Vessel Cylinders

Hester, R K; Ramos, Kenneth S.

doi:10.1016/b978-0-12-461201-3.50021-9

Cited by 1 publication

(1 citation statement)

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“…After removal of the adventitial layer, vessel cylinders were processed for denudation of intimal cells. Cylinders were opened longitudinally and intimal cells removed by mechanical scraping of the cylinders as has been described in detail previously (19). Removal of the intima and adventitia was verified by scanning electron microscopy.…”

Section: Tissue Preparationmentioning

confidence: 99%

Modulation of aortic protein phosphorylation by benzo(a)pyrene: Implications in PAH‐induced atherogenesis

Ramos

1992

J. Biochem. Toxicol.

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The toxicity of polycyclic aromatic hydrocarbons such as benzo(a)pyrene, 7,12-dimethylbenz(a)anthracene, and 3-methylcholanthrene has been associated with alterations in the proliferation of vascular smooth muscle cells and the development of lesions of mesenchymal origin. Because phosphorylation of endogenous substrates plays a central role in the regulation of smooth muscle cell growth, the present studies were conducted to evaluate the phosphorylation pattern of medial aortic protein upon repeated in vivo exposure of Japanese quail to benzo(a)pyrene (BaP). Medial aortic homogenates from quail treated for 10 weeks with 10 mg/kg benzo(a)pyrene or vehicle were processed for in vitro measurements of protein phosphorylation. In vitro phosphorylation of endogenous or exogenous proteins stimulated in vitro by phorbol myristate acetate/phosphatidylserine or cyclic AMP, known activators of protein kinase C and cyclic AMP-dependent protein kinase, respectively, was examined in the cytosolic and particulate fractions of homogenates from control and treated animals. Benzo(a)pyrene treatment significantly enhanced the basal phosphorylation of M(r) 113, 35, and 23 kDa proteins in the cytosolic fraction. Modest increases in the phosphorylation of M(r) 71, 52, and 38 kDa were also observed under basal conditions. No changes in the basal phosphorylation of particulate proteins were observed. Phosphorylation of endogenous protein substrates by protein kinase C in the cytosolic fraction was not altered by benzo(a)pyrene treatment. In contrast, inhibition of C-kinase-mediated phosphorylation of endogenous M(r) 272, 72, and 45 kDa proteins was observed in the particulate fraction of aortic homogenates from benzo(a)pyrene-treated quail relative to controls. Exogenous histone phosphorylation by PKC in the particulate, but not cytosolic fraction, was decreased by benzo(a)pyrene treatment.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Tissue Preparationmentioning

confidence: 99%