Polyamine dependent protein kinase from rat brain and human laryngeal carcinoma
Başlık çevirisi mevcut değil.
- Tez No: 16727
- Danışmanlar: PROF.DR. WAYNE E. CRİSS
- Tez Türü: Yüksek Lisans
- Konular: Biyokimya, Biochemistry
- Anahtar Kelimeler: Laringeal neoplazmlar, Neoplazmlar, Poliaminler, Protein kinazlar, Sıçanlar, Laryngeal neoplasms, Neoplasms, Polyamines, Protein kinases, Rats
- Yıl: 1991
- Dil: İngilizce
- Üniversite: Hacettepe Üniversitesi
- Enstitü: Sağlık Bilimleri Enstitüsü
- Ana Bilim Dalı: Belirtilmemiş.
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: Belirtilmemiş.
Özet
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Özet (Çeviri)
ABSTRACT Poiyamines are essential for both normal and cancer cell proliferation. The biosynthethic pathway for these poiyamines is well established. Most anticancer drugs focus here. While the molecular mechanlsm(s) of action of poiyamines Is not understood. The current research was designed to elucidate some of the mechanisms by which poiyamines control cell growth. A polyamine dependent, self phosphoryiating protein kinase (PPK) was identified in rat brain tissue and human laryngeal carcinomas. The rat brain PPK activity was purified 30 foid using Sephadex G150 and DEAE-Trisacryl chromatographies. The brain enzyme did not bind to Phosphocelluiose or Carboxymethylsepharose. In addition to two enzyme bound-endogenous substrates, the brain PPK phosphorylated casein and histone as exogenous substrates. Poiyiysine stimulated both the endogenous and the exogenous substrate phosphorylation activities. Similar to poiyiysine, poiyornithine and spermidine stimulated the PPK activity. The apparent Km of the enzyme for ATP was 14.8 |iM for endogenous substrate phosphorylation and 35.7 \M for casein + endogenous substrate phosphorylation in the presence of poiyiysine. PPK activity was inhibited by heparin and dextran sulfate. The adenocarcinoma PPK activity was purified from human larynx tumor tissue using Sephadex G150 and Phosphocelluiose chromatographies. The rat brain PPK was then compared with laryngeal carcinoma PPK using enzyme kinetics and SDS-polyacrylamlde gel electrophoresis (SDS-PAGE) in attempts to analyze the phosphorylated protein products. The SDS-PAGE analysis revealed that both enzymes had at least two non-simiiar endogenous substrates; one was of high and one was of low molecular weight. The substrate specificities of the two enzymes changed with the addition of55 various exogenous substrates. In the presence of polyiysine, a high molecular weight substrate was preferred by both enzymes. When casein and polyiysine were present, the substrate specificity changed to casein and a low molecular weight substrate. Histone stimulated both enzymes to phosphoryiate a low molecular weight substrate. The brain PPK phosphorylated histone. This latter phosphorylation was also stimulated by polyiysine. However, the carcinoma PPK did not phosphoryiate histone In the absence or presence of polyiysine. Both the brain and carcinoma enzymes were inhibited by heparin and dextran sulfate. This study identifies and characterizes a polyamine dependent protein kinase from brain tissue. It provides data which supports the hypothesis that there are at least two cytoplasmic polyamine dependent protein kinases, one in brain tissue and one in laryngeal cancer tissue. These two enzymes have different physical and kinetic properties. Initial comparisons with previously published data on a rat hepatoma cytoplasmic PPK indicate that the laryngeal carcinoma PPK is similar. Therefore, it is suggested that, in addition to the polyamine biosynthethic pathway, anticancer polyamine metabolite drugs should also focus on the post synthesis actions of the poiyamlnes, such as at the PPK level of cellular growth control.
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