INTERACTION OF LAMININ WITH THE PLASMA MEMBRANE COMPONENTS OF ASCITIC ZAJDELA HEPATOMA CELLS
I. I. Tyuryaeva,1,* O. A. Mirgorodskaya,1 O. A. Cherepanova,1
E. P. Podolskaya,2 M. V. Serebryakova,3 V. A. Ivanov 1
1 Institute of Cytology RAS, 2 Institute of Analytical Instrumentation RAS,
St. Petersburg,
and 3 Institute of Biomedical Chemistry RAMS, Moscow;
* e-mail: miroslav@kd1537.spb.edu
The laminin affinity chromatography was used for isolating laminin-binding proteins from the plasma membrane of
Zajdela hepatoma cells synthesizing laminin. These were components with mol. weights about 80, 67, 60, 55, 52, 48 and 43 kDa. The
isolation of laminin integrin receptors from plasma membranes of Zajdela hepatoma cells in the presence of MnCl2 detected only a
protein with mol. weight about 80 kDa in EDTA-elution conditions. This protein was identified by mass spectrometry method as the
78 kDa glucose-regulated protein precursor (GRP78). It belongs to the family of 70 kDa heat shock proteins, recently GRP78 was
reported to be localized on the surface of different cell types, including hepatocytes.
Key words: hepatoma, laminin, laminin receptor, heat shock proteins, GRP78
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