Hepatocellular localisation of biosynthesis of vitronectin. Characterisation of the primary structure of rat vitronectin
article
To characterize the primary structure of rat Vn, a cDNA library constructed from freshly isolated rat hepatocytes, was screened with a human Vn cDNA probe. Comparison of the sequence of the obtained rat cDNA clone with the sequences of human, mouse and rabbit Vn cDNA's showed predominantly consensus in the somatomedin B domain, the RGD-sequence and its flanking regions, in the first hemopexin type domain and at the carboxyl terminal part of Vn, the heparin binding site. To specify the liver cell type involved in the biosynthesis of Vn, we used a competitive PCR-assay to discriminate between expression levels. We found that expression of Vn in hepatocytes is at least 1000-fold higher than in Kupffer cells and 3000-fold higher than in endothelial liver cells. Chemicals/CAS: DNA, Complementary; Vitronectin
Topics
cDNA
Competitive PCR
Liver
Localisation
Rat
Vitronectin
complementary dna
hemopexin
heparin binding protein
somatomedin b
vitronectin
amino acid sequence
animal cell
article
carboxy terminal sequence
cell type
consensus sequence
dna library
endothelium cell
kupffer cell
liver cell
male
nonhuman
polymerase chain reaction
protein expression
protein localization
protein synthesis
rabbit
rat
sequence homology
Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
DNA, Complementary
Endothelium
Genetic Code
Humans
Kupffer Cells
Liver
Male
Mice
Molecular Sequence Data
Polymerase Chain Reaction
Rabbits
Rats
Sequence Homology, Amino Acid
Structure-Activity Relationship
Vitronectin
TNO Identifier
233125
ISSN
10399712
Source
Biochemistry and Molecular Biology International, 37(3), pp. 563-572.
Pages
563-572
Files
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