Correction of the spontaneous and DEB-induced chromosomal aberrations in Fanconi anemia cells of the FA(C) complementation group by the FACC gene

1996 ◽  
Vol 72 (2-3) ◽  
pp. 194-196 ◽  
Author(s):  
D.J. Stavropoulos ◽  
S. Sood ◽  
D.J. Tomkins ◽  
M. Buchwald
Keyword(s):  
Fanconi Anemia ◽  
Chromosomal Aberrations ◽  
Complementation Group

scholarly journals A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M

2005 ◽  
Vol 37 (9) ◽  
pp. 958-963 ◽  
Author(s):  
Amom Ruhikanta Meetei ◽  
Annette L Medhurst ◽  
Chen Ling ◽  
Yutong Xue ◽  
Thiyam Ramsing Singh ◽  
...  
Keyword(s):  
Dna Repair ◽  
Fanconi Anemia ◽  
Complementation Group ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Human Ortholog

Cellular characterization of cells from the Fanconi anemia complementation group, FA-D1/BRCA2

2006 ◽  
Vol 601 (1-2) ◽  
pp. 191-201 ◽  
Author(s):  
Barbara C. Godthelp ◽  
Paul P.W. van Buul ◽  
Nicolaas G.J. Jaspers ◽  
Elhaam Elghalbzouri-Maghrani ◽  
Annemarie van Duijn-Goedhart ◽  
...  
Keyword(s):  
Fanconi Anemia ◽  
Complementation Group

scholarly journals Identification of Cytosolic Proteins That Bind to the Fanconi Anemia Complementation Group C Polypeptidein Vitro

1995 ◽  
Vol 270 (17) ◽  
pp. 9876-9882 ◽  
Author(s):  
Hagop Youssoufian ◽  
Arleen D. Auerbach ◽  
Peter C. Verlander ◽  
Viktor Steimle ◽  
Bernard Mach
Keyword(s):  
Fanconi Anemia ◽  
Complementation Group ◽  
Cytosolic Proteins

Associations of complementation group, ALDH2 genotype, and clonal abnormalities with hematological outcome in Japanese patients with Fanconi anemia

2018 ◽  
Vol 98 (2) ◽  
pp. 271-280 ◽  
Author(s):  
Miharu Yabe ◽  
Takashi Koike ◽  
Keisuke Ohtsubo ◽  
Eri Imai ◽  
Tsuyoshi Morimoto ◽  
...  
Keyword(s):  
Fanconi Anemia ◽  
Japanese Patients ◽  
Complementation Group ◽  
Clonal Abnormalities

SNX5, a New Member of the Sorting Nexin Family, Binds to the Fanconi Anemia Complementation Group A Protein

1999 ◽  
Vol 265 (3) ◽  
pp. 630-635 ◽  
Author(s):  
Tetsuya Otsuki ◽  
Sachiko Kajigaya ◽  
Keiya Ozawa ◽  
Johnson M. Liu
Keyword(s):  
Fanconi Anemia ◽  
Complementation Group ◽  
Sorting Nexin ◽  
Group A

scholarly journals Localization of the Fanconi Anemia Complementation Group D Gene to a 200-kb Region on Chromosome 3p25.3

2000 ◽  
Vol 66 (5) ◽  
pp. 1540-1551 ◽  
Author(s):  
James A. Hejna ◽  
Cynthia D. Timmers ◽  
Carol Reifsteck ◽  
Donald A. Bruun ◽  
Lora W. Lucas ◽  
...  
Keyword(s):  
Fanconi Anemia ◽  
Complementation Group ◽  
Group D

Complementation group assignments in fanconi anemia fibroblast cell lines from North America

1997 ◽  
Vol 23 (1) ◽  
pp. 1-7 ◽  
Author(s):  
P. M. Jakobs ◽  
E. Fiddler-Odell ◽  
C. Reifsteck ◽  
S. Olson ◽  
R. E. Moses ◽  
...  
Keyword(s):  
North America ◽  
Cell Lines ◽  
Fanconi Anemia ◽  
Fibroblast Cell ◽  
Complementation Group ◽  
Fibroblast Cell Lines

scholarly journals The Fanconi anemia complementation group C protein corrects DNA interstrand cross-link-specific apoptosis in HSC536N cells

Blood ◽  
1996 ◽  
Vol 88 (6) ◽  
pp. 2298-2305 ◽  
Author(s):  
UK Marathi ◽  
SR Howell ◽  
RA Ashmun ◽  
TP Brent
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Fanconi Anemia ◽  
Complementation Group ◽  
Cross Linking ◽  
Wild Type ◽  
Cross Link ◽  
Cycle Arrest ◽  
Protein Functions ◽  
Induced Apoptosis

Fanconi anemia (FA) cells are hypersensitive to cytotoxicity, cell cycle arrest, and chromosomal aberrations induced by DNA cross-linking agents, such as mitomycin C (MMC) and nitrogen mustard (HN2). Although MMC hypersensitivity is complemented in a subset of FA cells (complementation group C [FA-C]) by wild-type FAC cDNA, the cytoprotective mechanism is unknown. In the current study, we tested the hypothesis that FAC protein functions in the suppression of DNA interstand cross-link (ISC)-induced cell cycle arrest and apoptosis. Comparison of HN2-induced cell cycle arrest and apoptosis with those of its non-cross-linking analogs, diethylaminoethyl chloride and 2- dimethylaminoethyl chloride, delineated the DNA ISC specificity of FAC- mediated cytoprotection. Overexpression of wild-type FAC cDNA in FA-C lymphoblasts (HSC536N cell line) prevented HN2-induced growth inhibition, G2 arrest, and DNA fragmentation that is characteristic of apoptosis. In contrast cytoprotection was not conferred against the effects of the non-cross-linking mustards. Our data show that DNA ISCs induce apoptosis more potently than do DNA monoadducts and suggest that FAC suppresses specifically DNA ISC-induced apoptosis in the G2 phase of the cell cycle.

Molecular Chaperone GRP94 Binds to the Fanconi Anemia Group C Protein and Regulates Its Intracellular Expression

Blood ◽  
1998 ◽  
Vol 91 (11) ◽  
pp. 4379-4386 ◽  
Author(s):  
Taizo Hoshino ◽  
Jianxiang Wang ◽  
Marcel P. Devetten ◽  
Nobuhisa Iwata ◽  
Sachiko Kajigaya ◽  
...  
Keyword(s):  
Fanconi Anemia ◽  
Molecular Chaperone ◽  
B Lymphocyte ◽  
Complementation Group ◽  
Splicing Mutation ◽  
Cytoplasmic Proteins ◽  
Intracellular Expression ◽  
Anemia Group

Abstract The FAC protein encoded by the gene defective in Fanconi anemia (FA) complementation group C binds to at least three ubiquitous cytoplasmic proteins in vitro. We used here the complete coding sequence ofFAC in a yeast two-hybrid screen to identify interacting proteins. The molecular chaperone GRP94 was isolated twice from a B-lymphocyte cDNA library. Binding was confirmed by coimmunoprecipitation of FAC and GRP94 from cytosolic, but not nuclear, lysates of transfected COS-1 cells, as well as from mouse liver cytoplasmic extracts. Deletion mutants of FAC showed that residues 103-308 were required for interaction with GRP94, and a natural splicing mutation within the IVS-4 of FAC that removes residues 111-148 failed to bind GRP94. Ribozyme-mediated inactivation of GRP94 in the rat NRK cell line led to significantly reduced levels of immunoreactive FAC and concomitant hypersensitivity to mitomycin C, similar to the cellular phenotype of FA. Our results demonstrate that GRP94 interacts with FAC both in vitro and in vivo and regulates its intracellular level in a cell culture model. In addition, the pathogenicity of the IVS-4 splicing mutation in the FAC gene may be mediated in part by its inability to bind to GRP94.

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