TY - JOUR
T1 - Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm
AU - Charonis, A. S.
AU - Tsilibary, E. C.
AU - Saku, T.
AU - Furthmayr, H.
PY - 1986
Y1 - 1986
N2 - Laminin is a major glycoprotein of the basement membrane. Although its precise localization and orientation within this structure is unknown, it is presumably anchored to other macromolecules such as type IV collagen or proteoheparan sulfate. In vitro, laminin has the ability to self-assemble and to bind to type IV collagen molecules at distinct sites. To identify more precisely the domains of the complex, cross-shaped laminin molecule that are involved in these interactions, images of laminin-laminin dimers and laminin-type IV collagen complexes obtained by the rotary shadowing method were analyzed. We observed that the complex domain at the end of the long arm of laminin is predominantly involved in these interactions. By using Fab fragments of antibodies specific for a peptide fragment derived from this complex domain, it is shown that laminin self-assembly is inhibited in their presence, as measured by turbidity and by electron microscopy. In addition, these antibodies inhibit the specific interaction of laminin with type IV collagen. These data suggest that the complex domain at the end of the long arm of laminin contains binding sites of potential importance for the assembly of basement membranes.
AB - Laminin is a major glycoprotein of the basement membrane. Although its precise localization and orientation within this structure is unknown, it is presumably anchored to other macromolecules such as type IV collagen or proteoheparan sulfate. In vitro, laminin has the ability to self-assemble and to bind to type IV collagen molecules at distinct sites. To identify more precisely the domains of the complex, cross-shaped laminin molecule that are involved in these interactions, images of laminin-laminin dimers and laminin-type IV collagen complexes obtained by the rotary shadowing method were analyzed. We observed that the complex domain at the end of the long arm of laminin is predominantly involved in these interactions. By using Fab fragments of antibodies specific for a peptide fragment derived from this complex domain, it is shown that laminin self-assembly is inhibited in their presence, as measured by turbidity and by electron microscopy. In addition, these antibodies inhibit the specific interaction of laminin with type IV collagen. These data suggest that the complex domain at the end of the long arm of laminin contains binding sites of potential importance for the assembly of basement membranes.
UR - http://www.scopus.com/inward/record.url?scp=0022979094&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022979094&partnerID=8YFLogxK
U2 - 10.1083/jcb.103.5.1689
DO - 10.1083/jcb.103.5.1689
M3 - Article
C2 - 2430974
AN - SCOPUS:0022979094
SN - 0021-9525
VL - 103
SP - 1689
EP - 1697
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 5
ER -