The adhesive glycoprotein laminin is an agglutinin

Kennedy, Dorothy W.; Rohrbach, David H.; Martin, George R.; Momoi, Takashi; Yamada, Katsushi

doi:10.1002/jcp.1041140302

Cited by 43 publications

(10 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the actual experiment, Sendai virions were incubated with SV-201, Mu1SV-201, Mu2SV-201, and the fusion peptide (0 -15 M each) for 80 min to allow the binding of peptides to virions, followed by the addition of 4% RBCs (100 l) to each suspension. One hour after the addition of RBCs, the degree of agglutination was observed as described by others (45,46). The agglutinated RBCs settled in the bottom of the wells in aggregates to form a uniform carpet of cells, whereas unagglutinated RBCs formed a compact button of cells.…”

Section: Methodsmentioning

confidence: 76%

See 1 more Smart Citation

A Peptide Derived from a Conserved Domain of Sendai Virus Fusion Protein Inhibits Virus-Cell Fusion

Ghosh

Shai

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

Section: Methodsmentioning

confidence: 76%

“…Hemagglutinin Assay-Hemagglutinating activity of Sendai virus in the presence and absence of peptides was determined using fresh human RBCs in a 96-well microtiter plate by standard methods (27,45,46). In a control experiment, 100 l of 4% RBC were added to 100 l of Sendai virus suspension.…”

Section: Methodsmentioning

confidence: 99%

A Peptide Derived from a Conserved Domain of Sendai Virus Fusion Protein Inhibits Virus-Cell Fusion

Ghosh

Shai

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…Inhibition studies of hemagglutination suggested that gangliosides and some anionic phospholipids might also be receptors for laminin (19). We have tested this hypothesis by measuring binding of laminin to erythrocyte membrane lipids, gangliosides, and other glycolipids.…”

mentioning

confidence: 99%

“…Laminin agglutinates aldehyde-fixed sheep, human, and rabbit erythrocytes (18,19). Inhibition studies of hemagglutination suggested that gangliosides and some anionic phospholipids might also be receptors for laminin (19).…”

mentioning

confidence: 99%

Laminin binds specifically to sulfated glycolipids.

Roberts¹,

Rao²,

Magnani³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

190

142

View full text Add to dashboard Cite

Previous studies of the agglutination of erythrocytes by the basement membrane glycoprotein laminin have suggested that laminin binds to gangliosides [Kennedy, D.W., Rohrbach, D.H., Martin, G.R., Momoi, T. & Yamada, K.M. (1983) J. Cell. Physiol. 114, 257-262]. Based on the following evidence, however, we find that laminin binds specifically to sulfatides, not gangliosides. Monogalactosyl sulfatides, purified from sheep erythrocytes with a yield of 4.3 mg/kg of packed cells, bound laminin with high affinity as did authentic bovine brain sulfatide (galactosylceramide-I3-sulfate). The binding activity of these lipids and of total erythrocyte lipids was stable to alkali and neuraminidase treatment but labile to dilute acid under conditions that destroy sulfatides but not gangliosides. Of various glycolipid and phospholipid standards tested, only sulfatides bound laminin with high affinity. Sulfatide binding and agglutinating activities of proteolytic fragments of laminin indicated that the globular end regions of the 200-kDa subunits are required for both activities. Thus, monogalactosylsulfatides, and possibly other more complex sulfated glycolipids, are probably involved in the agglutination of erythrocytes. These results also suggest a physiological function of sulfatides in cell adhesion. The agglutination of erythrocytes by fibronectin is also inhibited by gangliosides [Yamada, K.M., Kennedy, D.W., Grotendorst, G.R. & Momoi, T. (1981) J. Cell. Physiol. 109, 343-351]. Fibronectin, however, did not bind to sulfatides with high affinity but rather bound with low affinity to all anionic lipids tested, including phospholipids, gangliosides, and sulfatides.

show abstract

“…However, Tyr-Ile-Gly-SerArg peptide and synthetic fragments from the intersection of the chains lack neurite-promoting activity. The cell-surface ligand responsible for laminin-mediated neurite outgrowth has not been identified, but several candidates exist, including integrin, sulfatides, and gangliosides (17)(18)(19)(20).…”

mentioning

confidence: 99%

Laminin receptors for neurite formation.

Kleinman

Ogle²,

Cannon³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

157

View full text Add to dashboard Cite

Laminin, a basement membrane glycoprotein promotes both cell attachment and neurite outgrowth. Separate domains on laminin elicit these responses, suggesting that distinct receptors occur on the surface of cells. NG108-15 neuroblastoma-glioma cells rapidly extend long processes in the presence of laminin. We report here that '251-labeled laminin specifically binds to these cells and to three membrane proteins of 67, 110, and 180 kDa. These proteins were isolated by affinity chromatography on laminin-Sepharose. The 67-kDa protein reacted with antibody to the previously characterized receptor for cell attachment to laminin. Antibodies to the 110-kDa and 180-kDa bands demonstrated that the 110-kDa protein was found in a variety of epithilial cell lines and in brain, whereas the 180-kDa protein was neural specific. Antibodies prepared against the 110-kDa and 180-kDa proteins inhibited neurite outgrowth induced by the neuritepromoting domain of laminin, whereas antibodies to the 67-kDa laminin receptor had no effect on neurite outgrowth. We conclude that neuronal cells have multiple cell-surface laminin receptors and that the 110-kDa and 180-kDa proteins are involved in neurite formation.Laminin, a major glycoprotein of basement membranes, induces a variety of cellular responses, including cell attachment (1-3) and neurite outgrowth (4)(5)(6)(7)(8)(9). Laminin is composed of three chains, including the A chain (400 kDa), B1 chain (210 kDa), and B2 chain (200 kDa), which are arranged in a cross-shaped structure. A large fragment of laminin with cell-attachment activity has been produced by proteolysis and localized to the central portion of the cross where the three chains intersect (10). Subsequently, a synthetic pentapeptide, Tyr-Ile-Gly-Ser-Arg, was found to exhibit cell attachment activity for a variety of epithelial cells (11). However, this is not the only biologically active domain in laminin, since a separate site near the globule at the end of the long arm of the cross has neurite-promoting activity and cell attachment activity for certain cells (12,13). Since these separate domains elicit distinct activities, it is likely that different receptors mediate these activities.Previous studies have shown that there is a specific laminin receptor on cells (67 kDa) that recognizes the synthetic peptide Tyr-Ile-Gly-Ser-Arg from a sequence in the B1 chain (11,(14)(15)(16). Evidence that this receptor mediates cell attachment has been shown with antibody to the receptor, the Tyr-Ile-Gly-Ser-Arg peptide, and proteolytic fragments of laminin, all of which inhibit the attachment of a variety of cells to laminin (11). However, Tyr-Ile-Gly-SerArg peptide and synthetic fragments from the intersection of the chains lack neurite-promoting activity. The cell-surface ligand responsible for laminin-mediated neurite outgrowth has not been identified, but several candidates exist, including integrin, sulfatides, and gangliosides (17-20).Here we have used laminin affinity chromatography to identify receptors on neuronal cell...

show abstract

The adhesive glycoprotein laminin is an agglutinin

Cited by 43 publications

References 29 publications

A Peptide Derived from a Conserved Domain of Sendai Virus Fusion Protein Inhibits Virus-Cell Fusion

A Peptide Derived from a Conserved Domain of Sendai Virus Fusion Protein Inhibits Virus-Cell Fusion

Laminin binds specifically to sulfated glycolipids.

Laminin receptors for neurite formation.

Contact Info

Product

Resources

About