Death the Fas way: Regulation and pathophysiology of CD95 and its ligand

K. Sharma, R. X. Wang, L. Y. Zhang, D. L. Yin, X. Y. Luo, J. C. Solomon, R. F. Jiang, K. Markos, W. Davidson, D. W. Scott, Y. F. Shi*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

188 Scopus citations

Abstract

Apoptotic cell death mediated by the members of the tumor necrosis factor receptor family is an essential process involved in the regulation of cellular homeostasis during development, differentiation, and pathophysiological conditions. Among the cell death receptors comprising the tumor necrosis factor receptor superfamily, CD95/APO-1 (Fas) is the best characterized. The specific interaction of Fas with its cognate ligand, Fas ligand (FasL), elicits the activation of a death-inducing caspase (cysteine aspartic acid proteases) cascade, occurring in a transcription-independent manner. Caspase activation executes the apoptosis process by cleaving various intracellular substrates, leading to genomic DNA fragmentation, cell membrane blebbing, and the exposure of phagocytosis signaling molecules on the cell surface. Recent studies have shown that the Fas/FasL pathway plays an important role in regulating the life and death of the immune system through activation-induced cell death. In addition, these molecules have been implicated in aging, human immunodeficiency virus infection, drug abuse, stress, and cancer development. In this review, we will focus on the mechanisms that regulate Fas and FasL expression, and how their deregulation leads to diseases.

Original languageEnglish
Pages (from-to)333-347
Number of pages15
JournalPharmacology and Therapeutics
Volume88
Issue number3
DOIs
StatePublished - 2000
Externally publishedYes

Keywords

  • Apoptosis
  • Caspase
  • Fas/CD95
  • Immune responses
  • Ligand
  • TNF

Fingerprint

Dive into the research topics of 'Death the Fas way: Regulation and pathophysiology of CD95 and its ligand'. Together they form a unique fingerprint.

Cite this