组织蛋白酶H
| 组织蛋白酶H | |||||||||||||||||||||||||
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| 識別號 | |||||||||||||||||||||||||
| 别名 | CTSH；, ACC-4, ACC-5, CPSB, minichain, ACC4, ACC5, cathepsin H | ||||||||||||||||||||||||
| 外部ID | OMIM：116820 MGI：107285 HomoloGene：36159 GeneCards：CTSH | ||||||||||||||||||||||||
| 相關疾病 | |||||||||||||||||||||||||
| 双相障碍、1型糖尿病[1] | |||||||||||||||||||||||||
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| 物種 | 人類 | 小鼠 | |||||||||||||||||||||||
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| mRNA序列 |
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| 蛋白序列 |
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| 基因位置（UCSC） | Chr 15: 78.92 – 78.95 Mb | Chr 9: 89.94 – 89.96 Mb | |||||||||||||||||||||||
| PubMed查找 | [4] | [5] | |||||||||||||||||||||||
| 維基數據 | |||||||||||||||||||||||||
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组织蛋白酶H（英文：Cathepsin H）是一种在人体中由CTSH基因编码的蛋白质。[6][7]
该基因编码的蛋白质是木瓜样蛋白酶（英语：Papain-like protease），一种溶酶体半胱氨酸蛋白酶，在溶酶体蛋白质的整体降解中很重要。它由二硫键连接的重链和轻链的二聚体组成，均由单一蛋白质前体产生。编码的蛋白质属于肽酶C1蛋白质家族，既可以作为氨肽酶（英语：Aminopeptidase），也可以作为内肽酶。该基因的表达增加与前列腺肿瘤的恶性进展有关。该基因已发现了编码不同蛋白异构体的两种转录变体。[7]
参考文献
- ^ 與组织蛋白酶H相關的疾病；在維基數據上查看/編輯參考.
- ^ 2.0 2.1 2.2 GRCh38: Ensembl release 89: ENSG00000103811 - Ensembl, May 2017
- ^ 3.0 3.1 3.2 GRCm38: Ensembl release 89: ENSMUSG00000032359 - Ensembl, May 2017
- ^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Fuchs R, Machleidt W, Gassen HG. Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H. Biol Chem Hoppe-Seyler. Feb 1989, 369 (6): 469–75. PMID 2849458. doi:10.1515/bchm3.1988.369.1.469.
- ^ 7.0 7.1 Entrez Gene: CTSH cathepsin H.
拓展阅读
- Sawicki G, Warwas M. Cathepsin H from human placenta.. Acta Biochim. Pol. 1990, 36 (3–4): 343–51. PMID 2486008.
- Fuchs R, Gassen HG. Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase.. Nucleic Acids Res. 1990, 17 (22): 9471. PMC 335148
. PMID 2587265. doi:10.1093/nar/17.22.9471. - Chernaia VI, Reva AD. [Cathepsin H activity in the human brain and human brain neoplasms]. Ukr. Biokhim. Zh. 1990, 61 (5): 47–50. PMID 2588347.
- Ritonja A, Popović T, Kotnik M, et al. Amino acid sequences of the human kidney cathepsins H and L.. FEBS Lett. 1988, 228 (2): 341–5. PMID 3342889. doi:10.1016/0014-5793(88)80028-0 .
- Järvinen M, Rinne A. Human spleen cysteineproteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants.. Biochim. Biophys. Acta. 1983, 708 (2): 210–7. PMID 6184075. doi:10.1016/0167-4838(82)90222-9.
- Kato S, Sekine S, Oh SW, et al. Construction of a human full-length cDNA bank.. Gene. 1995, 150 (2): 243–50. PMID 7821789. doi:10.1016/0378-1119(94)90433-2.
- Baumgrass R, Williamson MK, Price PA. Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S.. J. Bone Miner. Res. 1997, 12 (3): 447–55. PMID 9076588. doi:10.1359/jbmr.1997.12.3.447 .
- Söderström M, Salminen H, Glumoff V, et al. Cathepsin expression during skeletal development.. Biochim. Biophys. Acta. 1999, 1446 (1–2): 35–46. PMID 10395917. doi:10.1016/S0167-4781(99)00068-8.
- Jokimaa V, Oksjoki S, Kujari H, et al. Expression patterns of cathepsins B, H, K, L and S in the human endometrium.. Mol. Hum. Reprod. 2001, 7 (1): 73–8. PMID 11134363. doi:10.1093/molehr/7.1.73 .
- Uusitalo H, Hiltunen A, Söderström M, et al. Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and endochondral ossification in mouse fracture callus.. Calcif. Tissue Int. 2001, 67 (5): 382–90. PMID 11136537. S2CID 31004810. doi:10.1007/s002230001152.
- Pol E, Björk I. Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases.. Protein Sci. 2001, 10 (9): 1729–38. PMC 2253190 . PMID 11514663. doi:10.1110/ps.11901.
- Waghray A, Keppler D, Sloane BF, et al. Analysis of a truncated form of cathepsin H in human prostate tumor cells.. J. Biol. Chem. 2002, 277 (13): 11533–8. PMID 11796715. doi:10.1074/jbc.M109557200 .
- Brasch F, Ten Brinke A, Johnen G, et al. Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes.. Am. J. Respir. Cell Mol. Biol. 2002, 26 (6): 659–70. PMID 12034564. doi:10.1165/ajrcmb.26.6.4744.
- Bühling F, Waldburg N, Krüger S, et al. Expression of cathepsins B, H, K, L, and S during human fetal lung development.. Dev. Dyn. 2003, 225 (1): 14–21. PMID 12203716. doi:10.1002/dvdy.10134 .
- Strausberg RL, Feingold EA, Grouse LH, et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.. Proc. Natl. Acad. Sci. U.S.A. 2003, 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899 .
- Jenko S, Dolenc I, Guncar G, et al. Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases.. J. Mol. Biol. 2003, 326 (3): 875–85. PMID 12581647. doi:10.1016/S0022-2836(02)01432-8.
- Nagai A, Terashima M, Harada T, et al. Cathepsin B and H activities and cystatin C concentrations in cerebrospinal fluid from patients with leptomeningeal metastasis.. Clin. Chim. Acta. 2003, 329 (1–2): 53–60. PMID 12589965. doi:10.1016/S0009-8981(03)00023-8.
- Han SR, Momeni A, Strach K, et al. Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.. Arterioscler. Thromb. Vasc. Biol. 2004, 23 (4): 661–7. PMID 12615673. doi:10.1161/01.ATV.0000063614.21233.BF .
- Dodt J, Reichwein J. Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase.. Biol. Chem. 2004, 384 (9): 1327–32. PMID 14515996. S2CID 23726105. doi:10.1515/BC.2003.149.
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