PMID- 6321620
OWN - NLM
STAT- MEDLINE
DCOM- 19840411
LR  - 20210217
IS  - 0022-2275 (Print)
IS  - 0022-2275 (Linking)
VI  - 24
IP  - 12
DP  - 1983 Dec
TI  - Receptors for homologous plasma lipoproteins on a rat hepatoma cell line.
PG  - 1568-77
AB  - Hepatocytes express on their surfaces more than one class of receptors capable of 
      mediating the internalization of lipoproteins. However, relatively little is 
      known about the binding characteristics of hepatic receptors for various 
      lipoproteins, about the regulation of the receptors, and about the consequences 
      for intracellular lipid metabolism of uptake of lipoproteins via different 
      classes of receptors. The aim of the present studies was to characterize the 
      binding and degradation of various lipoproteins and their mutual competition for 
      cellular processing. Since these kinds of studies may be more easily carried out 
      in continuous established hepatoma cell lines than in nondividing primary 
      hepatocyte cultures, we examined the lipoprotein receptor functions of a well 
      differentiated rat hepatoma (H-35). Cells were grown to confluence in Eagle's 
      minimal essential medium in 15% newborn calf serum. Medium then was changed to 
      15% lipoprotein-deficient serum for 44 hr before experiments. External binding of 
      125I-labeled rat plasma and intestinal lymph lipoproteins was assessed at 4 
      degrees C. Cellular uptake and degradation were assessed at 37 degrees C. 
      Lipoproteins were isolated by fixed angle or zonal ultracentrifugation or by 
      heparin affinity column chromatography and characterized as to their lipid and 
      apoprotein compositions. Labeled low density (LDL), high density (HDL2), 
      non-apoE-HDL, very low density lipoproteins (VLDL), and chylomicron remnants 
      (CM-R) each manifested specific and saturable binding and degradation by the 
      hepatoma cells. Competition experiments indicated that separate receptors were 
      present for LDL, HDL2, and CM-R. Most of HDL2 appeared to be bound to the 
      non-apoE-HDL receptor.(ABSTRACT TRUNCATED AT 250 WORDS)
FAU - Tamai, T
AU  - Tamai T
FAU - Patsch, W
AU  - Patsch W
FAU - Lock, D
AU  - Lock D
FAU - Schonfeld, G
AU  - Schonfeld G
LA  - eng
GR  - HL 15427/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Lipid Res
JT  - Journal of lipid research
JID - 0376606
RN  - 0 (Carrier Proteins)
RN  - 0 (Chylomicrons)
RN  - 0 (Lipoproteins)
RN  - 0 (Lipoproteins, HDL)
RN  - 0 (Lipoproteins, LDL)
RN  - 0 (Lipoproteins, VLDL)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, LDL)
RN  - 0 (Receptors, Lipoprotein)
RN  - 0 (VLDL receptor)
RN  - 0 (chylomicron receptor)
RN  - 0 (high density lipoprotein receptors)
RN  - 147605-06-9 (high density lipoprotein binding protein)
SB  - IM
MH  - Animals
MH  - *Carrier Proteins
MH  - Cell Line
MH  - Chylomicrons/*metabolism
MH  - Female
MH  - Kinetics
MH  - Lipoproteins/blood
MH  - Lipoproteins, HDL/*metabolism
MH  - Lipoproteins, LDL/*metabolism
MH  - Lipoproteins, VLDL/*metabolism
MH  - Liver Neoplasms, Experimental/*metabolism
MH  - *RNA-Binding Proteins
MH  - Rats
MH  - Rats, Inbred Strains
MH  - Receptors, Cell Surface/*metabolism
MH  - Receptors, LDL
MH  - *Receptors, Lipoprotein
EDAT- 1983/12/01 00:00
MHDA- 1983/12/01 00:01
CRDT- 1983/12/01 00:00
PHST- 1983/12/01 00:00 [pubmed]
PHST- 1983/12/01 00:01 [medline]
PHST- 1983/12/01 00:00 [entrez]
AID - S0022-2275(20)37855-X [pii]
PST - ppublish
SO  - J Lipid Res. 1983 Dec;24(12):1568-77.