Tony W. Liang
Brigham and Women's Hospital
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Publication
Featured researches published by Tony W. Liang.
Journal of Immunology | 2002
Tony W. Liang; Henry H. Chiu; Austin L. Gurney; Aiko Sidle; Daniel Tumas; Peter Schow; Jessica Foster; Toni Klassen; Kathryn Dennis; Richard DeMarco; Thinh Pham; Gretchen Frantz; Sherman Fong
Screening expressed sequence tag databases for endothelial-specific homologs to human junctional adhesion molecule (JAM) and A33-Ag, we identified a protein of 298 aa that represents the recently described vascular endothelial-JAM (VE-JAM)/JAM 2. We confirmed VE-JAM/JAM 2 expression to be restricted to the high endothelial venule of tonsil and lymph nodes, and we further expanded the localization to the endothelium of arterioles in and around inflammatory and tumor foci. In our functional characterizations of VE-JAM/JAM 2, we discovered that it can function as an adhesive ligand for the T cell line J45 and can interact with GM-CSF/IL-4-derived peripheral blood dendritic cells, circulating CD56+ NK cells, circulating CD56+CD3+ NK/T cells, and circulating CD56+CD3+CD8+ cytolytic T cells. In the course of our studies, we also isolated and characterized the functional VE-JAM/JAM 2 receptor, which, upon cloning, turned out to be a submitted sequence representing JAM 3 (accession number NP 113658). With these understandings, we have characterized a protein-interacting pair that can be important in the role of T, NK, and dendritic cell trafficking and inflammation.
Journal of Immunology | 2007
Monica Sircar; Paul F. Bradfield; Michel Aurrand-Lions; Richard J. Fish; Pilar Alcaide; Lin Yang; Gail Newton; Deanna J. Lamont; Seema Sehrawat; Tanya N. Mayadas; Tony W. Liang; Charles A. Parkos; Beat A. Imhof; Francis W. Luscinskas
Endothelial cell junctional adhesion molecule (JAM)-C has been proposed to regulate neutrophil migration. In the current study, we used function-blocking mAbs against human JAM-C to determine its role in human leukocyte adhesion and transendothelial cell migration under flow conditions. JAM-C surface expression in HUVEC was uniformly low, and treatment with inflammatory cytokines TNF-α, IL-1β, or LPS did not increase its surface expression as assessed by FACS analysis. By immunofluorescence microscopy, JAM-C staining showed sparse localization to cell-cell junctions on resting or cytokine-activated HUVEC. Surprisingly, staining of detergent-permeabilized HUVEC revealed a large intracellular pool of JAM-C that showed little colocalization with von Willebrand factor. Adhesion studies in an in vitro flow model showed that functional blocking JAM-C mAb alone had no inhibitory effect on polymorphonuclear leukocyte (PMN) adhesion or transmigration, whereas mAb to ICAM-1 significantly reduced transmigration. Interestingly, JAM-C-blocking mAbs synergized with a combination of PECAM-1, ICAM-1, and CD99-blocking mAbs to inhibit PMN transmigration. Overexpression of JAM-C by infection with a lentivirus JAM-C GFP fusion protein did not increase adhesion or extent of transmigration of PMN or evoke a role for JAM-C in transendothelial migration. These data suggest that JAM-C has a minimal role, if any, in PMN transmigration in this model and that ICAM-1 is the preferred endothelial-expressed ligand for PMN β2 integrins during transendothelial migration.
Gastroenterology | 1998
L.B. Balsam; Tony W. Liang; Charles A. Parkos
In the intestine, lung, and urinary tract, neutrophil (polymorphonuclear leukocyte, PMN) transepithelial migration is dependent on the leukocyte beta2 integrin CD11b/CD18. While the regions of CD11b involved in recognition of several soluble ligands are known, those that mediate PMN-epithelial interactions have not been investigated. In this study, mAbs reactive with four extracellular regions on CD11b, the NH2-terminal region, I (inserted) domain, cation-binding region, and region proximal to the transmembrane domain (C domain), were analyzed for the ability to block CD11b/CD18-mediated interactions with T84 intestinal epithelial cells. In such a manner, epitope mapping was applied to the complex interactions between CD11b/CD18 and a cell-based ligand system. I domain Abs strongly inhibited both adhesion of PMN to epithelial cells and PMN migration across T84 epithelial monolayers. However, the profile of inhibition was distinct from that of other known ligands of CD11b/CD18. CBRM1/32, an Ab to a discontinuous epitope residing within the NH2- and cation-binding domains, strongly inhibited both adhesion and transmigration responses. C domain Abs had minimal effects on adhesion and transmigration. These findings appear applicable to other epithelia, since similar results were obtained in transmigration experiments with CF15 human airway epithelial cells. Finally, Ab inhibition profiles were confirmed with adhesion assays of isolated epithelial cells to purified CD11b/CD18. These findings demonstrate the central role of the I domain and the participation of a discontinuous region shared by the NH2- and cation-binding domains in mediating PMN-adhesive interactions with epithelial cells.
Molecular Medicine | 1996
Charles A. Parkos; Sean P. Colgan; Michael S. Diamond; Asma Nusrat; Tony W. Liang; Timothy A. Springer; James L. Madara
Gastroenterology | 1997
Asma Nusrat; Charles A. Parkos; Tony W. Liang; Denice K. Carnes; James L. Madara
Blood | 1999
Luca Mazzucchelli; James B. Burritt; Algirdas J. Jesaitis; Asma Nusrat; Tony W. Liang; Andrew T. Gewirtz; Frederick J. Schnell; Charles A. Parkos
Journal of Immunology | 1998
Leora B. Balsam; Tony W. Liang; Charles A. Parkos
Infection and Immunity | 1999
Heather A. Edens; Charles A. Parkos; Tony W. Liang; Algirdas J. Jesaitis; Jim E. Cutler; Heini M. Miettinen
Archive | 2013
Gretchen Frantz; Sherman Fong; Kathryn Dennis; Richard DeMarco; Thinh Pham; Daniel Tumas; Peter Schow; Jessica Foster; Toni Klassen; Tony W. Liang; Henry H. Chiu; Austin L. Gurney; Aiko Sidle
The FASEB Journal | 2008
Abigail Betanzos; Michael Schnoor; Eric A. Severson; Tony W. Liang; Charles A. Parkos