<原著>腎組織でのplasminogen activator inhibitor-1の同定とその性質
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The author demonstrated that plasminogen activator inhibitor (PAI) exists in renal tissues in both stroke-prone spontaneously hypertensive rat (SHRSP) and Wistar Kyoto rat (WKY). PAI activity was determined by the synthetic substrate and fibrinplate methods. The homogenized solution of the kidney showed one band with a molecular weight of 42 kD on reverse fibrin autography, which indicates the presence of PAI. On sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), the final samples of both the glycine- and guanidine-eluted PAI from the 2nd anti-human PAI IgG-Sepharose showed one major band with the molecular weight of 42 kD at the non-reduced condition and one band with the molecular weight of 50 kD in the reduced condition. The purification factor of the PAI in the kidney of SHRSP was 1,236 for the glycine-eluted fraction and 824 for the guanidine-HCI-eluted fraction, and that of PAI in WKY 875 and 1,750,respectively. The purified PAI inhibited human two-chain u-PA, single-chain t-PA and two-chain t-PA. The kinetic constant on S-2444 amidolysis by u-PA, the kcat/Km value, was decreased to 70% in the presence of PAI obtained from SHRSP and 60% in that of WKY respectively. Enzymography indicated the presence of u-PA with 43 kD, 37 kD and t-PA with 68 kD, but no complexed form with PAI was observed. Immunohistochemical analysis performed with the antibodies detected of u-PA in the cytoplasm of distal tubular epithelial cells. u-PA, t-PA and PAI were observed along the glomerular capillary walls and the arteriolae. Fine staining for PAI antigen was present in the peritubular capillary and apical surface membrane of distal tubules.
- 近畿大学の論文
- 1990-09-25
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- 腎組織でのplasminogen activator inhibitor-1の同定とその性質