THE EFFECT OF THEOPHYLLINE ON THE KINETICS OF cAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT, cAMP, PROTEIN KINASE INHIBITOR AND THEIR RELATIONSHIP IN LUNG TISSUE
نویسندگان
چکیده مقاله:
We have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. The results show that the point of highest concentration of the C subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 Ilg/ InL and 10µg/mL theophylline, this is shifted to I.S and 2.S hrs, respectively. Also the maximum concentration of cAMP for the control is at 2.S h of incubation time, butin the treated samples shifts to 2.15 and LIS hrs, respectively. Inhibitor protein content also changes considerably in the presence of 10µg/mL theophylline. The results suggest an effect of theophylline on the function of cAMP-dependent protein kinase.
منابع مشابه
the effect of theophylline on the kinetics of camp-dependent protein kinase catalytic subunit, camp, protein kinase inhibitor and their relationship in lung tissue
we have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. the results show that the point of highest concentration of the c subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 ilg/ inl and 10µg/ml theophylline, this is shifted to i.s and 2....
متن کاملEffect of the thermostable protein kinase inhibitor on intracellular localization of the catalytic subunit of cAMP-dependent protein kinase.
cAMP-dependent protein kinase mediates a variety of cellular responses in most eukaryotic cells. Many of these responses are cytoplasmic, whereas others appear to require nuclear localization of the catalytic subunit. In order to understand further the molecular basis for subcellular localization of the catalytic subunit, the effect of the heat stable protein kinase inhibitor (PKI) was investig...
متن کاملAutophosphorylation of the catalytic subunit of cAMP-dependent protein kinase.
The catalytic subunit of cAMP-dependent protein kinase contains two stable phosphorylation sites, Thr-197 and Ser-338 (Shoji, S., Titani, K., Demaille, J. G., and Fischer, E. H. (1979) J. Biol. Chem. 254, 6211-6214). Thr-197 is very resistant to dephosphorylation and thus cannot typically be autophosphorylated in vitro once the stable subunit is formed. Ser-338 is slowly dephosphorylated and ca...
متن کاملThe inhibitor protein of the cAMP-dependent protein kinase-catalytic subunit interaction. Parameters of complex formation.
The formation of a complex between the catalytic subunit of the cAMP-dependent protein kinase and the Inhibitor Protein of this enzyme has been examined by means of nondenaturing gel electrophoresis. Two forms of complex were identified, both containing a 1:1 molar ratio of the component proteins. The formation of the major of the two forms is markedly enhanced by the presence of nucleotide tri...
متن کامل: the effect of sericin levels (silk glue protein) on rate of in vitro maturation, fertilization and culture of sheep oocytes
هدف از آزمایش اول بررسی اثر سطوح مختلف سریسین [0 (control), 0.1, 0.5, 1.0, 2.5 %] افزوده شده به محیط , ivm بر cumulus cell expansion، بلوغ هسته و توسعه متوالی جنین، در گوسفندان نژاد سنجابی در فصل تولید مثلی می باشد. از سرگیری میوز به وسیله خارج شدن اولین پولار بادی اندازه گیری و هم چنین درصد رسیدن جنین های دو سلولی به مرحله کلیواژ و بلاستوسیت نیز به عنوان نشانه ای از میزان شایستگی توسعه اولیه ج...
Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase.
The catalytic subunit of cAMP-dependent protein kinase expressed in Escherichia coli is a phosphoprotein. By in vivo labeling with [32Pi]orthophosphate, the sites of phosphorylation were identified as Ser-10, Ser-139, Thr-197, and Ser-338. Two of these sites, Thr-197 and Ser-338, are found in the mammalian enzyme (Shoji, S., Titani, K., Demaille, J. G., and Fischer, E. H. (1979) J. Biol. Chem. ...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ذخیره در منابع من قبلا به منابع من ذحیره شده{@ msg_add @}
عنوان ژورنال
دوره 8 شماره 4
صفحات 249- 253
تاریخ انتشار 1995-02
با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023