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Link to original content: https://omim.org/entry/185250
Alternative titles; symbols
HGNC Approved Gene Symbol: MMP3
Cytogenetic location: 11q22.2 Genomic coordinates (GRCh38) : 11:102,835,801-102,843,609 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 11q22.2 | {Coronary heart disease, susceptibility to, 6} | 614466 | 3 |
Human fibroblast stromelysin (also called transin or matrix metalloproteinase-3) is a proteoglycanase closely related to collagenase (MMP1; 120353) with a wide range of substrate specificities. It is a secreted metalloprotease produced predominantly by connective tissue cells. Together with other metalloproteases, it can synergistically degrade the major components of the extracellular matrix (Sellers and Murphy, 1981). Stromelysin is capable of degrading proteoglycan, fibronectin, laminin, and type IV collagen, but not interstitial type I collagen.
Whitham et al. (1986) found that the amino acid sequences predicted from the cDNAs of collagenase and stromelysin indicate that they are closely related enzymes, with a particularly well-conserved region of 14 amino acids that shares significant homology with the zinc-chelating region of the bacterial metalloprotease thermolysin (Matthews et al., 1974).
Wilhelm et al. (1987) purified and determined the complete primary structure of human stromelysin. It is synthesized in a preproenzyme form with a calculated size of 53,977 Da and a 17-amino acid signal peptide. A comparison of primary structures suggested that stromelysin is the human analog of rat transin. Saus et al. (1988) determined the complete primary structure of human matrix metalloproteinase-3, which has 477 amino acid residues, including the 17-residue signal peptide. The findings indicated that MMP3 is identical to stromelysin. MMP3 and collagenase were found to be 54% identical in sequence, suggesting a common evolutionary origin of the 2 proteinases. Koklitis et al. (1991) purified 2 forms of recombinant human prostromelysin.
By immunohistochemical analysis of human bone tissues, Bord et al. (1998) found distinct patterns of expression for SL1 and SL2 (MMP10; 185260). In situ zymography revealed that SL1 was secreted in the latent form, whereas SL2 was active. Latent SL1 was detected in extracellular matrix in fibrous tissue surrounding endochondral ossification in osteophytes, and adjacent to periosteum in fetal rib bone. Active SL1 was detected in osteocytes and the matrix surrounding osteocytic lacunae. In contrast, SL2 associated with cells at sites of resorption in areas of endochondral ossification and in resorptive cells at the chondroosseous junction. In fetal rib, active SL2, but not SL1, localized in chondrocytes of the growth plate. Vascular areas showed strong SL2 staining with some proteolytic activity. SL2, but not SL1, was strongly expressed in osteoclasts and most mononuclear cells within the marrow. At sites of bone formation, both SL1 and SL2 were expressed by osteoblasts, with SL1 also in osteoid. Bord et al. (1998) concluded that SL2 is secreted in an active form with associated degradation, whereas SL1 is produced in a matrix-bound proenzyme form that may act as a reservoir for later activation.
By somatic cell hybridization and in situ hybridization, Spurr et al. (1988) mapped the stromelysin locus to 11q and confirmed the location of the collagenase gene on chromosome 11, specifically on 11q. Gatti et al. (1989) placed the STMY locus in the 11q22-q23 region by linkage analysis with markers in that area, including ataxia-telangiectasia (208900). By pulsed field gel electrophoresis, Formstone et al. (1993) showed that a cluster of metalloproteinase genes--stromelysin I, fibroblast collagenase (MMP1), and stromelysin II (MMP10; 185260)--are located in a 135-kb region of chromosome 11. The physical proximity of these 3 genes, together with the DNA marker D11S385, was confirmed using 2 YAC clones, and their relative order determined. This information, combined with the pattern of marker representation in a panel of radiation-reduced chromosome 11 hybrids, suggested that the order was cen--STMY2--CLG--STMY1--D11S385--ter. Pendas et al. (1996) noted that the family of human MMPs was composed of 14 members at the time of their report. MMP genes have been mapped to chromosomes 11, 14 (MMP14; 600754), 16 (MMP2; 120360), 20 (MMP9; 120361), and 22 (MMP11; 185261), with several clustered within the long arm of chromosome 11. Pendas et al. (1996) isolated a 1.5-Mb YAC clone mapping to 11q22. Detailed analysis of this nonchimeric YAC clone ordered 7 MMP genes as follows: cen--MMP8 (120355)--MMP10--MMP1--MMP3--MMP12 (601046)--MMP7 (178990)--MMP13 (600108)--tel.
Saus et al. (1988) found that MMP3 and collagenase expression appeared to be coordinately modulated in synovial fibroblast cultures. Levels of mRNA for both proteins are induced by interleukin-1-beta (147720) and suppressed by retinoic acid or dexamethasone. Stromelysin expression is regulated primarily at the level of transcription, with the promoter of the MMP3 gene responding to stimuli including growth factors and cytokines (Quinones et al., 1989; Quinones et al., 1994).
Kerr et al. (1988) examined the role of c-fos protein (164810) in growth factor stimulation of transin, a matrix-degrading secreted metalloproteinase. The stimulatory effect of both platelet-derived growth factor (190040) and epidermal growth factor (131530) on transin transcription involved factors recognizing the sequence TGAGTCA, which is found in the transin promoter and is a binding site for the transcriptional factor JUN/AP1 (165160) and for associated FOS and FOS-related complexes.
Wound repair involves cell migration and tissue remodeling, and these ordered and regulated processes are facilitated by matrix-degrading proteases. Saarialho-Kere et al. (1992) found that interstitial collagenase is invariantly expressed by basal keratinocytes at the migrating front of healing epidermis. Because the substrate specificity of collagenase is limited principally to interstitial fibrillar collagens, other enzymes must also be produced in the wound environment to restructure tissues effectively with a complex matrix composition. The stromelysins can degrade many noncollagenous connective tissue macromolecules. Using in situ hybridization and immunohistochemistry, Saarialho-Kere et al. (1994) found that both stromelysin I and stromelysin II are produced by distinct populations of keratinocytes in a variety of chronic ulcers. Stromelysin I mRNA and protein were detected in basal keratinocytes adjacent to but distal from the wound edge in what probably represented the sites of proliferating epidermis. In contrast, stromelysin II mRNA was seen only in basal keratinocytes at the migrating front, in the same epidermal cell population that expressed collagenase. Stromelysin I producing keratinocytes resided on the basement membrane, whereas stromelysin II-producing keratinocytes were in contact with the dermal matrix. Furthermore, stromelysin I expression was prominent in dermal fibroblasts, whereas no signal for stromelysin II was seen in any dermal cell. These findings demonstrated that the 2 stromelysins are produced by different populations of basal keratinocytes in response to wounding and suggested that they serve distinct roles in tissue repair.
Using immunofluorescence staining, RT-PCR, and in situ hybridization, Lu et al. (1999) localized stromelysin I to the epithelial layers of unwounded and wounded corneas. They found stromelysin I in the deep stromal layer in the first 3 days after wounding and in the area of newly synthesized stromal matrix 1 week after surgery. Imai et al. (1995) found that stromelysin I activates matrilysin (MMP7; 178990), and Lu et al. (1999) showed that stromelysin I and matrilysin interact during tissue remodeling. Lu et al. (1999) concluded that stromelysin I may be involved in the reparative process in the wound bed after excimer keratectomy, whereas matrilysin may play a role in epithelial wound remodeling not only in the migration phase but also in the subsequent proliferation phase.
Sternlicht et al. (1999) examined how MMP3, or STR1, affects tumor progression using 2 genetic approaches: phenotypically normal mammary epithelial cells that express STR1 in a tetracycline-regulated manner, and an STR1 transgene targeted to mouse mammary glands by the mouse 'whey acidic protein' (WAP) gene promoter. Phenotypically normal mammary epithelial cells with tetracycline-regulated expression of STR1 formed epithelial glandular structures in vivo without STR1 but formed invasive mesenchymal-like tumors with STR1. Once initiated, the tumors became independent of continued STR1 expression. STR1 also promoted spontaneous premalignant changes and malignant conversion in mammary glands of transgenic mice. These changes were blocked by coexpression of a TIMP1 (305370) transgene. The premalignant and malignant lesions had stereotyped genomic changes unlike those seen in other murine mammary cancer models. These data indicated that STR1 influences tumor initiation and alters neoplastic risk.
Humphries et al. (2002) noted that vascular remodeling is an essential feature in the development of atherosclerotic changes in the arterial wall, and that genes involved in these processes, including MMP3, are candidates for determining coronary heart disease (CHD) risk. The MMP gene family and their endogenous tissue inhibitors regulate the accumulation of extracellular matrix, and thus the growth of the atherosclerotic plaque.
Matsuyama et al. (2003) measured circulating levels of MMP2, MMP3, and MMP9 in 25 patients with Takayasu arteritis (207600) and 20 age- and sex-matched healthy controls. Levels of all 3 metalloproteinases were higher in patients with active disease than in controls (p less than 0.0001 for each), and MMP2 levels remained elevated even in remission. In contrast, an improvement in clinical signs and symptoms was associated with a marked reduction in circulating MMP3 and MMP9 levels in all patients (p less than 0.05). Matsuyama et al. (2003) concluded that MMP2 could be helpful in diagnosing Takayasu arteritis and that MMP3 and MMP9 could be used as activity markers for the disease.
D'Souza et al. (2002) found that expression of Mmp3, but not of other Mmps, was elevated about 10-fold in spontaneously demyelinating transgenic mice overexpressing Dm20 (300401). Increased Mmp3 expression occurred between 5 days and 1 month of age, more than 2 months before the onset of disease, and was coordinated with expression of the Dm20 transgene. Protein levels of Timp1 were also upregulated in Dm20 transgenic mice. Overexpression of Timp1 in double transgenic mice ameliorated development of disease.
Radisky et al. (2005) found that exposure of mouse mammary epithelial cells to MMP3 induces the expression of an alternatively spliced form of RAC1 (602048), which causes an increase in cellular reactive oxygen species. The reactive oxygen species stimulated the expression of the transcription factor Snail (see 604238) and epithelial-mesenchymal transition, and caused oxidative damage to DNA and genomic instability. Radisky et al. (2005) concluded that these findings identified a pathway in which a component of the breast tumor microenvironment alters cellular structure in culture and tissue structure in vivo, leading to malignant transformation.
There is a common polymorphism in the promoter sequence of the STMY1 gene, with 1 allele containing a run of 6 adenosines (6A) and the other 5 adenosines (5A) (185250.0001). Ye et al. (1996) followed up on a previously reported 3-year study by Richardson et al. (1989) of patients with coronary atherosclerosis (CHDS6; 614466) which indicated that those patients who were homozygous for the 6A allele showed a more rapid progression of both global and focal atherosclerotic stenoses. This observation supported the findings by others that the metalloproteinases are involved in connective tissue remodeling during atherogenesis. Ye et al. (1996) investigated whether the 5A/6A promoter polymorphism plays a role in the regulation of STMY1 gene expression. In transient expression experiments, a STMY1 promoter construct with 6A at the polymorphic site was found to express less of the reporter gene than a construct containing 5A. Binding of a nuclear protein factor was more readily detectable with an oligonucleotide probe corresponding to the 6A allele as compared with a probe corresponding to the 5A allele. Thus, Ye et al. (1996) found that the 5A/6A polymorphism appears to play an important role in regulating STMY1 expression. In a study by Quinones et al. (1989), the frequency of the 2 alleles (5A/6A) was found to be 0.51/0.49 in a sample of 354 healthy individuals from the UK.
Humphries et al. (2002) reported on the relationship between smoking, MMP3 genotype, and risk of clinical CHD in a prospective survey of healthy middle-aged men. They found that current smoking nearly doubled the risk for CHD, and examined the hypothesis that this risk was modified by MMP3 genotype. They found that in nonsmoking men, compared with the 5A/5A group, the relative risk was 1.37 in those with the 5A/6A genotype and 3.02 in those with the 6A/6A genotype. Smoking increased risk 1.4-fold in the 5A/6A group to 1.91, 1.3-fold in the 6A/6A group to 4.01, and 3.81-fold in the 5A/5A group. The data indicated a key role for stromelysin in the atherosclerotic process. Men with the 5A/5A genotype represented 29% of the general population, and their high risk, if smokers, provided a strong argument for avoiding smoking.
Medley et al. (2003) determined the MMP3 5A/6A genotype in 203 low cardiovascular risk, unmedicated individuals who were divided prospectively into 2 groups, 30 to 60 years old and greater than 60 years old. In the older group, homozygotes were found to have significantly (p less than 0.01) higher aortic input and characteristic impedance (i.e., greater stiffness) than heterozygotes, after correction for the effects of age, gender, and mean arterial pressure. There was no such difference in the younger group. Gene expression was determined by real-time PCR in dermal biopsies of 40 randomly selected men from the older group and was found to be 4-fold higher in 5A homozygotes (p less than 0.05) and 2-fold lower in 6A homozygotes (p less than 0.05) compared with the heterozygotes, and differences in gene expression were associated with corresponding significant changes in MMP3 protein levels. Medley et al. (2003) concluded that the MMP3 genotype may be an important determinant of vascular remodeling and age-related arterial stiffening, with the heterozygote having the optimal balance between matrix accumulation and deposition.
Mice infected with Citrobacter rodentium develop colonic mucosal hyperplasia and a local Th1 inflammatory response similar to that seen in other mouse models of inflammatory bowel disease (IBD; see 266600), and this response is enhanced in mice lacking Tnfrsf1a (191190), Il12p40 (IL12B; 161561), or Ifng (147570). Using competitive RT-PCR analysis, Li et al. (2004) showed that these cytokine knockout mice had increased levels of Mmp3 following C. rodentium infection, suggesting that the enhanced pathology is due to increased mucosal remodeling. However, mice lacking Mmp3 had mucosal thickening similar to that seen in wildtype mice following infection. Colonic tissues from Mmp3 -/- mice showed a compensatory increase in expression of other MMPs, such as Mmp7 and Mmp12, but clearance of bacteria and appearance of Cd4 (186940)-positive T cells into intestinal lamina propria were delayed. Li et al. (2004) concluded that mucosal remodeling can occur in the absence of MMP3 and that MMP3 plays a role in the migration of CD4-positive T cells into the intestinal mucosa.
Ye et al. (1996) identified a polymorphism in the promoter region of the MMP3 gene approximately 1,600 bp upstream from the start of transcription, at position -1171, in which 1 allele has a run of 6 adenosines (6A) while the other has 5 (5A). In vitro studies of promoter strength showed that the 5A allele expressed higher activity than the 6A allele in both cultured fibroblasts and vascular smooth muscle cells. They suggested that because of reduced gene transcription, homozygosity for the 6A allele would be associated with lower stromelysin levels in arterial walls than other genotypes. This lower level of proteolytic activity would favor extracellular matrix deposition in atherosclerotic lesions. In agreement with this hypothesis, 3 independent studies (Ye et al., 1995; Humphries et al., 1998; de Maat et al., 1999) found the most rapid progression of angiographically documented coronary atherosclerosis (CHDS6; 614466) in patients with the 6A/6A genotype. By contrast, homozygosity for the 5A allele would be predicted to be associated with higher intraarterial levels of stromelysin, which would be predicted to predispose to plaque instability and rupture in the presence of a high atherosclerotic burden. This hypothesis was supported by a study of Japanese patients with unstable angina in which the 5A/5A genotype was associated with acute myocardial infarction (Terashima et al., 1999).
In Japanese women, Yamada et al. (2002) found a significant association between the -1171 5A/6A promoter region polymorphism and myocardial infarction.
Humphries et al. (2002) reported on the interaction between smoking, the MMP3 5A/6A promoter polymorphism, and the risk of coronary heart disease in healthy men. They found that current smoking was associated with a relative risk for coronary heart disease that was approximately doubled as compared with nonsmokers; in individuals with the 5A/5A genotype, smoking increased risk 3.81-fold.
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