High expression of TIAF-1 in chronic kidney and liver allograft rejection and in activated T-helper cells1

Leij, Judith van der; Berg, Anke van den; Albrecht, Ester W.J.A.; Blokzijl, Tjasso; Roozendaal, Ramon; Gouw, Annette S.H.; Jong, Koert P. de; Stegeman, Coen A.; Goor, Harry van; Chang, Nan Shan; Poppema, Sibrand

doi:10.1097/01.tp.0000069829.71088.88

Cited by 18 publications

(11 citation statements)

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“…Most intriguingly, the level of TIAF1 is significantly increased in patients with chronic kidney and liver allograft rejection and in their activated TH2 helper T lymphocytes (Van Der Leij et al, 2003). Although the underlying mechanisms are poorly understood, we believe that TIAF1 may regulate the TH2 response, by either regulating cytokine production or TH2 cell proliferation, which leads to chronic allograft rejection.…”

Section: Discussionmentioning

confidence: 95%

TIAF1 and p53 Functionally Interact in Mediating Apoptosis and Silencing of TIAF1 Abolishes Nuclear Translocation of Serine 15-Phosphorylated p53

Schultz

Khera

Sleve

et al. 2004

DNA and Cell Biology

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TIAF1 is a TGF-beta 1-induced factor that protects L929 fibroblasts from TNF-mediated apoptosis. In contrast, overexpressed TIAF1 induces growth inhibition and apoptosis of monocytic U937 and various nonfibroblast cells. TIAF1-mediated apoptosis of U937 cells involves upregulation of p53, p21, and Smad2/4, but downregulation of ERK phosphorylation. To determine whether p53 and TIAF1 functionally interact in regulating cell death, ectopic TIAF1 and p53 were shown to induce apoptosis of U937 cells in both synergistic and antagonistic manners. At optimal levels both TIAF1 and p53 mediated apoptosis cooperatively. Also, both proteins suppressed adherence-independent growth of L929 cells. In contrast, initiation of apoptosis by overexpressed TIAF1 was blocked by low doses of p53, and vice versa. Furthermore, ectopic p53 blocked an ongoing apoptosis in U937 cells stably expressing TIAF1. Yeast two-hybrid analyses failed to demonstrate the binding of p53 with TIAF1, suggesting an unidentified protein that links the p53/TIFA1 interaction. Suppression of TIAF1 expression by siRNA could not inhibit Ser15 phosphorylation in p53 in response to UV and etoposide. However, nuclear translocation of these Ser15-phosphorylated p53 was significantly reduced in TIAF1-silenced cells. Taken together, TIAF1 and p53 functionally interact in regulating apoptosis, and TIAF1 is likely to participate in the nuclear translocation of activated p53.

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Section: Discussionmentioning

confidence: 95%

TIAF1 and p53 Functionally Interact in Mediating Apoptosis and Silencing of TIAF1 Abolishes Nuclear Translocation of Serine 15-Phosphorylated p53

Schultz

Khera

Sleve

et al. 2004

DNA and Cell Biology

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“…Both TP53INP1 and TIAF1 genes were found to be overexpressed in the naturally occurring T Reg cells in our study. Apart from this, TIAF1 is known to be upregulated in T h 2 compared with T h 1 lymphocytes, and a functional role as an apoptosis protector has been discussed [31]. …”

Section: Resultsmentioning

confidence: 99%

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et al. 2006

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This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. T regulatory cell signatures

Comparison of the gene expression in human T regulatory cells and naïve cells using a T regulatory cell-specific microarray reveals cellspecific gene signatures.

Abstract Background: Naturally occurring CD4 + CD25 + regulatory T cells (T Reg ) are involved in the control of autoimmune diseases, transplantation tolerance, and anti-tumor immunity. Thus far, genomic studies on T Reg cells were restricted to murine systems, and requirements for their development, maintenance, and mode of action in humans are poorly defined.

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“…TIAF1, a 12-kDa TIAF1, 6 participates in TGF- β signaling 7 and controls p53 activation. 8 TIAF1 is implicated in the activation of TH2 helper T lymphocytes in chronic organ rejection 9 and development of regulatory T cells, 10 as well as association with Hirschsprung's disease. 11 TIAF1 tends to aggregate, and the protein aggregates are found in the hippocampi of postmortem nondemented humans and AD patients.…”

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confidence: 99%

TGF-β induces TIAF1 self-aggregation via type II receptor-independent signaling that leads to generation of amyloid β plaques in Alzheimer's disease

et al. 2010

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The role of a small transforming growth factor beta (TGF-β)-induced TIAF1 (TGF-β1-induced antiapoptotic factor) in the pathogenesis of Alzheimer's disease (AD) was investigated. TIAF1 physically interacts with mothers against DPP homolog 4 (Smad4), and blocks SMAD-dependent promoter activation when overexpressed. Accordingly, knockdown of TIAF1 by small interfering RNA resulted in spontaneous accumulation of Smad proteins in the nucleus and activation of the promoter governed by the SMAD complex. TGF-β1 and environmental stress (e.g., alterations in pericellular environment) may induce TIAF1 self-aggregation in a type II TGF-β receptor-independent manner in cells, and Smad4 interrupts the aggregation. Aggregated TIAF1 induces apoptosis in a caspase-dependent manner. By filter retardation assay, TIAF1 aggregates were found in the hippocampi of nondemented humans and AD patients. Total TIAF1-positive samples containing amyloid β (Aβ) aggregates are 17 and 48%, respectively, in the nondemented and AD groups, suggesting that TIAF1 aggregation occurs preceding formation of Aβ. To test this hypothesis, in vitro analysis showed that TGF-β-regulated TIAF1 aggregation leads to dephosphorylation of amyloid precursor protein (APP) at Thr668, followed by degradation and generation of APP intracellular domain (AICD), Aβ and amyloid fibrils. Polymerized TIAF1 physically interacts with amyloid fibrils, which would favorably support plaque formation in vivo.

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High expression of TIAF-1 in chronic kidney and liver allograft rejection and in activated T-helper cells1

Cited by 18 publications

References 30 publications

TIAF1 and p53 Functionally Interact in Mediating Apoptosis and Silencing of TIAF1 Abolishes Nuclear Translocation of Serine 15-Phosphorylated p53

TIAF1 and p53 Functionally Interact in Mediating Apoptosis and Silencing of TIAF1 Abolishes Nuclear Translocation of Serine 15-Phosphorylated p53

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TGF-β induces TIAF1 self-aggregation via type II receptor-independent signaling that leads to generation of amyloid β plaques in Alzheimer's disease

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