Endothelial dysfunction is implicated in a variety of cardiovascular diseases although the detailed mechanisms are not yet completely understood. A relationship has been suggested to exist between inflammation and end...Endothelial dysfunction is implicated in a variety of cardiovascular diseases although the detailed mechanisms are not yet completely understood. A relationship has been suggested to exist between inflammation and endothelial dysfunction. TNF-α serves as one of the most important pro-inflammatory cytokines. The main objectives of the present study were to explore the effect of PKC-ζ on TNF-α-impaired endothelial function as well as the underlying mechanisms. Acetylcho-line-induced endothelium-dependent vasodilation of mouse thoracic aorta stimulated by TNF-α was initially determined. PKC-ζ deficient mice and the specific inhibitor of NADPH oxidase were respectively applied to elucidate their roles in TNF-α-induced endothelial dysfunction. In vitro superoxide generation in HAECs was detected by DHE staining after administration of TNF-α. Meanwhile, the regulatory p47phox subunit of NADPH oxidase was evaluated by Western blotting and RT-PCR. The results showed that TNF-α conspicuously impaired endothelium-dependent vasodilation and the impairment was attenuated by either depleting PKC-ζ or inhibiting NADPH oxidase. In vitro TNF-α increased superoxide production and p47phox expression in HAECs, and such increases could be ameliorated by the specific PKC-ζ inhibitor. Our findings suggest that superoxide over-production triggered by PKC-ζ-dependent NADPH oxidase activation contributes to TNF-α-induced endothelial dysfunction.展开更多
Protein kinase C (PKC) is a family of serine/threonine protein kinases, and its multiple isoforms are expressed in various mammalian tissues. The expressions of PKC α and PKC δ at protein and mRNA level in mouse tes...Protein kinase C (PKC) is a family of serine/threonine protein kinases, and its multiple isoforms are expressed in various mammalian tissues. The expressions of PKC α and PKC δ at protein and mRNA level in mouse testis were identified by Western blotting and RT\|PCR. The expression of both PKC isoenzymes in the developing mouse testis was also examined. In testes of mouse at various developmental stages, both the protein and the mRNA of PKC\|α were uniformity; but the PKC\|δ expression occurred in the testes of 3\|week old, perhaps even relatively late in spermatid development. The results suggest that each isoenzyme may have different roles in processing and modulating physiological cellular responses of spermatogenesis.展开更多
文摘Endothelial dysfunction is implicated in a variety of cardiovascular diseases although the detailed mechanisms are not yet completely understood. A relationship has been suggested to exist between inflammation and endothelial dysfunction. TNF-α serves as one of the most important pro-inflammatory cytokines. The main objectives of the present study were to explore the effect of PKC-ζ on TNF-α-impaired endothelial function as well as the underlying mechanisms. Acetylcho-line-induced endothelium-dependent vasodilation of mouse thoracic aorta stimulated by TNF-α was initially determined. PKC-ζ deficient mice and the specific inhibitor of NADPH oxidase were respectively applied to elucidate their roles in TNF-α-induced endothelial dysfunction. In vitro superoxide generation in HAECs was detected by DHE staining after administration of TNF-α. Meanwhile, the regulatory p47phox subunit of NADPH oxidase was evaluated by Western blotting and RT-PCR. The results showed that TNF-α conspicuously impaired endothelium-dependent vasodilation and the impairment was attenuated by either depleting PKC-ζ or inhibiting NADPH oxidase. In vitro TNF-α increased superoxide production and p47phox expression in HAECs, and such increases could be ameliorated by the specific PKC-ζ inhibitor. Our findings suggest that superoxide over-production triggered by PKC-ζ-dependent NADPH oxidase activation contributes to TNF-α-induced endothelial dysfunction.
文摘Protein kinase C (PKC) is a family of serine/threonine protein kinases, and its multiple isoforms are expressed in various mammalian tissues. The expressions of PKC α and PKC δ at protein and mRNA level in mouse testis were identified by Western blotting and RT\|PCR. The expression of both PKC isoenzymes in the developing mouse testis was also examined. In testes of mouse at various developmental stages, both the protein and the mRNA of PKC\|α were uniformity; but the PKC\|δ expression occurred in the testes of 3\|week old, perhaps even relatively late in spermatid development. The results suggest that each isoenzyme may have different roles in processing and modulating physiological cellular responses of spermatogenesis.
