Abstract：
:Of the several families of adhesion receptors involved in leukocyte-endothelial cell interactions, only the selectins have been shown to initiate leukocyte interaction under physiologic shear; indeed, beta 2 (CD18) intergrins responsible for neutrophil arrest are unable to engage without prior selectin-mediated rolling. In contrast, alpha 4 (CD49d) integrins are shown here to initiate lymphocyte contract ("tethering") in vitro under shear and in the absence of a selectin contribution. The alpha 4 integrin ligands MAdCAM-1 and VCAM-1 support loose reversible interactions including rolling, as well as rapid sticking and arrest that is favored following integrin activation. Moreover, alpha 4 beta 7 mediates L-selectin (CD62L)-independent attachment of blood-borne lymphocytes to lamina propria venules in situ. Scanning electron microscopy of alpha 4 beta 7hi lymphoid cells reveals that, like L-selectin, alpha 4 beta 7 is highly concentrated on microvillous sites of initial cellular contact, whereas the beta 2 integrin LFA-1 is excluded from villi. Thus, alpha 4 but not beta 2 integrins can initiate leukocyte adhesion under flow, a capacity that may be in part a function of topographic presentation on microvilli.
journal_name
Celljournal_title
Cellauthors
Berlin C,Bargatze RF,Campbell JJ,von Andrian UH,Szabo MC,Hasslen SR,Nelson RD,Berg EL,Erlandsen SL,Butcher ECdoi
10.1016/0092-8674(95)90491-3subject
Has Abstractpub_date
1995-02-10 00:00:00pages
413-22issue
3eissn
0092-8674issn
1097-4172pii
0092-8674(95)90491-3journal_volume
80pub_type
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