Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor
Affinity chromatography was used to identify a putative cell surface receptor for fibronectin. A large cell-attachment-promoting fibronectin fragment was used as the affinity matrix, and specific elution was effected by using synthetic peptides containing the sequence Arg-Gly-Asp, which is derived from the cell recognition sequence in the fibronectin cell attachment site. A 140 kd protein was bound by the affinity matrix from octylglucoside extracts of MG-63 human osteosarcoma cells and specifically eluted with the synthetic peptide Gly-Arg-Gly-Asp-Ser-Pro. The 140 kd protein was labeled by cell surface specific radioiodination and became incorporated into liposomes at a high efficiency. Liposomes containing this protein showed specific affinity toward fibronectin-coated surfaces, and this binding could be selectively inhibited by the synthetic cell-attachment peptide but not by inactive peptides. Affinity chromatography on wheat germ agglutinin-Sepharose showed that the 140 kd protein is a glycoprotein and, in combination with the fibronectin fragment chromatography, gave highly enriched preparations of the 140 kd protein. These properties suggest that the 140 kd glycoprotein is a membrane-embedded cell surface protein directly involved in the initial step of cell adhesion to fibronectin substrates.
- Research Organization:
- La Jolla Cancer Research Foundation, CA
- OSTI ID:
- 5617239
- Journal Information:
- Cell; (United States), Vol. 40:1
- Country of Publication:
- United States
- Language:
- English
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GLUCOPROTEINS
RECEPTORS
SURFACE PROPERTIES
ADHESION
AFFINITY
CELL MEMBRANES
CHEMICAL BONDS
CHROMATOGRAPHY
IODINE ISOTOPES
LABELLED COMPOUNDS
LIPOSOMES
TRACER TECHNIQUES
CARBOHYDRATES
CELL CONSTITUENTS
ISOTOPE APPLICATIONS
ISOTOPES
MEMBRANES
ORGANIC COMPOUNDS
ORGANOIDS
PROTEINS
SACCHARIDES
SEPARATION PROCESSES
550201* - Biochemistry- Tracer Techniques