Literature DB >> 2987037

Calcium-activated, phospholipid-dependent protein kinase activity and protein phosphorylation in HL60 cells induced to differentiate by retinoic acid.

J P Durham, C A Emler, F R Butcher, J A Fontana.   

Abstract

Treatment of human promyelocytic (HL60) cells with retinoic acid for at least 48 h causes differentiation to more mature myeloid forms. Prior to commitment of cells to the myeloid pathway there is a marked increase in cytosolic calcium-activated, phospholipid-dependent protein kinase activity. This increase does not result from an intracellular redistribution of the enzyme. Concomitant with the increased enzyme activity there is enhanced phospholipid-dependent phosphorylation of proteins of 29, 49, 52, 58, 68, 69, 120, 170, 200 and 245 kDa.

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Year:  1985        PMID: 2987037     DOI: 10.1016/0014-5793(85)80761-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Decreased phosphorylation of a low molecular weight protein by cGMP-dependent protein kinase in variant HL-60 cells resistant to nitric oxide- and cGMP-induced differentiation.

Authors:  J S Scheele; R B Pilz; G Clark; N Gupta; D Loo; P Martis; G R Boss
Journal:  Mol Cell Biochem       Date:  1998-08       Impact factor: 3.396

Review 2.  Human neuroblastoma cell lines as models for the in vitro study of neoplastic and neuronal cell differentiation.

Authors:  E Abemayor; N Sidell
Journal:  Environ Health Perspect       Date:  1989-03       Impact factor: 9.031

3.  Antagonistic control of tumor necrosis factor receptors by protein kinases A and C. Enhancement of TNF receptor synthesis by protein kinase A and transmodulation of receptors by protein kinase C.

Authors:  P Scheurich; G Köbrich; K Pfizenmaier
Journal:  J Exp Med       Date:  1989-09-01       Impact factor: 14.307

  3 in total

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