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F Hog

Publications and source records attributed to F Hog.

7 recordsLinked to original sources
PubMed1993

Cytoplasmic poly(ADP-ribose)polymerase from mouse plasmacytoma free messenger ribonucleoprotein particles: purification and characterization.

A cytoplasmic poly(ADP-ribose)polymerase (PARP) was purified from mouse plasmacytoma free messenger ribonucleoprotein particles using chromatography on 3-aminobenzamide affigel-10. The purified protein showed one band at 116 kDa on SDS-polyacrylamide gel electrophoresis and shared similar antigenic sites to the nuclear PARP. An apparent Km for NAD of 100.5 +/- 6.3 microM and a Vmax of 174 +/- 40 nmoles of ADP-ribose incorporated/min/mg protein were observed. RNA was detected in the enzyme preparation and the enzymatic activity was not DNA dependent.

Animals↗
PubMed1993

ADP-ribosylation of neurofilaments by a cytoplasmic ADP-ribose transferase associated with free mRNP.

ADP-ribosylation of neurofilaments by an ADP-ribose transferase isolated from cytoplasmic ribonucleoprotein particles is demonstrated. The 150 kDa neurofilament subunit appears to be the main ADP-ribose acceptor with the transfer of ADP-ribose dimers or monomers. A binding of about 1 mole ADP-ribose per 8 moles of neurofilament subunits has been recorded. An interaction between neurofilaments' ADP-ribosylation and their phosphorylation state is demonstrated.

Adenosine Diphosphate Ribose↗
PubMed1992

Poly(ADPR)polymerase expression and activity during proliferation and differentiation of rat astrocyte and neuronal cultures.

Poly(ADPR)polymerase (poly(ADPR)P) mRNA and enzymatic activity levels were investigated in primary cultures of rat astrocytes and neurons in the absence or presence of basic fibroblast growth factor (bFGF) and nerve growth factor (NGF), respectively. In cultured rat astrocytes, a biphasic increase in poly(ADPR)P mRNA, associated with enhanced nuclear poly(ADPR)P enzymatic activity, were observed. The first rise in poly(ADPR)P mRNA and enzymatic activity is at the beginning of cell proliferation and the second with the occurrence of cell differentiation. In the presence of bFGF (5 ng/ml) the mRNA peaks and the differentiation-associated poly(ADPR)P enzymatic activity undergoes a 2-fold increase. In neuronal cultures an initial high level of poly(ADPR)P mRNA is followed by a decrease while differentiation is progressively achieved. A limited increase of poly(ADPR)P activity is observed during this phase. In the presence of NGF (50 ng/ml), similar poly(ADPR)P mRNA expression and enzymatic activity patterns are observed. The results suggest that poly(ADPR)P is involved at the onset of nerve-cell proliferation and differentiation.

Animals↗
PubMed1989

[Phosphorylation of cytoplasmic poly (ADP-ribose) polymerase linked to free ribonucleoprotein particles by an associated protein kinase C].

Considering the eventuality of an interaction between the two post-translational modifications, phosphorylation and ADP-ribosylation, we investigated the possibility of phosphorylation of the mRNP polyADPR polymerase by a protein kinase C associated to these particles. We demonstrated that cytoplasmic poly (ADP-ribose) polymerase associated with ribonucleoprotein particles containing silent mRNA is phosphorylated by a specifically activated endogenous protein kinase C which in turn induces an inhibition of the polymerase activity. In the absence of protein kinase C activators the mRNP polyADPR-P is also phosphorylated but without changes of its enzymatic activity.

Blotting, Western↗