Membrane glycoproteins involved in hepatocyte adhesion to collagen type I

Donald Gullberg, Louis Terracio, Kristofer Rubin

Research output: Contribution to journalArticlepeer-review


Liver membrane glycoproteins with affinity for immobilized collagen type I were subjected to preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by electroelution of the separated proteins. Electroeluted glycoproteins with ability to neutralize the inhibitory effect of anti-CollCAM antibodies on hepatocyte adhesion to collagen were collected from several consecutive runs and used to raise a high titer antiserum, denoted anti-CollCAM II. IgG from this antiserum inhibited the attachment of hepatocytes to dishes coated with collagen type I, but not to fibronectin- or collagen type IV-coated dishes. When the antibodies were immobilized to Sepharose CL-4B they bound three sets of glycoproteins with apparent Mr's of 105,000, 115,000, and 130,000 as analyzed by SDS-PAGE under nonreducing (NR) conditions. Upon reduction (R) the glycoproteins migrated with apparent Mr's of 115,000, 130,000, and 160,000, respectively. The Mr 105,000-115,000 (NR) glycoproteins effectively neutralized the inhibitory effect exerted by both anti-CollCAM and anti-CollCAM II antibodies, on hepatocyte spreading and attachment to collagen type I substrates. Peptide mapping suggested the Mr 160,000 (R) species to be different from the Mr 115,000 (R).

Original languageEnglish (US)
Pages (from-to)388-395
Number of pages8
JournalExperimental Cell Research
Issue number2
StatePublished - Apr 1988

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'Membrane glycoproteins involved in hepatocyte adhesion to collagen type I'. Together they form a unique fingerprint.

Cite this