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Fibronectin binding to gangliosides and rat liver plasma membranes

Journal Article:

Abstract

Binding of fibronectins to gangliosides was tested directly using several different in vitro models. Using an enzyme-linked immunoabsorbent assay (ELISA), gangliosides were immobilized on polystyrene tubes and relative binding of fibronectin was estimated by alkaline phosphatase activity of conjugated second antibody. Above a critical ganglioside concentration, the gangliosides bound the fibronectin (G/sub T1b/ approx. = G/sub D1b/ approx. = G/sub D1a/ > G/sub M1/ >> G/sub M2/ approx. = G/sub D3/ approx. = G/sub M3/) in approximately the same order of efficiency as they competed for the cellular sites of fibronectin binding in cell attachment assays. Alternatively, these same gangliosides bound to immobilized fibronectin. Rat erythrocytes coated with gangliosides G/sub M1/, G/sub D1a/ or G/sub T1b/ bound more fibronectin than erythrocytes not supplemented with gangliosides. Using fibronectin in which lysine residues were radioiodinated, an apparent K/sub d/ for binding to mixed rat liver gangliosides of 7.8 x 10/sup -9/ M was determined. This value compared favorably with the apparent K/sub d/ for attachment of fibronectin to isolated plasma membranes from rat liver of 3.7 x 10/sup -9/ M for fibronectin modified on the tyrosine residue, or 6.4 x 10/sup -9/ M for fibronectin modified on lysine residues. As shown previously  More>>
Publication Date:
Feb 01, 1986
Product Type:
Journal Article
Reference Number:
ERA-11-041674; EDB-86-130548
Resource Relation:
Journal Name: Exp. Cell Biol.; (Switzerland); Journal Volume: 162:2
Subject:
59 BASIC BIOLOGICAL SCIENCES; ALKALINE PHOSPHATASE; ENZYME ACTIVITY; GANGLIOSIDES; ENZYME IMMUNOASSAY; GLUCOPROTEINS; BIOCHEMICAL REACTION KINETICS; ANTIBODIES; CELL MEMBRANES; ERYTHROCYTES; IODINE 125; LIVER CELLS; RATS; TRACER TECHNIQUES; ANIMAL CELLS; ANIMALS; BETA DECAY RADIOISOTOPES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CARBOHYDRATES; CELL CONSTITUENTS; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; ENZYMES; ESTERASES; HYDROLASES; IMMUNOASSAY; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; LIPIDS; MAMMALS; MATERIALS; MEMBRANES; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; PHOSPHATASES; PROTEINS; RADIOISOTOPES; REACTION KINETICS; RODENTS; SACCHARIDES; SOMATIC CELLS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques
OSTI ID:
5491337
Research Organizations:
Purdue Univ., West Lafayette, IN
Country of Origin:
Switzerland
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: ECEBD
Submitting Site:
JMT
Size:
Pages: 296-318
Announcement Date:
Aug 01, 1986

Journal Article:

Citation Formats

Matyas, G R, Evers, D C, Radinsky, R, and Morre, D J. Fibronectin binding to gangliosides and rat liver plasma membranes. Switzerland: N. p., 1986. Web.
Matyas, G R, Evers, D C, Radinsky, R, & Morre, D J. Fibronectin binding to gangliosides and rat liver plasma membranes. Switzerland.
Matyas, G R, Evers, D C, Radinsky, R, and Morre, D J. 1986. "Fibronectin binding to gangliosides and rat liver plasma membranes." Switzerland.
@misc{etde_5491337,
title = {Fibronectin binding to gangliosides and rat liver plasma membranes}
author = {Matyas, G R, Evers, D C, Radinsky, R, and Morre, D J}
abstractNote = {Binding of fibronectins to gangliosides was tested directly using several different in vitro models. Using an enzyme-linked immunoabsorbent assay (ELISA), gangliosides were immobilized on polystyrene tubes and relative binding of fibronectin was estimated by alkaline phosphatase activity of conjugated second antibody. Above a critical ganglioside concentration, the gangliosides bound the fibronectin (G/sub T1b/ approx. = G/sub D1b/ approx. = G/sub D1a/ > G/sub M1/ >> G/sub M2/ approx. = G/sub D3/ approx. = G/sub M3/) in approximately the same order of efficiency as they competed for the cellular sites of fibronectin binding in cell attachment assays. Alternatively, these same gangliosides bound to immobilized fibronectin. Rat erythrocytes coated with gangliosides G/sub M1/, G/sub D1a/ or G/sub T1b/ bound more fibronectin than erythrocytes not supplemented with gangliosides. Using fibronectin in which lysine residues were radioiodinated, an apparent K/sub d/ for binding to mixed rat liver gangliosides of 7.8 x 10/sup -9/ M was determined. This value compared favorably with the apparent K/sub d/ for attachment of fibronectin to isolated plasma membranes from rat liver of 3.7 x 10/sup -9/ M for fibronectin modified on the tyrosine residue, or 6.4 x 10/sup -9/ M for fibronectin modified on lysine residues. As shown previously by Grinnell and Minter, fibronectin modified on tyrosine residues did not promote spreading and attachment of CHO cells. It did, however, bind to cells. In contrast, lysine-modified fibronectin both bound to cells and promoted cell attachment. Plasma membranes isolated from hepatic tumors in which the higher gangliosides that bind fibronectin were depleted bound 43-75% less (/sup 125/I)fibronectin than did plasma membranes from control livers. The findings were consistent with binding of fibronectins to gangliosides, including the same gangliosides depleted from cell surfaces during tumorigenesis in the rat.}
journal = {Exp. Cell Biol.; (Switzerland)}
volume = {162:2}
journal type = {AC}
place = {Switzerland}
year = {1986}
month = {Feb}
}