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Titolo:
EFFECTS OF SURAMIN-RELATED AND OTHER CLINICALLY THERAPEUTIC POLYANIONS ON PROTEIN-KINASE-C ACTIVITY
Autore:
KHALED Z; RIDEOUT D; ODRISCOLL KR; PETRYLAK D; CACACE A; PATEL R; CHIANG LC; ROTENBERG S; STEIN CA;
Indirizzi:
COLUMBIA UNIV,DEPT MED,630 W 168TH ST NEW YORK NY 10032 COLUMBIA UNIV,DEPT MED NEW YORK NY 10032 CUNY QUEENS COLL FLUSHING NY 11367 SCRIPPS CLIN & RES INST LA JOLLA CA 92037
Titolo Testata:
Clinical cancer research
fascicolo: 1, volume: 1, anno: 1995,
pagine: 113 - 122
SICI:
1078-0432(1995)1:1<113:EOSAOC>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBROBLAST GROWTH-FACTOR; PHOSPHOROTHIOATE OLIGODEOXYNUCLEOTIDES; REVERSE-TRANSCRIPTASE; DNA-POLYMERASES; GENE-EXPRESSION; KAPOSIS SARCOMA; FACTOR RECEPTOR; CELLS; INHIBITION; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
Z. Khaled et al., "EFFECTS OF SURAMIN-RELATED AND OTHER CLINICALLY THERAPEUTIC POLYANIONS ON PROTEIN-KINASE-C ACTIVITY", Clinical cancer research, 1(1), 1995, pp. 113-122

Abstract

The mechanism of the antineoplastic effects of suramin may involve interference with signal transduction, but in general is not well understood. We examined several polyanions to determine their effects on thekinase activity of the protein kinase C (PKC) beta(1) and other PKC isoforms. Similar to suramin, a phosphorothioate oligodeoxynucleotide 28-mer homopolymer of cytidine (SdC28) inhibited the phosphatidylserineand Ca2+-dependent phosphorylation of an epidermal growth factor receptor octapeptide substrate, The inhibition by suramin was mixed competitive/noncompetitive with respect to ATP, but uncompetitive with respect to substrate. In contrast, the inhibition by SdC28 was competitive with respect to substrate (K-i = 5.4 mu M) and not competitive with respect to ATP. The PKC alpha and beta(1) isoforms were inhibited to thesame extent with SdC28, while PKC epsilon was not inhibited, SdC28, in the absence of lipid cofactor, stimulated substrate phosphorylation,and in the absence of substrate induced PKC beta(1) autophosphorylation, Similar behavior was seen with another polyanion, the polysulfatedcarbohydrate pentosan polysulfate (polyxylyl hydrogen sulfate), H4, abis-naphthalene disulfonate tetraanion structurally related to suramin, also inhibited kinase activity but was not competitive with respectto ATP, Dianions closely related to H4 failed to inhibit PKC beta(1),suggesting that multiple (>2) negative charges are required, The interactions of polyanions with PKC are complex, and are dependent on the molecular structure of the polyanion, the presence of cofactors, and the PKC isoform.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:25:42