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Title: Selective regulation of intrinsic membrane proteins in HepG2

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6180162

The asialoglycoprotein receptor (ASGP-R) and insulin receptor (IR) are cell-surface glycoproteins whose activity varies with the state of cellular differentiation. Expression of ASGP-R, IR and an organic anion binding protein (OABP) was studied in HepG2 cells grown in minimal essential medium (MEM) supplemented with 10% fetal bovine serum (FBS), dialyzed FBS (dFBS) or serum from other species and corresponding to different physiological states of the liver. Cells grown in MEM-10% FBS maximally express ASGP-R and IR binding activity at confluence while OABP antigen appears independent of the state of cellular proliferation. Growth in dFBS reduces expression of ASGP-R and IR at confluence by 60-80% without altering OABP content, total cellular protein synthesis, or /sup 3/H-thymidine incorporation. Immunoblot of these cells reveals virtually no mature, 45 kDa ASGP-R, but a small amount of 36 kDa protein; metabolic labelling with /sup 35/S-methionine shows reduced synthesis of 45 kDa ASGP-R and absence of the 36 kDa antigen. Northern blot analysis of ASGP-R mRNA levels suggests post-translational regulation is affected. Normal expression of ASGP-R and IR are restored by addition of a 300-350 dalton fraction of FBS to medium.

Research Organization:
Albert Einstein College of Medicine, Bronx, NY
OSTI ID:
6180162
Report Number(s):
CONF-870644-; TRN: 87-033986
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
Country of Publication:
United States
Language:
English

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