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Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domains.

1994; Springer Nature; Volume: 13; Issue: 19 Linguagem: Inglês

10.1002/j.1460-2075.1994.tb06771.x

1460-2075

Paul R. Crocker, S. Mucklow, Veronique Bouckson-Castaing Bouckson, Andrew McWilliam, Anthony C. Willis, Siamon Gordon, Geneviève Milon, Sørge Kelm, Paul F. Bradfield,

Proteoglycans and glycosaminoglycans research

Research Article3 October 1994free access Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domains. P.R. Crocker P.R. Crocker Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author S. Mucklow S. Mucklow Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author V. Bouckson V. Bouckson Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author A. McWilliam A. McWilliam Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author A.C. Willis A.C. Willis Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author S. Gordon S. Gordon Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author G. Milon G. Milon Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author S. Kelm S. Kelm Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author P. Bradfield P. Bradfield Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author P.R. Crocker P.R. Crocker Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author S. Mucklow S. Mucklow Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author V. Bouckson V. Bouckson Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author A. McWilliam A. McWilliam Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author A.C. Willis A.C. Willis Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author S. Gordon S. Gordon Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author G. Milon G. Milon Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author S. Kelm S. Kelm Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author P. Bradfield P. Bradfield Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. Search for more papers by this author Author Information P.R. Crocker1, S. Mucklow1, V. Bouckson1, A. McWilliam1, A.C. Willis1, S. Gordon1, G. Milon1, S. Kelm1 and P. Bradfield1 1Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Headington, Oxford, UK. The EMBO Journal (1994)13:4490-4503https://doi.org/10.1002/j.1460-2075.1994.tb06771.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Sialoadhesin is a macrophage-restricted adhesion molecule of 185 kDa that mediates sialic acid-dependent binding to cells. It is expressed strongly by macrophages in lymphoid and haemopoietic tissues where it is likely to mediate cell-cell interactions. Here we report the molecular cloning of murine sialoadhesin and show that it is a new member of the immunoglobulin (Ig) superfamily with 17 Ig-like domains. COS cells transfected with a cDNA encoding full-length sialoadhesin bound mouse bone marrow cells in a sialic acid-dependent manner. Alternatively spliced cDNAs, predicting soluble forms of sialoadhesin containing the first three or 16 Ig-like domains of sialoadhesin, were expressed in COS cells and the respective proteins purified. When immobilized on plastic, the 16-domain form bound cells in a sialic acid-dependent manner, suggesting that sialoadhesin can function in both secreted and membrane-bound forms. The most similar proteins in the database were CD22, myelin-associated glycoprotein, Schwann cell myelin protein and CD33. Like sialoadhesin, CD22 mediates sialic acid-dependent cell adhesion. The sequence similarity of sialoadhesin to CD22 and related members of the Ig superfamily indicates the existence of a novel family of sialic acid binding proteins involved in cell-cell interactions. Previous ArticleNext Article Volume 13Issue 191 October 1994In this issue RelatedDetailsLoading ...