Search results for NFYB

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Species

Types

Compartments

Reaction types

Search properties

Protein (1 results from a total of 1)

Identifier: R-HSA-381067
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: NFYB: P25208

Reaction (3 results from a total of 3)

Identifier: R-HSA-9622572
Species: Homo sapiens
Compartment: nucleoplasm
Based on studies in rat neurons, the NF-Y transcription factor complex (composed of NFYA, NFYB and NFYC) and histone acetyltransferases EP300 (p300) and/or CREBBP (CBP) constitutively bind to evolutionarily conserved sites in the promoter of the BCL2L11 (BIM) gene (Hughes et al. 2011).
Identifier: R-HSA-9659680
Species: Homo sapiens
Compartment: plasma membrane, cytosol, extracellular region
The ATP-dependent translocase ABCB1 (also known as Multidrug resistance protein 1, or MDR1, P-glycoprotein, or PGP) is the best characterized xenobiotic transporter of the ABC transporter family (Shen et al. 1986, Gottesman and Pastan 1988). The ABCB1 gene maps to the chromosomal band 7q21, which is frequently gained or amplified in cancer (Genovese et al. 2017). Transcription of ABCB1 is negatively regulated by TP53 (p53) and positively regulated by CEBPB (C/EBPbeta), JUN (AP-1), NFYB (NF-Y) and YBX1 (YB-1) (Chen and Sikic 2012). ABCB1 is a 12-pass transmembrane protein with two ATP-binding domains (Chen et al. 1986, Gottesman et al. 2002). The question of how many molecules of ATP are hydrolyzed for the full conformational change cycle and export of xenobiotic substrates out of the cell is not settled. The best biochemical evidence is for one molecule of ATP (Shapiro and Ling, 1998; with a review of methods). Structural studies point to the binding of two molecules but do not allow statements about ATP hydrolysis stoichiometry (reviewed in Jones and George, 2020).


Many anti-cancer drugs and anti-inflammatory drugs, as well as some antibiotics, are exported from the cell by ABCB1 (reviewed by Ambudkar et al. 1999, Gottesman et al. 2002; International Transporter Consortium et al, 2010).

Anti-cancer drugs that are substrates of ABCB1 include:
actinomycin D (Horio et al. 1989, Ambudkar et al. 1992, Hill et al. 2013);
bisantrene (Zhang et al. 1994, Aksentijevich et al. 1996);
daunorubicin (Horio et al. 1989, Ambudkar et al. 1992);
docetaxel (Shirakawa et al. 1999);
doxorubicin (Ueda et al. 1987, Ambudkar et al. 1992);
etoposide (Pastan et al. 1988, Lincke et al. 1990, Klamt et al. 2008);
imatinib (Dai et al. 2003);
irinotecan (Paule et al. 2010, Tagen et al. 2010);
melphalan (Kühne et al. 2009);
paclitaxel (Jang et al. 2001);
temozolomide (Munoz et al. 2015);
teniposide (Boiocchi et al. 1992);
vinblastine (Ueda et al. 1987, Ambudkar et al. 1992);
vincristine (Horio et al. 1989).

Anti-inflammatory drugs that are substrates of ABCB1 include:
budenoside (Dilger et al. 2004);
colchicine (Ueda et al. 1987);
dexamethasone (Gruol et al. 1999, Yates et al. 2003);
methylprednisolone (Yates et al. 2003, Cuppen et al. 2017);
prednisolone (PREDL) (Karssen et al. 2002, Yates et al. 2003);
prednisone (PREDN) (Dilger et al. 2004).
The presence of 11-, 17-, and 21-hydroxyl groups appears to be a critical determinant for transport efficiency of steroids by the efflux pump ABCB1 (MDR1). Prednisone contains the 17-, and prednisolone both the 17- and 21-hydroxy groups, and both molecules are effectively exported out of cells expressing ABCB1, with reduced intracellular accumulation and toxicity (Yates et al, 2003).


Antibiotics that are substrates of ABCB1 include:
gramicidin D (Lincke et al. 1990, Mechetner and Roninson 1992);
azithromycin (Munić et al. 2010);
erythromycin (Dey et al. 2004, Munić et al. 2010).



Identifier: R-HSA-1467457
Species: Homo sapiens
Compartment: plasma membrane, cytosol, extracellular region
Some members of the ABC transporter superfamily are able to mediate the efflux of a broad range of cytotoxic drugs from cells, leading to the name multidrug resistance (MDR) proteins (Seeger and van Veen 2009). The ABCB1 (P-glycoprotein 1[PGP], multidrug resistance protein 1 [MRP1]) is the most characterised MDR (Shen et al. 1986, Gottesman & Pastan 1988). ABCB5 (Frank et al. 2005) and ABCA8 (Tsuruoka et al. 2002) are newer members of MDRs.

The ABCB1 (also known as MDR1, P-glycoprotein, or PGP) is the best characterized xenobiotic transporter of the ABC transporter family (Shen et al. 1986, Gottesman and Pastan 1988). The ABCB1 gene maps to the chromosomal band 7q21, which is frequently gained or amplified in cancer (Genovese et al. 2017). Transcription of ABCB1 is negatively regulated by TP53 (p53) and positively regulated by CEBPB (C/EBPbeta), JUN (AP-1), NFYB (NF-Y) and YBX1 (YB-1) (Chen and Sikic 2012). ABCB1 is a 12-pass transmembrane protein with two ATP-binding domains (Chen et al. 1986, Gottesman et al. 2002).The question of how many molecules of ATP are hydrolyzed for the full conformational change cycle and export of xenobiotic substrates out of the cell is not settled. The best biochemical evidence is for one molecule of ATP (Shapiro and Ling, 1998; with a review of methods). Structural studies point to the binding of two molecules but do not allow statements about ATP hydrolysis stoichiometry (reviewed in Jones and George, 2020).

Many anti-cancer drugs and anti-inflammatory drugs, as well as some antibiotics, are exported from the cell by ABCB1 (reviewed by Ambudkar et al. 1999, Gottesman et al. 2002).

Anti-cancer drugs that are substrates of ABCB1 include:
actinomycin D (Horio et al. 1989, Ambudkar et al. 1992, Hill et al. 2013);
bisantrene (Zhang et al. 1994, Aksentijevich et al. 1996);
daunorubicin (Horio et al. 1989, Ambudkar et al. 1992);
docetaxel (Shirakawa et al. 1999);
doxorubicin (Ueda et al. 1987, Ambudkar et al. 1992);
etoposide (Pastan et al. 1988, Lincke et al. 1990, Klamt et al. 2008);
imatinib (Dai et al. 2003);
irinotecan (Paule et al. 2010, Tagen et al. 2010);
melphalan (Kühne et al. 2009);
paclitaxel (Jang et al. 2001);
temozolomide (Munoz et al. 2015);
teniposide (Boiocchi et al. 1992);
vinblastine (Ueda et al. 1987, Ambudkar et al. 1992);
vincristine (Horio et al. 1989).

Anti-inflammatory drugs that are substrates of ABCB1 include:
budenoside (Dilger et al. 2004);
colchicine (Ueda et al. 1987);
dexamethasone (Gruol et al. 1999, Yates et al. 2003);
methylprednisolone (Yates et al. 2003, Cuppen et al. 2017);
prednisolone (PREDL) (Karssen et al. 2002, Yates et al. 2003);
prednisone (PREDN) (Dilger et al. 2004).
The presence of 11-, 17-, and 21-hydroxyl groups appears to be a critical determinant for transport efficiency of steroids by the efflux pump ABCB1 (MDR1). Prednisone contains the 17-, and prednisolone both the 17- and 21-hydroxy groups, and both molecules are effectively exported out of cells expressing ABCB1, with reduced intracellular accumulation and toxicity (Yates et al, 2003).


Antibiotics that are substrates of ABCB1 include:
gramicidin D (Lincke et al. 1990, Mechetner and Roninson 1992);
azithromycin (Munić et al. 2010);
erythromycin (Dey et al. 2004, Munić et al. 2010).
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