TIMP4

TIMP4
식별자
에일리어스	TIMP4, TIMP 메탈로펩티드가수분해효소억제제4, TIMP-4
외부 ID	OMIM: 601915 MGI: 109125 HomoloGene: 37748 GenCard: TIMP4
유전자 위치(인간)
크르.	3번 염색체(인간)
끝.	12,136,912 bp
유전자 위치(마우스)
크르.	6번 염색체(쥐)
끝.	115,229,128 bp
RNA발현패턴
	상단 표시 위치:
	복부 지방; ; 피하 지방 조직; ; 흉부 대동맥; ; 좌관상동맥; ; 상행 대동맥; ; 활액관절; ; 슬와 동맥; ; 좌심실; ; 갑상선 우엽; ; 활막;
	상단 표시 위치:
	심실중격; ; 백색 지방 조직; ; 소뇌충; ; 운동 뉴런; ; 흑색 실체; ; 갈색 지방 조직; ; 심실 심근; ; 발바닥근; ; 안마근; ; 정강이뼈전근;
	추가 참조 표현식 데이터
	추가 참조 표현식 데이터
유전자 존재론
분자 함수	펩티드가수분해효소억제활성; 효소억제활성; 금속 이온 결합; 단백질분해효소결합; 메탈로엔도펩티드가수분해효소억제제활성;
셀룰러 컴포넌트	서커머; 세포외 영역; 세포외 공간; 세포외 매트릭스;
생물학적 과정	노치 시그널링 패스; 펩티드가수분해효소활성음성조절; 펩타이드 호르몬에 대한 반응; 중추 신경계의 발달; 리포다당류에 대한 반응; 배란 주기; 막단백질 엑토도메인 단백질 분해 음성 조절; 촉매 활성의 음성 조절; 엔도펩티드가수분해효소활성음성조절; 호르몬에 대한 반응; 사이토카인에 대한 반응; 생물학적 과정; 유기물에 대한 반응;
	출처:아미고 / QuickGO
맞춤법
	7079
	110595
	ENSG00000157150
	ENSMUSG000030317
	Q99727
	Q9JHB3
	NM_003256
	NM_080639; NM_001356406
	NP_003247
	NP_542370; NP_001343335
	위키데이터
인간 보기/편집	마우스 표시/편집

금속단백질가수분해효소억제제4는 TIMP4 ^[5]^[6]^[7]유전자에 의해 인체 내에서 암호화되는 효소이다.

이 유전자는 금속단백질가수분해효소 유전자군의 조직억제제에 속한다.이 유전자 패밀리에 의해 코드된 단백질은 세포외 기질의 분해에 관여하는 펩티다아제 그룹인 매트릭스 메탈로프로테이나아제 억제제이다.이 유전자에 의해 코드된 분비된 네트린 도메인 함유 단백질은 혈소판 응집 및 모집 조절에 관여하며 호르몬 조절 및 자궁내막 조직 ^[7]리모델링에 역할을 할 수 있다.

상호 작용

TIMP4는 MMP2와 ^[8]^[9]대화하는 것으로 나타났습니다.

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TIMP1, TIMP2, TIMP3

레퍼런스

^ ^a ^b ^c GRCh38: 앙상블 릴리즈 89: ENSG00000157150 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리즈 89: ENSMUSG000030317 - 앙상블, 2017년 5월
^ "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.
^ Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE (Jan 1997). "Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4". J Biol Chem. 271 (48): 30375–30380. doi:10.1074/jbc.271.48.30375. PMID 8939999.
^ Olson TM, Hirohata S, Ye J, Leco K, Seldin MF, Apte SS (Sep 1998). "Cloning of the human tissue inhibitor of metalloproteinase-4 gene (TIMP4) and localization of the TIMP4 and Timp4 genes to human chromosome 3p25 and mouse chromosome 6, respectively". Genomics. 51 (1): 148–151. doi:10.1006/geno.1998.5362. PMID 9693046.
^ ^a ^b "Entrez Gene: TIMP4 TIMP metallopeptidase inhibitor 4".
^ Bigg, H F; Shi Y E; Liu Y E; Steffensen B; Overall C M (Jun 1997). "Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2". J. Biol. Chem. 272 (24): 15496–15500. doi:10.1074/jbc.272.24.15496. ISSN 0021-9258. PMID 9182583.
^ Kai, Heidi S-T; Butler Georgina S; Morrison Charlotte J; King Angela E; Pelman Gayle R; Overall Christopher M (Dec 2002). "Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain". J. Biol. Chem. 277 (50): 48696–48707. doi:10.1074/jbc.M209177200. ISSN 0021-9258. PMID 12374789.

추가 정보

Bigg HF, Shi YE, Liu YE, et al. (1997). "Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2". J. Biol. Chem. 272 (24): 15496–15500. doi:10.1074/jbc.272.24.15496. PMID 9182583.
Pohar N, Godenschwege TA, Buchner E (1999). "Invertebrate tissue inhibitor of metalloproteinase: structure and nested gene organization within the synapsin locus is conserved from Drosophila to human". Genomics. 57 (2): 293–296. doi:10.1006/geno.1999.5776. PMID 10198170.
Hernandez-Barrantes S, Shimura Y, Soloway PD, et al. (2001). "Differential roles of TIMP-4 and TIMP-2 in pro-MMP-2 activation by MT1-MMP". Biochem. Biophys. Res. Commun. 281 (1): 126–130. doi:10.1006/bbrc.2001.4323. PMID 11178970.
Huang W, Li WQ, Dehnade F, Zafarullah M (2002). "Tissue inhibitor of metalloproteinases-4 (TIMP-4) gene expression is increased in human osteoarthritic femoral head cartilage". J. Cell. Biochem. 85 (2): 295–303. doi:10.1002/jcb.10138. PMID 11948685. S2CID 43053515.
Zhang J, Cao YJ, Zhao YG, et al. (2003). "Expression of matrix metalloproteinase-26 and tissue inhibitor of metalloproteinase-4 in human normal cytotrophoblast cells and a choriocarcinoma cell line, JEG-3". Mol. Hum. Reprod. 8 (7): 659–666. doi:10.1093/molehr/8.7.659. PMID 12087081.
Kai HS, Butler GS, Morrison CJ, et al. (2003). "Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain". J. Biol. Chem. 277 (50): 48696–48707. doi:10.1074/jbc.M209177200. PMID 12374789.
Radomski A, Jurasz P, Sanders EJ, et al. (2003). "Identification, regulation and role of tissue inhibitor of metalloproteinases-4 (TIMP-4) in human platelets". Br. J. Pharmacol. 137 (8): 1330–1338. doi:10.1038/sj.bjp.0704936. PMC 1573597. PMID 12466243.
Troeberg L, Tanaka M, Wait R, et al. (2003). "E. coli expression of TIMP-4 and comparative kinetic studies with TIMP-1 and TIMP-2: insights into the interactions of TIMPs and matrix metalloproteinase 2 (gelatinase A)". Biochemistry. 41 (50): 15025–15035. doi:10.1021/bi026454l. PMID 12475252.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Chegini N, Rhoton-Vlasak A, Williams RS (2003). "Expression of matrix metalloproteinase-26 and tissue inhibitor of matrix metalloproteinase-3 and -4 in endometrium throughout the normal menstrual cycle and alteration in users of levonorgestrel implants who experience irregular uterine bleeding". Fertil. Steril. 80 (3): 564–570. doi:10.1016/S0015-0282(03)00797-0. PMID 12969699.
Zhao YG, Xiao AZ, Park HI, et al. (2004). "Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion". Cancer Res. 64 (2): 590–598. doi:10.1158/0008-5472.CAN-03-1932. PMID 14744773.
Pilka R, Domanski H, Hansson S, et al. (2005). "Endometrial TIMP-4 mRNA is high at midcycle and in hyperplasia, but down-regulated in malignant tumours. Coordinated expression with MMP-26". Mol. Hum. Reprod. 10 (9): 641–650. doi:10.1093/molehr/gah092. PMID 15273280.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Lee MH, Rapti M, Murphy G (2005). "Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme". J. Biol. Chem. 280 (16): 15967–75. doi:10.1074/jbc.M500897200. PMID 15713681.
Lizarraga F, Espinosa M, Maldonado V, Melendez-Zajgla J (2005). "Tissue inhibitor of metalloproteinases-4 is expressed in cervical cancer patients". Anticancer Res. 25 (1B): 623–7. PMID 15816637.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Koskivirta I, Rahkonen O, Mäyränpää M, et al. (2007). "Tissue inhibitor of metalloproteinases 4 (TIMP4) is involved in inflammatory processes of human cardiovascular pathology". Histochem. Cell Biol. 126 (3): 335–342. doi:10.1007/s00418-006-0163-8. PMID 16521002. S2CID 10581957.
Pilka R, Noskova V, Domanski H, et al. (2006). "Endometrial TIMP-4 mRNA is expressed in the stroma, while TIMP-4 protein accumulates in the epithelium and is released to the uterine fluid". Mol. Hum. Reprod. 12 (8): 497–503. doi:10.1093/molehr/gal055. PMID 16809379.

외부 링크

펩티드가수분해효소 및 그 억제제에 대한 MEROPS 온라인 데이터베이스: I35.004

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리즈 89: ENSG00000157150 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리즈 89: ENSMUSG000030317 - 앙상블, 2017년 5월

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8939999-5] Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE (Jan 1997). "Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4". J Biol Chem. 271 (48): 30375–30380. doi:10.1074/jbc.271.48.30375. PMID 8939999.

[pmid9693046-6] Olson TM, Hirohata S, Ye J, Leco K, Seldin MF, Apte SS (Sep 1998). "Cloning of the human tissue inhibitor of metalloproteinase-4 gene (TIMP4) and localization of the TIMP4 and Timp4 genes to human chromosome 3p25 and mouse chromosome 6, respectively". Genomics. 51 (1): 148–151. doi:10.1006/geno.1998.5362. PMID 9693046.

[entrez-7] "Entrez Gene: TIMP4 TIMP metallopeptidase inhibitor 4".

[pmid9182583-8] Bigg, H F; Shi Y E; Liu Y E; Steffensen B; Overall C M (Jun 1997). "Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2". J. Biol. Chem. 272 (24): 15496–15500. doi:10.1074/jbc.272.24.15496. ISSN 0021-9258. PMID 9182583.

[pmid12374789-9] Kai, Heidi S-T; Butler Georgina S; Morrison Charlotte J; King Angela E; Pelman Gayle R; Overall Christopher M (Dec 2002). "Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain". J. Biol. Chem. 277 (50): 48696–48707. doi:10.1074/jbc.M209177200. ISSN 0021-9258. PMID 12374789.

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TIMP4

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TIMP4

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