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Home/Research/Paper Chase/Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families.
Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families.
Cell.Mar 25, 1988;52(6):925-33.
Staunton DE, Marlin SD, Stratowa C, Dustin ML, Springer TA.
Laboratory of Membrane Immunochemistry, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.
Intercellular adhesion molecule 1 (ICAM-1) is a 90 kd inducible surface glycoprotein that promotes adhesion in immunological and inflammatory reactions. ICAM-1 is a ligand of lymphocyte function-associated antigen-1 (LFA-1), an alpha beta complex that is a member of the integrin family of cell-cell and cell-matrix receptors. ICAM-1 is encoded by an inducible 3.3 kb mRNA. The amino acid sequence specifies an integral membrane protein with an extracellular domain of 453 residues containing five immunoglobulin-like domains. Highest homology is found with neural cell adhesion molecule (NCAM) and myelin-associated glycoprotein (MAG), which also contain five Ig-like domains. NCAM and MAG are nervous system adhesion molecules, but unlike ICAM-1, NCAM is homophilic. The ICAM-1 and LFA-1 interaction is heterophilic and unusual in that it is between members of the immunoglobulin and intergrin families. Unlike other integrin ligands, ICAM-1 does not contain an RGD sequence.