LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin.

Focal adhesion (FA) consists of multiple cellular proteins including paxillin and serves as a center for adhesion-mediated signaling. The assembly and disassembly of FAs is regulated by locally produced intracellular signals, and tyrosine phosphorylation of paxillin has been implicated in this process. A Lin-11 Isl-1 Mec-3 (LIM) domain-containing adaptor protein, leupaxin, a member of the paxillin family, is expressed in leukocytes as well as in certain cancer cells, and shares overall structural characteristics with paxillin.

The expression of anamorsin in diffuse large B cell lymphoma: possible prognostic biomarker for low IPI patients.

Anamorsin is a cell-death-defying factor, which was originally isolated as a molecule that conferred resistance to apoptosis induced by growth factor starvation. In order to evaluate anamorsin expression levels in malignant lymphoma, we immunostained paraffin-embedded sections with anti-anamorsin monoclonal antibodies. About 40% (89/234) of sections from patients with diffuse large B cell lymphoma (DLBCL) showed strong anamorsin expression.

[Hypersensitivity reactions to multiple drugs during the course of hairy cell leukemia treated with 2-chlorodeoxyadenosine].

A 38-year-man developed diffuse erythema 3 days after the administration of 2-chlorodeoxyadenosine (cladribine or 2-CdA) and many other drugs for hairy cell leukemia (HCL). Patch-testing and scratch patch-testing showed positive reactions for clindamycin (10%, 30%) at 24 hours and 48 hours. Furthermore, provocation-testing showed positive reactions for sulfamethoxazole.

Lymphocyte binding to MAdCAM-1 via alpha4beta7 integrin activates a signal transduction pathway involving tyrosine phosphorylation of paxillin and p105(Cas-L).

Alpha4beta7 integrin mediates lymphocyte trafficking to mucosal lymphoid organs by interacting with the mucosal vascular addressin MAdCAM-1. While the structural basis for the alpha4beta7 integrin-MAdCAM-1 interaction has been well characterized, less is known about the signal transduction pathways that regulate the alpha4beta7 integrin-mediated lymphocyte interaction with MAdCAM-1-expressing endothelial cells. Here we demonstrate that ligation of alpha4beta7 integrin with MAdCAM-1 induces a prominent tyrosine phosphorylation of paxillin and a 105-kDa protein (p105) that is reactive with an anti-p130(Cas) antibody, in the mouse T-cell line TK-1.