Similar effects of platelet-derived growth factor and epidermal growth factor on the phosphorylation of tyrosine in cellular proteins

Cooper, Jonathan A.; Bowen‐Pope, Daniel F.; Raines, Elaine W.; Ross, Russell; Hunter, Tony

doi:10.1016/0092-8674(82)90426-3

Cited by 361 publications

(162 citation statements)

References 32 publications

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“…In the CA1 and CA3 areas of the rodent hippocampus, the relative postnatal growth of the comissural/associational terminal ®elds, and the elaboration of stratum radiatum pyramidal dendrites, are most rapid in the second postnatal week (Loy, 1980;Pokorny and Yamamoto, 1981). PDGF-B/c-SIS has been shown to exhibit various properties, including enhancement of neurite extension, induction of c-fos (Smits et al, 1993), stimulation of tyrosine phosphorylation (Cooper et al, 1982), inhibition of gapjunctional communication (Maldonado et al, 1988), and inhibition of NMDA receptor function (Valenzuela et al, 1996), all of which are consistent with the possible involvement of PDGF-B/c-SIS in synaptic transmission. Considering the abundant receptor (PDGFR-b) expression in neonatal neurons (Smits et al, 1991), the expression of PDGF-B/c-SIS in the hippocampus during the second postnatal week may be related to the maturation of neurons, including as neurite extension and elaboration of synaptic network.…”

Section: Discussionmentioning

confidence: 67%

Normal developing rat brain expresses a platelet-derived growth factor B chain (c-sis) mRNA truncated at the 5′ end

et al. 1998

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Section: Discussionmentioning

confidence: 67%

Normal developing rat brain expresses a platelet-derived growth factor B chain (c-sis) mRNA truncated at the 5′ end

et al. 1998

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“…Members of this family become tyrosine-phosphorylated and activated in cells stimulated with diverse mitogens, including activators of cell surface protein tyrosine kinases and activators of protein kinase C (Cooper et al, 1982(Cooper et al, , 1984Bishop et al, 1983;Gilmore and Martin, 1983;Kohno, 1985;Ray and Sturgill, 1987;Hoshi et al, 1988;Rossomando et al, 1989;Ahn et al, 1990;Ferrell and Martin, 1990;Gotoh et al, 1990b;Haystead et al, 1990; Kyriakis and Avruch, 1990;Nel et al, 1990;Tsao et al, 1990;Anderson et al, 1991;L'Allemain et al, 1991;Tobe et al, 1991;Funasaka et al, 1992 1Abbreviations used: DMEM, Dulbecco's modified Eagle's medium; DTT, dithiothreitol; EGF, epidermal growth factor; ERK, extracellular signal-regulated kinase or early response kinase; HPLC, high-pressure liquid chromatography; MAP, microtubule-associated protein 2 or mitogen-activated protein; MBP, myelin basic protein; MES, 2-(N-morpholino)ethanesulfonic acid; PMSF, phenylmethylsulfonyl fluoride; SDS, sodium dodecyl sulfate; TPA, 12-0-tetradecanoylphorbol-13-acetate; TRE, TPA response element; Tris, tris(hydroxymethyl)aminomethane.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of c-Jun DNA binding by mitogen-activated protein kinase.

Baichwal

Ferrell

1992

MBoC

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Here we demonstrate that partially purified Xenopus p42 mitogen-activated protein (MAP) kinase phosphorylates bacterially expressed human c-Jun at a single site, serine 243. Several lines of evidence argue that this phosphorylation is due to p42 MAP kinase itself rather than some contaminating species. Phosphorylation of serine 243 markedly decreases the binding of c-Jun to oligonucleotides containing the 12-O-tetradecanoylphorbol-13-acetate response element. These findings suggest that MAP kinase may play a role in the down-regulation of c-Jun or in the cycle of transcriptional initiation and elongation.

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“…Parallel observations on phosphorylation of tyrosine residues have been made with the platelet-derived growth factor [68,69] and insulin [65] receptors. In the case of EGF, there is some evidence that stimulation of tyrosine phosphorylation could not be sufficient for mitogenesis.…”

Section: Discussionmentioning

confidence: 87%

“…6 shows the results of phosphoamino acid analysis performed on the 170000-M, polypeptide band excised from the gels. Separation of phosphoamino acids was carried out by the one-dimensional electrophoresis technique at pH 3.5 [6] after EGF stimulation (Fig. 6B), in comparison to the control (Fig.…”

Section: Phosphoamino Acid Specificity In Vitro Of the Egf-dependent mentioning

confidence: 99%

Characterization of the epidermal‐growth‐factor‐dependent phosphorylation system from normal mouse‐liver sinusoidal plasma membranes

Ehrhart

Rollet

Komano

et al. 1983

European Journal of Biochemistry

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Blood sinusoidal plasma membrane subfractions were isolated from normal mouse liver in the presence of the proteinase inhibitors PhMeSO2F and iodoacetamide. They were purified from smooth microsomal and Golgi vesicle contaminants. The phosphorylation reaction was studied at 33°C, in the presence of 2 mM MnCl2. Addition of epidermal growth factor (EGF) to the preparations stimulated 32P incorporation from [γ‐32P]ATP or [γ‐32P]GTP essentially into one 170000 Mr protein. Some incorporation was observed in a minor 120000‐Mr component which appears to be a degradation product of the 170000‐Mr component. No EGF‐dependent phosphorylation of other membrane proteins or various exogenous proteins could be detected in vitro. The dephosphorylation of the 170000‐Mr component was observed after 4 min of incubation at 33°C. This dephosphorylation reaction was inhibited by addition of 5 mM p‐nitrophenyl phosphate but not by addition of micromolar Zn2+, Be2+ or orthovanadate. The 170000‐Mr protein specifically bound 125I‐labeled EGF and thus appeared to be the hepatic EGF receptor. The EGF stimulatable kinase activity considerably enhances incorporation of 32P into tyrosine residues of the 170000‐Mr EGF receptor at 33°C. Tryptic peptide maps of the 32P‐labeled 170000‐Mr protein revealed a multiplicity of phosphorylated sites. Seven 32P‐labeled phosphopeptides were observed after EGF stimulation, three of them being largely prominent. Tryptic peptide maps of the 170000‐Mr protein after it was covalently linked to 125I‐labeled EGF showed only one 125I‐labeled peptide, the migration of which appeared different from that of 32P‐labeled phosphopeptides. These findings were confirmed by V8 protease unidimensional peptide mapping of the 170000‐Mr protein, labeled with 32P or 125I‐EGF.

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Similar effects of platelet-derived growth factor and epidermal growth factor on the phosphorylation of tyrosine in cellular proteins

Cited by 361 publications

References 32 publications

Normal developing rat brain expresses a platelet-derived growth factor B chain (c-sis) mRNA truncated at the 5′ end

Normal developing rat brain expresses a platelet-derived growth factor B chain (c-sis) mRNA truncated at the 5′ end

Inhibition of c-Jun DNA binding by mitogen-activated protein kinase.

Characterization of the epidermal‐growth‐factor‐dependent phosphorylation system from normal mouse‐liver sinusoidal plasma membranes

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