbol ester treatment. Clones that overexpress PKC-a, -5 or -e similarly do not express ST2/TI until they are stimulated with phorbol esters, which induces expression of ST2/TI with kinetics similar to wild-type NIH 3T3 but to different extents. In contrast, ST2/TI mRNA is already present in unstimulated cells that overexpress PKC-~III, -V, -~ and -~l, but phorbol ester greatly enhances ST2frl expression in these cells. These results suggest a differential role for PKC isozymes in mediating the ST2ffl expression that is induced by growth stimuli.

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“…The characterisation of the PKC isoenzyme encoded by the e gene has also been attempted [15][16][17]. A murine PKC-e subtype has been expressed in COS-1 cells which has unique substrate specificity and its activity is independent from Ca 2+.…”

Section: Introductionmentioning

confidence: 99%

Two components of type III protein kinase C with different substrate specificities and a phospholipid‐dependent but Ca²⁺‐inhibited protein kinase in rat brain

et al. 1989

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The activities of rat brain protein kinase C isoenzymic fractions separated by hydroxyapatite chromatography were measured with histone HI or the oligopeptide Ala-Ala-Ala-Ser-Phe-Lys-Ala-Lys-Lys-amide as substrates. The oligopeptide was a better substrate than histone HI for nearly all of the protein kinase C fractions. Two subfractions of type III isoenzyme were resolved (llIa and IIIb); type IIIb was characterized by a very low histone kinase activity compared to its peptide kinase activity. In some brain extracts a phospholipid-dependent but Ca2+-inhibited protein kinase was also observed which was eluted from the hydroxyapatite column between type II and III isoenzymes of protein kinase C.Protein kinase C; Substrate specificity; Synthetic oligopeptide substrate; Isoenzyme; Ca2+-inhibited enzyme

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A novel phorbol ester receptor/protein kinase, nPKC, distantly related to the protein kinase C family

Cited by 408 publications

References 45 publications

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

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

Identification of the primary growth response gene, ST2/T1, as a gene whose expression is differentially regulated by different protein kinase C isozymes

Two components of type III protein kinase C with different substrate specificities and a phospholipid‐dependent but Ca²⁺‐inhibited protein kinase in rat brain

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A novel phorbol ester receptor/protein kinase, nPKC, distantly related to the protein kinase C family

Cited by 408 publications

References 45 publications

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

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

Identification of the primary growth response gene, ST2/T1, as a gene whose expression is differentially regulated by different protein kinase C isozymes

Two components of type III protein kinase C with different substrate specificities and a phospholipid‐dependent but Ca2+‐inhibited protein kinase in rat brain

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Two components of type III protein kinase C with different substrate specificities and a phospholipid‐dependent but Ca²⁺‐inhibited protein kinase in rat brain