Title: Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. | Journal: Current biology : CB. 1994 Nov;4(11):965-72 | Authors: Kelm S, Pelz A, Schauer R, Filbin MT, Tang S, de Bellard ME, Schnaar RL, Mahoney JA, Hartnell A, Bradfield P. | Abstract: Protein-carbohydrate interactions are believed to be important in many biological processes that involve cell-cell communication. Apart from the selectins, the only well-characterized vertebrate sialic acid-dependent adhesion molecules are CD22 and sialoadhesin; CD22 is a member of the immunoglobulin superfamily that is expressed by B lymphocytes and sialoadhesin is a macrophage receptor. The recent cloning of the gene encoding sialoadhesin has shown that it is also immunoglobulin-like. Both proteins share sequence similarity with the myelin-associated glycoprotein, an adhesion molecule of oligodendrocytes and Schwann cells that has been implicated in the process of myelination, raising the important question of whether myelin-associated glycoprotein is also a sialic acid-binding protein. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/7533044 |
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