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Novel expression and localization of active thrombomodulin on the surface of mouse brain astrocytes

✍ Scribed by Armelle Pindon; Daniel Hantai; Martine Jandrot-Perrus; Barry W. Festoff

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 162 KB
Volume: 19
Category: Article
ISSN: 0894-1491
DOI: 10.1002/(sici)1098-1136(199703)19:3<259::aid-glia8>3.0.co;2-u

No coin nor oath required. For personal study only.

✦ Synopsis

Thrombin's potent effects on astrocytes are mediated by a specific receptor and inhibited by a serpin, protease nexin I (PNI). Thrombomodulin (TM), a membrane protein that forms complexes with thrombin, changing its enzymatic specificity, has not been studied in astrocytes. In primary astrocyte cultures, using Western blotting and immunocytochemistry, we found a 70 kDa TM band and TM localized to the surface with an anti-mouse TM monoclonal antibody. By reverse transcriptase coupled with polymerase chain reaction (RT-PCR), we found the correct sequence for mouse TM mRNA in astrocytes. Finally, we documented calcium-dependent activation of protein C by a thrombin:TM complex with thrombin added to the astrocytes. These results indicate the presence of functionally active TM at the astrocyte surface and add support to a role for thrombin signaling in the nervous system.

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