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evolution
MMP-2 is a member of the matrix metalloproteinase family
malfunction
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the inactivation of the MMP-2 gene prevents thrombosis induced by weak, but not strong, stimuli but produces only a moderate prolongation of the bleeding time. MMP-2 deficient mice have hyporeactive platelets, a defective thrombotic response and mildly impaired hemostasis
malfunction
in de novo formed fat pads, resulting from preadipocytes with Mmp2 knockdown, the expression of aP2, Ppar-gamma and adiponectin is significantly lower, and collagen is more preserved. The fat pad weights as well as size and density of adipocytes or blood vessels are not significantly different from controls, phenotype, overview
malfunction
induction of diabetes in transgenic mice overexpressing human MMP2 show ignificant improvements in glycemia, glucose tolerance and insulin secretion compared to diabetic wild-type mice. Increased hMMP2 levels in mice correlate with significant reduction in islet beta-cell apoptosis compared to wild-type counterparts, and an inhibitor of hMMP2 reverses this mitigating activity against diabetes
malfunction
knockdown of LvMMP-2 expression decreases shrimp cumulative mortality upon oxidative stress. Knocked-down expression of LvMMP-2 depresse sthe expression of penaeidin2 and beta-defensin. Downregulation of LvMMP-2 suppresses the cumulative mortality of shrimp infected with white spot syndrome virus (WSSV) or with Vibrio alginolyticus
malfunction
women with endometriosis show decreased MMP-2 activity in eutopic endometrium as compared to women without endometriosis, while ectopic ovarian endometrioma show significantly elevated MMP-2 activity with disease severity. Increased MMP-2 activation with disease progression
malfunction
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in de novo formed fat pads, resulting from preadipocytes with Mmp2 knockdown, the expression of aP2, Ppar-gamma and adiponectin is significantly lower, and collagen is more preserved. The fat pad weights as well as size and density of adipocytes or blood vessels are not significantly different from controls, phenotype, overview
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metabolism
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evaluation of the effect that the hormonal fluctuations of the reproductive cycle have on the stromal remodeling and the expression and activity of matrix metalloproteinases MMP-2 and -9 in the adult female gerbil prostate, overview
metabolism
expansion of adipose tissue is dependent on adipogenesis, angiogenesis and extracellular matrix remodeling by the gelatinase subfamily of the matrix metalloproteinases, overview
metabolism
aortic stiffness is an independent risk factor for development of cardiovascular diseases. Activation of renin-angiotensin-aldosterone system (RAAS) including angiotensin converting enzyme (ACE) activity leads to overproduction of angiotensin II (ANGII) from its precursor angiotensin I (ANGI). ANGII leads to overexpression and activation of matrix metalloproteinase-2 (MMP2), which is critically associated with pathophysiology of aortic stiffness
metabolism
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expansion of adipose tissue is dependent on adipogenesis, angiogenesis and extracellular matrix remodeling by the gelatinase subfamily of the matrix metalloproteinases, overview
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physiological function
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platelet-derived MMP-2 facilitates thrombus formation
physiological function
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in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor
physiological function
enzyme MMP-2 is considered a major enzyme involved in the turnover of the extracellular matrix. The enzyme is involved in the degradation of fibrillin-1 and fibrillin-2, the degradation patterns differ between the eye and the periodontal ligaments, possibly reflecting the sensitivity of fibrillin-1 and fibrillin-2 of each type of oxytalan fiber against enzyme MMP-2
physiological function
the enzyme act as important oncogenes that improve invasiveness of cancer cells
physiological function
the enzyme gelatinase A is involved in adipogenesis, selective modulation of MMP-2 levels affects adipogenesis
physiological function
chronic progression of diabetes is associated with decreased pancreatic islet mass due to apoptosis of beta-cells. Patients with diabetes have increased circulating matrix metalloproteinase-2 (MMP2). MMP2 might inhibit cell apoptosis, including islet beta-cells. The increased activation of Akt and BAD induced by hMMP2 in beta-cells compared to controls, links this signaling pathway to the anti-apoptotic activity of hMMP2, a property that is reversible by both an hMMP2 inhibitor and antibody against integrin-beta3. hMMP2 may attenuate the severity of diabetes by protecting islet beta-cells from apoptosis through an integrin-mediated activation of the Akt/BAD pathway. Preliminary treatment of cells, e.g. HepG2 cells, HUVE cells, and NHM cells, with active hMMP2 for 30-min significantly inhibits apoptosis (induced by starvation), hMMP2 inhibits apoptosis of beta-cell lines, which is modulated by intergrins
physiological function
LvMMP-2 plays a role in innate immunity response. Promoter activity of LvMMP-2 is enhanced by LvNRF2 in a ARE site dependent-manner. Overexpression of Lvc-Jun in S2 cells demonstrates that AP-1 factor c-Jun is also involved in LvMMP-2 regulation
physiological function
matrix metalloproteinase MMP-2 degrades components of the extracellular matrix, denatured interstitial type I collagen and native type IV collagen. MMP-2 is a key player in cancer invasion and metastasis. Different mechanisms contribute to regulate the activity of MMP-2 during its molecular existence: expression, secretion, activation, extra/pericellular localization, inhibition, endocytosis and lysosomal degradation. Epigenetic control also contributes to MMP-2 regulation. Levels of control of extra/pericellular MMP-2, overview The enzyme is present in the extracellular compartment for degrading denatured type I collagen. Cell membrane-bound MMP-2 can also act as transducers and trigger outside-in signaling. Binding of proMMP-2 to alphavbeta3 integrin on the surface of lung cancer cells stimulates tumor angiogenesis by activating PI3K/AKT pathway and HIF-1alpha, leading to VEGF-A expression
physiological function
matrix metalloproteinase-2 (gelatinase A) is a mediator of cancer metastasis, but it is also thought to be involved in several aspects of cancer development, including cell growth and inflammation. MMP-2 may be associated with colorectal cancer development and invasion in the Tunisian population
physiological function
MMP-2 isoforms do not seem to be directly involved with Mycobacterium tuberculosis evolution of infection
physiological function
potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
physiological function
regulation of matrix metalloproteinase-2 activity by COX-2-PGE2-pAKT axis promotes angiogenesis in endometriosis. Analysis of the regulation of MMP-2 activity in endothelial cells and on angiogenesis during progression of ovarian endometriosis, overview. Involvement of MT1MMP and TIMP-2 in MMP-2 activation during progression of endometriosis
physiological function
the enzyme exhibits gelatinolytic activity which is enhanced by p-aminophenylmercuric acetate (APMA). The APMA treated enzyme probably also produces proteolytic products of myosin and other muscle proteins
physiological function
Gallus gallus Hy-Line Brown
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potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
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physiological function
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the enzyme gelatinase A is involved in adipogenesis, selective modulation of MMP-2 levels affects adipogenesis
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physiological function
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in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor
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additional information
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the SDF-1a/CXCR4 axis is involved in osteopontininduced MMP-2 expression and activity, overview
additional information
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thrombin-dependent MMP-2 activity is regulated by heparan sulfate, molecular mechanism, regulatory role of hemopexin-like domain in MMP-2 degradation, overview
additional information
crucial role of the fibronectin-like domain in enzymatic activities, it is involved in substrate binding
additional information
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crucial role of the fibronectin-like domain in enzymatic activities, it is involved in substrate binding
additional information
enzyme MMP-2 forms heterodimers with various proteins, including TIMP-2, TIMP-3, TIMP-4, and glycosaminoglycans. Disruption of the cysteine-zinc ion pairing by homodimerization of MMP-2 opens the active site, but it may accommodate only small peptide substrates. Thus, MMP-2 propeptide processing is a prerequisite to gain its proteolytic activity against large substrates, including gelatin
additional information
MMP-2 has two isoforms: the 72 kDa latent form and an active form of 62 kDa, which is generated from the 10 kDa pro-domain cut-off. MMP-2 isoforms identification and determination of activities, overview
additional information
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MMP-2 has two isoforms: the 72 kDa latent form and an active form of 62 kDa, which is generated from the 10 kDa pro-domain cut-off. MMP-2 isoforms identification and determination of activities, overview
additional information
the Zn2+-binding motif of the catalytic domain is preceded by three cysteine-rich repeats comparable to the collagen-binding fibronectin type II (FN-II) repeats, which are required for recognizing collagen and elastin