A Lymphotoxin-β-Specific Receptor

Paul D. Crowe(University of California, Riverside), Todd VanArsdale(University of California, Riverside), Barbara Walter(University of California, Riverside), Carl F. Ware(University of California, Riverside), Catherine Hession(Biogen (United States)), Barbara Ehrenfels(Biogen (United States)), Jeffrey L. Browning(University of California, Riverside), Wenie S. Din(Research & Development Corporation), Raymond G. Goodwin(Research & Development Corporation), Craig A. Smith(University of California, Riverside)
Science
April 29, 1994
10.1126/science.8171323
Cited by 396

Abstract

Tumor necrosis factor (TNF) and lymphotoxin-alpha (LT-alpha) are members of a family of secreted and cell surface cytokines that participate in the regulation of immune and inflammatory responses. The cell surface form of LT-alpha is assembled during biosynthesis as a heteromeric complex with lymphotoxin-beta (LT-beta), a type II transmembrane protein that is another member of the TNF ligand family. Secreted LT-alpha is a homotrimer that binds to distinct TNF receptors of 60 and 80 kilodaltons; however, these receptors do not recognize the major cell surface LT-alpha-LT-beta complex. A receptor specific for human LT-beta was identified, which suggests that cell surface LT may have functions that are distinct from those of secreted LT-alpha.

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