scholarly journals Loss of Fas apoptosis inhibitory molecule leads to spontaneous obesity and hepatosteatosis

2016 ◽  
Vol 7 (2) ◽  
pp. e2091-e2091 ◽  
Author(s):  
J Huo ◽  
Y Ma ◽  
J-J Liu ◽  
Y S Ho ◽  
S Liu ◽  
...  
Keyword(s):  
Inhibitory Molecule ◽  
Fas Apoptosis Inhibitory Molecule

scholarly journals Nomenclature of Toso, Fas Apoptosis Inhibitory Molecule 3, and IgM FcR

2015 ◽  
Vol 194 (9) ◽  
pp. 4055-4057 ◽  
Author(s):  
Hiromi Kubagawa ◽  
Michael C. Carroll ◽  
Chaim O. Jacob ◽  
Karl S. Lang ◽  
Kyeong-Hee Lee ◽  
...  
Keyword(s):  
Inhibitory Molecule ◽  
Fas Apoptosis Inhibitory Molecule

scholarly journals FAIM: An Antagonist of Fas-Killing and Beyond

Cells ◽  
2019 ◽  
Vol 8 (6) ◽  
pp. 541 ◽  
Author(s):  
Jianxin Huo ◽  
Shengli Xu ◽  
Kong-Peng Lam
Keyword(s):  
Molecular Mechanisms ◽  
Cell Receptor ◽  
Primary Role ◽  
The Past ◽  
Pathological Conditions ◽  
Apoptotic Protein ◽  
Evolutionarily Conserved ◽  
Inhibitory Molecule ◽  
Alternatively Spliced ◽  
Fas Apoptosis Inhibitory Molecule

Fas Apoptosis Inhibitory Molecule (FAIM) is an anti-apoptotic protein that is up-regulated in B cell receptor (BCR)-activated B cells and confers upon them resistance to Fas-mediated cell death. Faim has two alternatively spliced isoforms, with the short isoform ubiquitously expressed in various tissues and the long isoform mainly found in the nervous tissues. FAIM is evolutionarily conserved but does not share any significant primary sequence homology with any known protein. The function of FAIM has been extensively studied in the past 20 years, with its primary role being ascribed to be anti-apoptotic. In addition, several other functions of FAIM were also discovered in different physiological and pathological conditions, such as cell growth, metabolism, Alzheimer’s disease and tumorigenesis. However, the detailed molecular mechanisms underlying FAIM’s role in these conditions remain unknown. In this review, we summarize comprehensively the functions of FAIM in these different contexts and discuss its potential as a diagnostic, prognostic or therapeutic target.

scholarly journals A Novel Gene Coding for a Fas Apoptosis Inhibitory Molecule (FAIM) Isolated from Inducibly Fas-resistant B Lymphocytes

1999 ◽  
Vol 189 (6) ◽  
pp. 949-956 ◽  
Author(s):  
Thomas J. Schneider ◽  
Gavin M. Fischer ◽  
Terrence J. Donohoe ◽  
Thomas P. Colarusso ◽  
Thomas L. Rothstein
Keyword(s):  
B Cells ◽  
Time Course ◽  
Fas Ligand ◽  
Parp Cleavage ◽  
New Class ◽  
B Lymphoma Cells ◽  
Gene Coding ◽  
Inhibitory Molecule ◽  
Lymphocyte Homeostasis ◽  
Fas Apoptosis Inhibitory Molecule

The sensitivity of primary splenic B cells to Fas-mediated apoptosis is modulated in a receptor-specific fashion. Here we used a differential display strategy to detect cDNAs present in B cells rendered Fas resistant but absent in those rendered Fas sensitive. This led to the cloning and characterization of a novel 1.2-kb gene that encodes a Fas apoptosis inhibitory molecule (FAIM). faim-transfected BAL-17 B lymphoma cells were less sensitive by half or more to Fas-mediated apoptosis than were vector-transfected controls, using Fas ligand–bearing T cells or a cytotoxic anti-Fas antibody to trigger Fas, and this was associated with inhibition of Fas- induced poly-ADP ribose polymerase (PARP) cleavage. In primary B cells, the time course of faim mRNA and FAIM protein expression correlated with the induction of Fas resistance by surface (s)Ig engagement. Thus, FAIM is an inducible effector molecule that mediates Fas resistance produced by sIg engagement in B cells. However, faim is broadly expressed in various tissues and the faim sequence is highly conserved evolutionarily, suggesting that its role extends beyond lymphocyte homeostasis. As FAIM has no significant regions of homology to other gene products that modulate Fas killing, it appears to represent a distinct, new class of antiapoptotic protein.

scholarly journals FAIM opposes stress-induced loss of viability and blocks the formation of protein aggregates

2019 ◽  
Author(s):  
Hiroaki Kaku ◽  
Thomas L. Rothstein
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Disease Onset ◽  
Protein Aggregates ◽  
Ubiquitinated Protein ◽  
Free System ◽  
Inhibitory Molecule ◽  
Fas Apoptosis Inhibitory Molecule ◽  
Shock Proteins

AbstractA number of proteinopathies are associated with accumulation of misfolded proteins, which form pathological insoluble deposits. It is hypothesized that molecules capable of blocking formation of such protein aggregates might avert disease onset or delay disease progression. Here we report that Fas Apoptosis Inhibitory Molecule (FAIM) counteracts stress-induced loss of viability. We found that levels of ubiquitinated protein aggregates produced by cellular stress are much greater in FAIM-deficient cells and tissues. Moreover, in an in vitro cell-free system, FAIM specifically and directly prevents pathological protein aggregates without participation by other cellular elements, in particular the proteasomal and autophagic systems. Although this activity is similar to the function of heat shock proteins (HSPs), FAIM, which is highly conserved throughout evolution, bears no homology to any other protein, including HSPs. These results identify a new actor that protects cells against stress-induced loss of viability by preventing protein aggregates.

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