TIMP4

TIMP metallopeptidase inhibitor 4
Identifiers
Symbols	TIMP4 ;
External IDs	Template:OMIM5 Template:MGI HomoloGene: 37748
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE TIMP4 206243 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

TIMP metallopeptidase inhibitor 4, also known as TIMP4, is a human gene.

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.

Further reading

• Greene J, Wang M, Liu YE; et al. (1997). "Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4". J. Biol. Chem. 271 (48): 30375–80. PMID 8939999.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 15496–500. PMID 9182583.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Olson TM, Hirohata S, Ye J; et al. (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): 148–51. doi:10.1006/geno.1998.5362. PMID 9693046.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 293–6. doi:10.1006/geno.1999.5776. PMID 10198170.CS1 maint: Multiple names: authors list (link)
• 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): 126–30. doi:10.1006/bbrc.2001.4323. PMID 11178970.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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): 659–66. PMID 12087081.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 48696–707. doi:10.1074/jbc.M209177200. PMID 12374789.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 1330–8. doi:10.1038/sj.bjp.0704936. PMID 12466243.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 15025–35. PMID 12475252.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 564–70. PMID 12969699.CS1 maint: Multiple names: authors list (link)
• 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): 590–8. PMID 14744773.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 641–50. doi:10.1093/molehr/gah092. PMID 15273280.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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): 335–42. doi:10.1007/s00418-006-0163-8. PMID 16521002.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)