TIMP4

TIMP4
Identifiers
AliasesTIMP4, TIMP metallopeptidase inhibitor 4
External IDsMGI: 109125 HomoloGene: 37748 GeneCards: TIMP4
Gene location (Human)
Chr.Chromosome 3 (human)[1]
BandNo data availableStart12,153,051 bp[1]
End12,159,351 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

7079

110595

Ensembl

ENSG00000157150

ENSMUSG00000030317

UniProt

Q99727

Q9JHB3

RefSeq (mRNA)

NM_003256

NM_080639

RefSeq (protein)

NP_003247

NP_542370

Location (UCSC)Chr 3: 12.15 – 12.16 MbChr 3: 115.24 – 115.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Metalloproteinase inhibitor 4 is an enzyme that in humans is encoded by the TIMP4 gene.[5][6][7]

This gene belongs to the tissue inhibitor of metalloproteinases gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. The secreted, netrin domain-containing protein encoded by this gene is involved in regulation of platelet aggregation and recruitment and may play role in hormonal regulation and endometrial tissue remodeling.[7]

Interactions

TIMP4 has been shown to interact with MMP2.[8][9]

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000157150 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030317 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. PMID 8939999. doi:10.1074/jbc.271.48.30375.
  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. PMID 9693046. doi:10.1006/geno.1998.5362.
  7. 1 2 "Entrez Gene: TIMP4 TIMP metallopeptidase inhibitor 4".
  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. UNITED STATES. 272 (24): 15496–15500. ISSN 0021-9258. PMID 9182583. doi:10.1074/jbc.272.24.15496.
  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. United States. 277 (50): 48696–48707. ISSN 0021-9258. PMID 12374789. doi:10.1074/jbc.M209177200.

Further reading

  • 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. PMID 9182583. doi:10.1074/jbc.272.24.15496. 
  • 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. PMID 10198170. doi:10.1006/geno.1999.5776. 
  • 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. PMID 11178970. doi:10.1006/bbrc.2001.4323. 
  • 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. PMID 11948685. doi:10.1002/jcb.10138. 
  • 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. PMID 12087081. doi:10.1093/molehr/8.7.659. 
  • 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. PMID 12374789. doi:10.1074/jbc.M209177200. 
  • 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. PMC 1573597 Freely accessible. PMID 12466243. doi:10.1038/sj.bjp.0704936. 
  • 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. PMID 12475252. doi:10.1021/bi026454l. 
  • 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. PMC 139241 Freely accessible. PMID 12477932. doi:10.1073/pnas.242603899. 
  • 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. PMID 12969699. doi:10.1016/S0015-0282(03)00797-0. 
  • 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. PMID 14744773. doi:10.1158/0008-5472.CAN-03-1932. 
  • 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. PMID 15273280. doi:10.1093/molehr/gah092. 
  • 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. PMC 528928 Freely accessible. PMID 15489334. doi:10.1101/gr.2596504. 
  • 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. PMID 15713681. doi:10.1074/jbc.M500897200. 
  • 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. PMID 16189514. doi:10.1038/nature04209. 
  • 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. PMID 16521002. doi:10.1007/s00418-006-0163-8. 
  • 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. PMID 16809379. doi:10.1093/molehr/gal055. 
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