Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization.

Matrix metalloproteinases (MMPs) are zinc-binding endopeptidases that degrade extracellular matrix macro-molecules such as collagens, glycoproteins, and proteoglycans and play an important role in tissue remodeling under many physiological and pathological conditions. At present the MMP family consists of 14 structurally related enzymes. Ten of these enzymes are secreted proteins, while the other 4, described recently, contain a transmembrane domain and a cytoplasmic tail at the carboxyl terminus. These are membrane-type matrix metalloproteinases, MT1-MMP, MT2-MMP, MT3-MMP, and MT4-MMP, MT1-, MT2-, and MT3-MMPs are closely related to each other (50% protein sequence homology), while MT4-MMP is more distant (less than 30% homology to MT1-MMP). Sequence conservation in MMP genes suggests that these proteins evolved from a single ancestor gene by gene duplication. Six of the 10 genes of the MMP family are clustered on human chromosome 11q21-q23, while the other 4 are scattered throughout the human genome. Thus chromosomal localization of new membrane-type enzymes is of particular interest. 13 refs., 1 fig.

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