Changes in protein kinase C activity are associated with the differentiation of Friend erythroleukemia cells

Balazovich, Kenneth J.; Portnow, Douglas; Boxer, Laurence A.; Prochownik, Edward V.

doi:10.1016/0167-4889(87)90141-8

Cited by 30 publications

(3 citation statements)

References 21 publications

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“…Hypoxanthine has been reported to have various biological activities such as stimula tion of DNA synthesis in serum-starved L cells (23) and neuroblasts (24), stimulation of differentiation of erythroleukemia cells (25,26), and maintenance of murine oocyte meiotic arrest (15), and enhancement of cel lular immunity (27). Besides these actions, we present here that hypoxanthine and inosine have an effect on FGF-dependent proliferation of PAEC grown in a serum-limited culture system.…”

Section: Discussionmentioning

confidence: 75%

Identification of Hypoxanthine and Inosine in Brain Dialyzable Fraction as Stimulators for Growth of Porcine Aortic Endothelial Cells in Response to Fibroblast Growth Factor in Either Dialyzed Serum Media or Low Serum Media

Hayashi

Hirai

Harayama

et al. 1990

Japanese Journal of Pharmacology

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Section: Discussionmentioning

confidence: 75%

Identification of Hypoxanthine and Inosine in Brain Dialyzable Fraction as Stimulators for Growth of Porcine Aortic Endothelial Cells in Response to Fibroblast Growth Factor in Either Dialyzed Serum Media or Low Serum Media

Hayashi

Hirai

Harayama

et al. 1990

Japanese Journal of Pharmacology

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“…Recently, we (11) and others (18) have provided evidence that a protein kinase C (PKC)-related signal is important in the early stages of induced MELC differentiation. The phorbol ester phorbol 12-myristate 13-acetate depletes cellular PKC activity and inhibits HMBA-mediated MELC differentiation.…”

mentioning

confidence: 99%

Introduction of the beta isozyme of protein kinase C accelerates induced differentiation of murine erythroleukemia cells.

Melloni

Pontremoli

Sparatore

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

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Induction of differentiation in murine erythroleukemia cells (MELCs) involves a protein kinase C (PKC)-mediated step. Vincristine-resistant cells respond more rapidly to hybrid polar/apolar inducers than the parental cells. These vincristine-resistant MELCs contain elevated levels of the 13 isozyme of PKC (PKC-fi). Exogenous homologous murine PKC-fl, incorporated into permeabilized MELCs, accelerates induced differentiation. Neither rat PKC-(3, nor mouse PKCa, nor rat PKC-a, incorporated into permeabilized MELCs, is effective in altering the kinetics of induced differentiation. This provides direct evidence for a rate-limiting role for this PKC isozyme during NN'-hexamethylenebisacetamide-mediated induced differentiation of a transformed cell.

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“…Addition of HMBA to MELC cultures causes changes in protein kinase C (PKC) distribution and activity within 30 to 45 min (2,3). PKC comprises a family ofclosely related serine/threonine protein kinases that are intermediaries in signal transduction pathways presumably engaged in regulation of cell proliferation and differentiation (for reviews, see refs.…”

mentioning

confidence: 99%

Protein kinase C isozymes epsilon and alpha in murine erythroleukemia cells.

Powell

Leng

Dong

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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Protein kinase C (PKC) has a role in signal transduction during hexamethylene bisacetamide (HMBA)-induced differentiation of murine erythroleukemia cells (MELC). Separation of MELC PKC isozymes by hydroxylapatite chromatography yields a major peak (HI) and a minor peak (II) of PKC activity, previously reported to contain the PKC a and (3 isozymes, respectively. In the present study, we confirm that peak m activity is PKCa but show that peak II contains PKCE and little or no PKCP. Immunoblot analysis with isozyme-specific anti-a and anti-E PKC antibodies detected PKCa in peak 11I and PKCE in peak II. Peak m activity was markedly enhanced (up to 20-fold) by phosphatidylserine, diolein, and Ca2+, whereas addition of these cofactors to the reaction mixture stimulated peak II activity only 2-to 4-fold. RNase protection analysis of MELC RNA showed that PKCa and PKCe RNAs were in a ratio of -2:1, but PKC(3 RNA was barely detectable. Taken together, these data indicate that MELC contain PKCa and PKCE but little or no PKCI.Murine erythroleukemia cells (MELC) are virus-transformed erythroid precursor cells that can be induced by hexamethylene bisacetamide (HMBA) and related compounds to terminal erythroid differentiation (1). Addition of HMBA to MELC cultures causes changes in protein kinase C (PKC) distribution and activity within 30 to 45 min (2, 3). PKC comprises a family ofclosely related serine/threonine protein kinases that are intermediaries in signal transduction pathways presumably engaged in regulation of cell proliferation and differentiation (for reviews, see refs. 4 and 5). PKC isozymes exhibit differences in substrate specificities and cofactor requirements, which may reflect different biological functions. PKC isozymes a, 1B, and 'y are markedly activated by phospholipids, diacylglycerol, or phorbol esters and by Ca21 (6, 7). The PKC isozymes 8 (8, 41), E (8-14), (8,15), and q/L (16,17) in general are activated to a lesser extent by phospholipids and diacylglycerol and are relatively Ca2' independent.Separation of the Ca2+-dependent PKC isozymes, a, 13, and y, is accomplished by chromatography on hydroxylapatite (HAP) columns (6, 18). Fractionation of MELC lysates yields two peaks of PKC activity, corresponding in location with peak II and peak III of Kikkawa et al. (6). We have reported evidence indicating an important role for MELC peak II activity in the pathway of HMBA-induced differentiation see Discussion).In a previous study, based upon a dot-blot immunoassay (20), the PKC activities in MELC peaks II and III were tentatively identified as the 13 and a isozymes, respectively.It has been shown that Ca2f-independent PKCE can be coeluted from HAP with PKCB (9). PKCS RNA is present at high levels in brain tissue (8, 10, 11) and in low-to-moderate levels in other tissues (10,11,22). In the present study, we have further characterized the peak II PKC activity in MELC by RNase protection and immunoblot assays and by comparing the effect of Ca2l on peak II and peak III kinase activities. We demonstra...

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Changes in protein kinase C activity are associated with the differentiation of Friend erythroleukemia cells

Cited by 30 publications

References 21 publications

Identification of Hypoxanthine and Inosine in Brain Dialyzable Fraction as Stimulators for Growth of Porcine Aortic Endothelial Cells in Response to Fibroblast Growth Factor in Either Dialyzed Serum Media or Low Serum Media

Identification of Hypoxanthine and Inosine in Brain Dialyzable Fraction as Stimulators for Growth of Porcine Aortic Endothelial Cells in Response to Fibroblast Growth Factor in Either Dialyzed Serum Media or Low Serum Media

Introduction of the beta isozyme of protein kinase C accelerates induced differentiation of murine erythroleukemia cells.

Protein kinase C isozymes epsilon and alpha in murine erythroleukemia cells.

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