Overproduction of protein kinase C causesdisordered growth control in rat fibroblasts

Housey, Gerard M.; Johnson, Mark D.; Hsiao, W.L. Wendy; O’Brian, Catherine A.; Murphy, James P.; Kirschmeier, Paul T.; Weinstein, I. Bernard

doi:10.1016/s0092-8674(88)80027-8

Cited by 468 publications

(221 citation statements)

References 33 publications

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“…This subclone was then used to develop derivatives that conditionally overexpress PKCa. Since our laboratory had previously studied in detail PKCb1 (Choi et al, 1990;Goldstein et al, 1995;Housey et al, 1988;Hsiao et al, 1989) it was also of interest to develop derivatives that conditionally over-express this closely related isoform of PKC to see if it would have e ects similar to those of PKCa. Pools and individual clones of cells that inducibly overexpress either PKCa (HC11-PKCa) or PKCb 1 (HC11-PKCb 1 ) and vector control cells (HC11-UHD) were obtained from the tTA3 cell line and further analysed.…”

Section: E Ects Of Tpa On Growth and Expression Of Endogenous Isoformmentioning

confidence: 99%

“…To create the pUHD-PKCb 1 plasmid the RP58 plasmid (Housey et al, 1988) was digested with HindIII and NotI, and the rat cDNA encoding PKCb 1 was gel-puri®ed and then ligated into the pMT vector digested with HindIII and NotI, creating pMTPKCb 1 . pMT-PKCb 1 was then digested with BamHI, and the fragment containing the PKCb 1 cDNA gel-puri®ed and ligated into the BamHI site of pUHD 10-3.…”

Section: Plasmid Constructionmentioning

confidence: 99%

“…Individual PKC isoforms show di erent substrate speci®cities, sub-cellular localization, cofactor requirements, and sensitivity to agonist induced down-regulation Jaken, 1996). The phenotypic e ects of ectopic overexpression of speci®c isoforms of PKC in various cell types are strongly dependent on both the cell type and isoform examined (Blumberg et al, 1994;Borner et al, 1991;Cacace et al, 1993;Housey et al, 1988). Several studies implicate an important role for PKC in human breast cancers Gordge et al, 1996;Kiley et al, 1996;O'Brian et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

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The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells

et al. 1999

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Section: E Ects Of Tpa On Growth and Expression Of Endogenous Isoformmentioning

confidence: 99%

Section: Plasmid Constructionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells

et al. 1999

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“…Over-expression of various PKCs in different cell lines has indicated that a certain isoenzyme might induce a specific effect, such as increased or reduced cell proliferation [5][6][7][8][9][10]. However, distinct functions of the different isoenzymes in signaling processes, especially with respect to selective phosphorylation of substrates, are unknown to date.…”

Section: Introductionmentioning

confidence: 99%

Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro

et al. 1994

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Native protein kinase C_~ from porcine spleen is phosphorylated in vitro by the tyrosine kinase src and to a much smaller extent by fyn. The tyrosine phosphorylation of PKC~ is restricted to the activated state of the enzyme, i.e. it occurs only in the presence of an activator, such as TPA or bryostatin. Upon phosphorylation at tyrosine, the apparent molecular weight of PKC~ increases by 6 kDa. Phosphorylation by src induces a stimulation of PKC~ activity apparently exhibiting some substrate selectivity. Other PKC isoenzymes, such as cPKC (g~,7), are not phosphorylated by src or only to a very small extent. This phosphorylation is not dependent on TPA and does not cause an increase in activity and molecular weight of the enzyme.

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“…Protein kinase C (PKC) has been implicated to play a key role in signal transduction and also in tumor promotion [1][2][3]. Terpenoid tumor promoters such as phorbol esters induce not only the activation of PKC by direct binding to the enzyme but also the downregulation of PKC by an indirect mechanism [1][2][3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Irreversible oxidative inactivation of protein kinase C by photosensitive inhibitor calphostin C

1992

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Isolated protein kinase C (PKC) was irreversibly inactivated by a brief (mm) incubation with calphoatin C in the prc~en~ of light, This inactivation required Ca"* either in a mdhmolar range in the absenc ,~ of lipid activators or in a submicrornolar range in the pre~nce of lipid activators. In addition, an oxygen atmosphere web required suggestmt~' the involvement of oxidation(s) in this inactivation process. Furthermore, laKC inactivation might involve a site-specific ox~dative modification of the enzyme at the CaZ*-mduced hydrophob~c region, lahysical queneher~ of singlet oxygen such as lycopene, fl.carotene, and =-tocopherol all reduced the calphostm C-induced inactivation of PKC. In intact cells treated with calphostm C, the iaaetivalion of laKC was rapid in the membrane fraction compar~:l to cytosol. Thin intrecellular PKC inactivation was also found to irreversibl~. Therefore, calphostin C can bring prolonged effects for several hours in cells treated for a short time. Taken together the~e rest,Its sugl3est that the calphostm C-mediated inactivation of PKC involves a site-specific and a "cage' type oxidative modification of lake.

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Overproduction of protein kinase C causesdisordered growth control in rat fibroblasts

Cited by 468 publications

References 33 publications

The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells

The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells

Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro

Irreversible oxidative inactivation of protein kinase C by photosensitive inhibitor calphostin C

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