HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mou, Y. Articles by Wilkins, J. A. Search for Related Content PubMed PubMed Citation Articles by Mou, Y. Articles by Wilkins, J. A.

The Selective Inhibition of ß₁ and ß₇ Integrin-Mediated Lymphocyte Adhesion by Bacitracin¹

Yanglong Mou^,*,, Heyu Ni^,* and John A. Wilkins^2,,*,,§

^* The Rheumatic Diseases Research Laboratory and Departments of Immunology, Medical Microbiology, and ^§ Medicine, University of Manitoba, Winnipeg, Canada

Integrins play an important role in lymphocyte adhesion to cellular and extracellular components of their microenvironment. The regulation of such adhesion often involves changes in the functional state of the integrins rather than alterations in their expression levels. Although the functional basis for such transitions is unknown, a possible role for disulfide exchange might be postulated based on the observations that integrin function can be activated by bifunctional reducing agents or by Abs that react with areas adjacent to predicted long-range disulfide bonds in integrins. Recently, it has been reported that enzymes that catalyze disulfide exchanges such as protein disulfide isomerase (PDI) are present on the surface of lymphoid cells, raising the possibility that such enzymes might be involved in the control of lymphocyte adhesion. A number of inhibitors of PDI function were examined for their effects on integrin-mediated adherence of T cells. The results did not support role for PDI in the regulation of integrin function, as the inhibitors somatostatin A, tocinoic acid, dithiobisnitrobenzoic acid, and anti-PDI mAb did not interfere with adherence. However, one of the PDI inhibitors, bacitracin, selectively interfered with the ß₁ integrin-mediated adherence of lymphoid cells to collagen, fibronectin, laminin, and VCAM-1, and with ₄ß₇-dependent adherence to fibronectin and to VCAM-1. In contrast, _vß₃- and _Lß₂-mediated adherence were not inhibited. Thus, it appears that bacitracin may be a selective inhibitor of ß₁ and ß₇ integrin functions by an as yet unknown mechanism.

This article has been cited by other articles:

				P. E. Lovat, M. Corazzari, J. L. Armstrong, S. Martin, V. Pagliarini, D. Hill, A. M. Brown, M. Piacentini, M. A. Birch-Machin, and C. P.F. Redfern Increasing Melanoma Cell Death Using Inhibitors of Protein Disulfide Isomerases to Abrogate Survival Responses to Endoplasmic Reticulum Stress Cancer Res., July 1, 2008; 68(13): 5363 - 5369. [Abstract] [Full Text] [PDF]

				S. Jain, L. W. McGinnes, and T. G. Morrison Thiol/Disulfide Exchange Is Required for Membrane Fusion Directed by the Newcastle Disease Virus Fusion Protein J. Virol., March 1, 2007; 81(5): 2328 - 2339. [Abstract] [Full Text] [PDF]

				J. Lahav, E. M. Wijnen, O. Hess, S. W. Hamaia, D. Griffiths, M. Makris, C. G. Knight, D. W. Essex, and R. W. Farndale Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin {alpha}2{beta}1 Blood, September 15, 2003; 102(6): 2085 - 2092. [Abstract] [Full Text] [PDF]

				A. Beardsley and L. O'Donnell Characterization of Normal Spermiation and Spermiation Failure Induced by Hormone Suppression in Adult Rats Biol Reprod, April 1, 2003; 68(4): 1299 - 1307. [Abstract] [Full Text] [PDF]

				S. O'Neill, A. Robinson, A. Deering, M. Ryan, D. J. Fitzgerald, and N. Moran The Platelet Integrin alpha IIbbeta 3 Has an Endogenous Thiol Isomerase Activity J. Biol. Chem., November 17, 2000; 275(47): 36984 - 36990. [Abstract] [Full Text] [PDF]