HSPA1A
出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2024/02/28 15:04 UTC 版)
HSPA1A（heat shock protein family A (Hsp70) member 1A）またはHSP70-1、Hsp72は、ヒトではHSPA1A遺伝子にコードされるタンパク質である[5][6]。Hsp70ファミリータンパク質、そしてシャペロンタンパク質の1つとして、新たに翻訳されたタンパク質や誤ったフォールディングをしたタンパク質が適切にフォールディングするよう促進するとともに、変異タンパク質の安定化や分解にも寄与する。さらに、DNA修復も促進する[7]。HSPA1Aの機能は、シグナル伝達、アポトーシス、タンパク質の恒常性、細胞成長、細胞分化などの生物学的過程に寄与している[6][8]。また、広範囲のがん、神経変性疾患、細胞老化や加齢、2型糖尿病や関節リウマチなどの炎症疾患とも関連している[8][9][10]。
- ^ a b c GRCh38: Ensembl release 89: ENSG00000234475、ENSG00000204389、ENSG00000237724、ENSG00000235941、ENSG00000215328 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000091971 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
- ^ a b c “Entrez Gene: HSPA1A heat shock 70kDa protein 1A”. 2024年2月28日閲覧。
- ^ a b c d e f g h “Hsp70 chaperones: cellular functions and molecular mechanism”. Cellular and Molecular Life Sciences 62 (6): 670–684. (Mar 2005). doi:10.1007/s00018-004-4464-6. PMC 2773841. PMID 15770419.
- ^ a b c “HspA1A facilitates DNA repair in human bronchial epithelial cells exposed to Benzo[apyrene and interacts with casein kinase 2”]. Cell Stress & Chaperones 19 (2): 271–9. (Mar 2014). doi:10.1007/s12192-013-0454-7. PMC 3933616. PMID 23979991.
- ^ a b c d e f “HSP72 and gp96 in gastroenterological cancers”. Clinica Chimica Acta; International Journal of Clinical Chemistry 417: 73–9. (Feb 2013). doi:10.1016/j.cca.2012.12.017. PMID 23266770.
- ^ a b “Chaperoning to the metabolic party: The emerging therapeutic role of heat-shock proteins in obesity and type 2 diabetes”. Molecular Metabolism 3 (8): 781–93. (Nov 2014). doi:10.1016/j.molmet.2014.08.003. PMC 4216407. PMID 25379403.
- ^ a b “Analysis of serum heat shock protein 70 (HSPA1A) concentrations for diagnosis and disease activity monitoring in patients with rheumatoid arthritis”. Cell Stress & Chaperones 20 (3): 537–43. (Mar 2015). doi:10.1007/s12192-015-0578-z. PMC 4406931. PMID 25739548.
- ^ a b c d e “Heat-shock protein 70 antagonizes apoptosis-inducing factor”. Nat. Cell Biol. 3 (9): 839–43. (September 2001). doi:10.1038/ncb0901-839. PMID 11533664.
- ^ a b c “Heat shock protein 72 suppresses apoptosis by increasing the stability of X-linked inhibitor of apoptosis protein in renal ischemia/reperfusion injury”. Mol Med Rep 11 (3): 1793–9. (2015). doi:10.3892/mmr.2014.2939. PMC 4270332. PMID 25394481.
- ^ a b “Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate”. PLOS ONE 9 (7): e103518. (2014). Bibcode: 2014PLoSO...9j3518Z. doi:10.1371/journal.pone.0103518. PMC 4110032. PMID 25058147.
- ^ “Extracellular Hsp72 concentration relates to a minimum endogenous criteria during acute exercise-heat exposure”. Cell Stress & Chaperones 19 (3): 389–400. (May 2014). doi:10.1007/s12192-013-0468-1. PMC 3982022. PMID 24085588.
- ^ “Crotonaldehyde induces heat shock protein 72 expression that mediates anti-apoptotic effects in human endothelial cells”. Toxicology Letters 223 (2): 116–23. (Nov 2013). doi:10.1016/j.toxlet.2013.09.010. PMID 24070736.
- ^ “Chaperoning to the metabolic party: The emerging therapeutic role of heat-shock proteins in obesity and type 2 diabetes”. Mol Metab 3 (8): 781–93. (2014). doi:10.1016/j.molmet.2014.08.003. PMC 4216407. PMID 25379403.
- ^ “HSP72 inhibits apoptosis-inducing factor release in ATP-depleted renal epithelial cells”. Am. J. Physiol., Cell Physiol. 285 (6): C1483–93. (December 2003). doi:10.1152/ajpcell.00049.2003. PMID 12930708.
- ^ “Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1”. Mol. Cell. Biol. 22 (22): 7721–30. (November 2002). doi:10.1128/mcb.22.22.7721-7730.2002. PMC 134722. PMID 12391142.
- ^ “CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70”. Oncogene 19 (38): 4385–95. (September 2000). doi:10.1038/sj.onc.1203797. PMID 10980614.
- ^ “Isolation of Bcl-2 binding proteins that exhibit homology with BAG-1 and suppressor of death domains protein”. Biochem. Biophys. Res. Commun. 286 (5): 1003–10. (September 2001). doi:10.1006/bbrc.2001.5512. PMID 11527400.
- ^ “The anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCC”. J. Biol. Chem. 277 (51): 49638–43. (December 2002). doi:10.1074/jbc.M209386200. PMID 12397061.
- ^ “Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport”. Exp. Cell Res. 289 (2): 211–21. (October 2003). doi:10.1016/s0014-4827(03)00261-1. PMID 14499622.
- ^ a b c “CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity”. Mol. Cell 10 (1): 55–67. (July 2002). doi:10.1016/s1097-2765(02)00583-x. PMID 12150907.
- ^ “Molecular chaperones as HSF1-specific transcriptional repressors”. Genes Dev. 12 (5): 654–66. (March 1998). doi:10.1101/gad.12.5.654. PMC 316571. PMID 9499401.
- ^ “Heat shock transcription factor-1 regulates heat shock protein-72 expression in human keratinocytes exposed to ultraviolet B light”. J. Invest. Dermatol. 111 (2): 194–8. (August 1998). doi:10.1046/j.1523-1747.1998.00266.x. PMID 9699716.
- ^ “HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors”. Biochem. Biophys. Res. Commun. 290 (2): 858–64. (January 2002). doi:10.1006/bbrc.2001.6271. PMID 11785981.
- ^ “Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions”. Mol. Cell. Biol. 19 (6): 4535–45. (June 1999). doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192.
[続きの解説]
「HSPA1A」の続きの解説一覧
- 1 HSPA1Aとは
- 2 HSPA1Aの概要
- 3 構造
- 4 相互作用
- 5 外部リンク
- HSPA1Aのページへのリンク
