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Identification of the inhibitor of the plasminogen activator as the major protein secreted by endothelial rat liver cells
Author(s) -
Kuiper Johan,
Kamps Jan A.A.M.,
Van Berkel Theo J.C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80227-3
Subject(s) - secretory protein , secretion , plasminogen activator , albumin , biology , parenchyma , kupffer cell , plasminogen activator inhibitor 1 , microbiology and biotechnology , endothelial stem cell , biochemistry , endocrinology , immunology , in vitro , botany
Freshly isolated Kupffer and endothelial liver cells exhibit a rate of ‘de novo’ protein synthesis which is twice as high per mg cell protein as that of parenchymal liver cells and contribute significantly (7.5% and 5.9%, respectively) to total liver protein secretion. In parenchymal cells the main secretory protein is a 68 kDa protein (containing 19% of the secreted radioactivity, presumably albumin). In Kupffer cells a 49 kDa protein contains 8% of the secreted radioactivity, while in endothelial liver cells a 55 kDa protein is the most prominent secretory protein (containing 11% of the secreted radioactivity). By aid of a specific antibody the 55 kDa protein was identified as the inhibitor of the plasminogen activator and in the liver this protein was only secreted by the endothelial cells.