title: Genomic organization of the human tissue inhibitor of metalloproteinases-3 (TIMP3)
abstract: The tissue inhibitors of metalloproteinases (TIMPs) play a crucial role in the physiological turnover of the extracellular matrix (ECM) by tightly regulating matrix metalloproteinase (MMP) activities. Disturbances in the TIMP/MMP system have been implicated in many disease processes where loss of ECM integrity is a principal feature. More recently, we have shown that mutations in TIMP3 cause the autosomal dominant disorder Sorsby's fundus dystrophy (SFD). This is a macular degeneration disorder with characteristic ECM irregularities in Bruch's membrane. To further facilitate mutational analysis and to provide a basis for functional studies, we now report the genomic organization of the human TIMP3 gene.
authors.forename: H
authors.initials: H
authors.lastname: Stöhr
authors.forename: K
authors.initials: K
authors.lastname: Roomp
authors.forename: U
authors.initials: U
authors.lastname: Felbor
authors.forename: B H
authors.initials: BH
authors.lastname: Weber
mesh_terms: D000818:Animals; D001483:Base Sequence; D002874:Chromosome Mapping; D004247:DNA / Q000235:genetics; D017931:DNA Primers / Q000235:genetics; D005109:Extracellular Matrix / Q000378:metabolism; D006801:Humans; D008268:Macular Degeneration / Q000235:genetics; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D051379:Mice; D008969:Molecular Sequence Data; D011480:Protease Inhibitors; D011506:Proteins / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D019717:Tissue Inhibitor of Metalloproteinase-3
chemical_list: D017931:DNA Primers; D011480:Protease Inhibitors; D011506:Proteins; D019717:Tissue Inhibitor of Metalloproteinase-3; D004247:DNA; D008666:Metalloendopeptidases