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Structure and function of macrophage adhesion molecule examined by epitope mapping
1Center for Blood Research, Harvard Medical School, Boston, MA 02115.
Journal of Immunology (Baltimore, Md. : 1950)
|August 1, 1988
Summary
Macrophage adhesion molecule (MAM) forms a heterodimer critical for cell adhesion. Specific regions on its subunits, generated upon heterodimerization, are essential for this adhesive function.
Area of Science:
- Cell Biology
- Immunology
- Biochemistry
Background:
- Macrophage adhesion molecule (MAM) is a guinea pig integrin involved in cell adhesion.
- MAM is synthesized as monomeric precursors that assemble into a heterodimer.
Purpose of the Study:
- To characterize the topographic regions of MAM involved in adhesion.
- To investigate the structural basis of MAM's adhesive properties.
Main Methods:
- Immunoprecipitation and immunoblotting using monoclonal antibodies (mAbs).
- Binding assays and quantitative cell adhesion assays.
- Characterization of monomeric and heterodimeric MAM forms.
Main Results:
- Seven topographic regions of MAM were identified.
- Two regions, M2/M4 on the alpha-subunit and M8/M15 on the beta-subunit, are critical for adhesion.
- These adhesion-critical regions are conformation-dependent, appearing only in the heterodimer.
Conclusions:
- Adhesion-critical epitopes on MAM are generated by conformational changes during heterodimer formation.
- These findings suggest general principles for integrin structure-function relationships.