𝔖 Bobbio Scriptorium
✦   LIBER   ✦

BAFF binding to T cell-expressed BAFF-R costimulates T cell proliferation and alloresponses

✍ Scribed by Qunrui Ye; Liqing Wang; Andrew D. Wells; Ran Tao; Rongxiang Han; Anne Davidson; Martin L. Scott; Wayne W. Hancock


Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
432 KB
Volume
34
Category
Article
ISSN
0014-2980

No coin nor oath required. For personal study only.

✦ Synopsis


Abstract

Binding of the TNF family member, B cell activating factor (BAFF), to its receptor (BAFF‐R, TNFRSF13C) is required for generation and maintenance of mature B cells, but there are no data as to any role for the BAFF/BAFF‐R pathway in T cell functions. We report that the binding of BAFF to BAFF‐R expressed by a subset of primarily CD4^+^ T cells costimulates T cell activation and allo‐proliferation in vitro and in vivo, and that mice with a mutation in the BAFF‐R, or with a targeted deletion of BAFF, show prolonged cardiac allograft survival as compared to wild‐type or transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI)^–/–^ controls. Taken together, these data indicate the BAFF/BAFF‐R pathway contributes to both T and B cell responses and may be an attractive target for control of acute and chronic allograft rejection.


📜 SIMILAR VOLUMES


Enhanced expression of human T-cell leuk
✍ Florry A. Vyth-Dreese; Jan E. De Vries 📂 Article 📅 1983 🏛 John Wiley and Sons 🌐 French ⚖ 847 KB

## Abstract Peripheral blood T cells from a patient with T‐cell chronic lymphocytic leukemia (T‐CLL) failed to respond to mitogenic lectins or alloantigens but could be induced to proliferate by the addition of exogenous interleukin‐2 (IL‐2). The T‐CLL cells also proliferated in response to 12‐__O_

Binding, internalization, and degradatio
✍ Kenneth D. Brown; Yun-Chi Yeh; Robert W. Holley 📂 Article 📅 1979 🏛 John Wiley and Sons 🌐 English ⚖ 852 KB

## Abstract Epidermal growth factor (EGF) stimulates the growth of both benzo[a]pyrene‐transformed Balb 3T3 cells (BP3T3) and untransformed Balb 3T3 cells. We describe here the binding, internalization, and degradation of [^125^I]‐EGF by BP3T3 cells and 3T3 cells. Binding of [^125^I]‐EGF reaches a