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malfunction
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in mice lacking MMP-9 the enhanced COX-1-PGE2 decreases caspase-3 expression and activity leading to impaired apoptosis of inflammatory neutrophils resulting in abnormal accumulation of the cells at the inflammatory focus
malfunction
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increased levels of MMP-9 protein cause myopathy in dystrophin-deficient mdx mice. Deletion of Mmp9 gene in mdx mice improves skeletal muscle structure and functions and reduces muscle injury, inflammation and fiber necrosis. Heterozygous or homozygous deletion of MMP-9 attenuates accumulation of macrophages, fiber necrosis and improves force production in skeletal muscle of mdx mice. Genetic deletion of MMP-9 attenuates fibrosis in diaphragm of mdx mice. Genetic ablation of MMP-9 inhibits the activation of activator protein-1 and nuclear factor-kappaB transcription factors, reduces the serum level of creatine kinase and improves skeletal muscle structure in mdx mice. Genetic ablation of MMP-9 augments myofiber regeneration, improves sarcolemmal structure and augments the cellular levels of beta-dystroglycan and nNOS in skeletal muscle of mdx mice
malfunction
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matrix metalloprotease-9 inhibition improves amyloid beta-mediated cognitive impairment and neurotoxicity in mice
malfunction
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matrix metalloproteinase-9 deficiency leads to prolonged foreign body response in the brain associated with increased IL-1beta levels and leakage of the blood-brain barrier, increased levels of interleukin-1beta and the delayed repair of blood-brain barrier are associated with prolongation of the foreign body response in MMP-9-null mice
malfunction
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mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis
malfunction
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mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis, MMP-9-null wounds display compromised reepithelialization, reduced clearance of fibrin clots and normal tensile strength
malfunction
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MMP-9 deficiency impairs ischemia-induced neovascularization, deficiency of MMP-9 reduces endothelial progenitor cell-like cell mobilization, lack of MMP-9 attenuates C-kit-positive bone marrow cell adhesion and migration
malfunction
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MMP-9 knockdown blocks SGC-7901 cells' invasion, migration and proliferation
malfunction
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MMP-9 knockout mice are resistant to dextran sodium sulfate-, Salmonella typhimurium-, or trinitrobenzene sulfonic acid-induced colitis
malfunction
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while a lack of MMP-9 does not alter vein graft wall area or cellularity, grafts from MMP-9 knockout mice accumulate more collagen and have earlier linear expansive remodelling, possibly due to an early compensatory increase in MMP-2
malfunction
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infection of chorioamniotic membranes with Escherichia coli induces an increase in the secretion of inactive forms and an association to extracellular matrix of active forms of MMP-2 and MMP-9 without changes in inhibitor TIMP-1, -2, and -4.These changes explain the significant decrease of collagen content and loss of structural continuity
malfunction
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inhibition of matrix metalloproteinase-9 activity by doxycycline ameliorates RANK ligand-induced osteoclast differentiation in vitro and in vivo, overview. Doxycycline treatment abrogates RANKL-induced osteoclastogenesis and TRAP activity in mouse calvaria along with the suppression of MMP9 enzyme activity, again without affecting the expression of MMP9 protein
malfunction
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inhibition of MMP activity, especially MMP-9, has the potential to inhibit tumor growth and metastasis
malfunction
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the broad-spectrum inhibitor of MMPs, BB-94, markedly reduces activation of trypsinogen, levels of CXCL2, infiltration of neutrophils, and tissue damage in acute pancreatitis
malfunction
a truncated 65 kDa enzyme lacks the haemopexin domain required for the high-affinity binding of the tissue inhibitor TIMP-1, and can be evaluated by activity assay in the presence of tissue inhibitor of metalloproteinases 1, TIMP-1
malfunction
administration of MMP-9 specific siRNA to the lungs of sensitized animals would abrogate development of an asthma phenotype, with endpoints of reduced airway hypersensitivity, less inflammation and tissue remodeling, less cellular migration of lymphocytes and eosinophils, and less activation of inflammatory cells, in both BAL fluids and lung tissues
malfunction
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enzyme inhibition prevents neural crest cells delamination and migration
malfunction
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
malfunction
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
malfunction
the enzyme is important for tooth development. Teeth of Mmp9-/- mice displayed a phenotype similar to dentinogenesis imperfecta, including decreased dentin mineral density, abnormal dentin architecture, widened predentin and irregular predentin-dentin boundary
malfunction
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in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
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malfunction
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enzyme inhibition prevents neural crest cells delamination and migration
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malfunction
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inhibition of matrix metalloproteinase-9 activity by doxycycline ameliorates RANK ligand-induced osteoclast differentiation in vitro and in vivo, overview. Doxycycline treatment abrogates RANKL-induced osteoclastogenesis and TRAP activity in mouse calvaria along with the suppression of MMP9 enzyme activity, again without affecting the expression of MMP9 protein
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malfunction
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the broad-spectrum inhibitor of MMPs, BB-94, markedly reduces activation of trypsinogen, levels of CXCL2, infiltration of neutrophils, and tissue damage in acute pancreatitis
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malfunction
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administration of MMP-9 specific siRNA to the lungs of sensitized animals would abrogate development of an asthma phenotype, with endpoints of reduced airway hypersensitivity, less inflammation and tissue remodeling, less cellular migration of lymphocytes and eosinophils, and less activation of inflammatory cells, in both BAL fluids and lung tissues
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metabolism
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activities of MMP-9 synthesized by fibroblasts tend to be regulated by the specific extracellular protein the cells are in contact with, whereas the gelatinolytic actions of proteases produced by myoblasts are more responsive to the mechanical deformation
metabolism
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auto-amplified NFATc1 plays a key role in upregulating expressions of genes required for osteoclastmaturation, such as TRAP, cathepsin K, or MMP-9,which are requisite for the bone resorption processes mediated by mature osteoclasts
metabolism
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auto-amplified NFATc1 plays a key role in upregulating expressions of genes required for osteoclastmaturation, such as TRAP, cathepsin K, or MMP-9,which are requisite for the bone resorption processes mediated by mature osteoclasts
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physiological function
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activated MMP-9 degrades components of the neurovascular unit, mediates blood-brain barrier leakage, and facilitates brain edema and hemorrhage
physiological function
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changes in MMP-9 activity may be essential to the tissue reorganization necessary for ovulation in the equine ovary
physiological function
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epithelial-derived MMP-9 is an important mediator of tissue injury in colitis
physiological function
expression of MMP-9 mRNA is associated with abnormal apparent diffusion coefficient after global cerebral ischemia
physiological function
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lipocalin-2 is associated with MMP-9 activity
physiological function
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matrix metalloproteinase 9 plays a key role in lyme arthritis but not in dissemination of Borrelia burgdorferi. MMP-9 cleavage of type I collagen results in increased monocyte chemoattraction, MMP-9 plays an important role in regulating inflammation in Lyme arthritis, potentially through the cleavage of collagen type I
physiological function
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matrix metalloproteinase-9 controls N-methyl-D-aspartate receptor surface diffusion through integrin beta1 signaling, enzymatic activity of MMP-9 increases lateral diffusion of NR1- N-methyl-D-aspartate receptors without cleavage of NR subunits, MMP-9 does not affect GluR2-alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid receptor surface diffusion, MMP-9 affects N-methyl-D-aspartate receptors lateral diffusion via integrin signaling
physiological function
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MMP-9 activity induced by iNOS-derived NO leads to detachment of hepatocytes from the extracellular matrix and cell death, in addition to regulating leukocyte migration across extracellular matrix barriers
physiological function
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MMP-9 catalytically induces angiogenesis via a basic fibroblast growth factor-2/fibroblast growth factor receptor-2 pathway. The enhanced angiogenesis catalyzed by neutrophil MMP-9 evokes also a localized, low threshold level vascular endothelial growth factor/vascular endothelial growth factor receptor-2 pathway, likely functioning in the formation and/or stabilization of blood vessels
physiological function
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MMP-9 directly delays wound healing through interference with re-epithelialization, MMP-9 interferes with the basement membrane protein structure, which in turn impedes keratinocyte migration, attachment, and the reestablishment of the epidermis
physiological function
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MMP-9 is a key enzyme in neutrophil biology
physiological function
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MMP-9 is essential for ischemia-induced neovascularization by modulating bone marrow-derived endothelial progenitor cells
physiological function
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MMP-9 is essential for osteoclastogenesis
physiological function
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MMP-9 is involved in both bacterial translocation and polymorphonuclear neutrophil granulocytes transmigration in rat severe acute pancreatitis
physiological function
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MMP-9 is involved in cardiomyocytes contractility dysfunction, MMP-9 treatment attenuates the voltage-induced contraction of primary cardiomyocytes
physiological function
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MMP-9 is required for tissue remodeling in response to natural hydroxyapatite
physiological function
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MMP-9 is the key factor involved in blood-brain barrier disruption and subsequent brain injury after photothrombotic cerebral ischemia in rats
physiological function
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MMP-9 plays a causal role in amyloid beta-induced cognitive impairment and neurotoxicity
physiological function
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MMP-9 plays a causative role in blood-brain barrier disruption after peripheral thermal injury
physiological function
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MMP-9 plays a pivotal role in vascular remodeling and development of atherosclerotic lesion
physiological function
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MMP-9 plays an important role in the function of the blood-brain barrier, the prolonged imbalance of MMP-9 and tissue inhibitor of metalloproteinase 1 is associated with the pathogenesis of non-herpetic acute limbic encephalitis
physiological function
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MMP-9 plays an important role in the pathogenesis of acute graft-versus-host disease
physiological function
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MMP-9 plays an important role in wound healing, angiogenesis, inflammation, tumor invasion, and metastasis
physiological function
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MMP-9 released from bone marrow-derived cells influences the progression of blood-brain barrier disruption in the ischemic brain, bone marrow-derived cell-derived MMP-9 contributes to blood-brain barrier dysfunction during early reperfusion period
physiological function
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MMP-9- mediated occludin degradation represents an important mechanism for blood brain barrier disruption in ischemic stroke
physiological function
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overexpression of MMP-9 in neoplastic and inflammatory cells in GC plays an important role in the progress of this carcinoma
physiological function
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the cooperation of p38 and MMP-9 may contribute to the mucin overproduction after inflammatory challenge with 4.0 ppm of acrolein for 21 days
physiological function
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the increased expression of MMP-9 may contribute to pathologic angiogenesis and/or to the instability of the vascular structure and could thereby cause hemorrhage in moyamoya disease
physiological function
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the recruitment of mesoangioblasts requires the secretion of MMP-9 by M2 cells
physiological function
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MMP-9 has a role as essential mediator in degradation/damage of the extracellular matrix of fetal membranes
physiological function
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MMP-9 is involved in the mechanism of cell-to-cell HIV-1 endocytosis in dendritic cells
physiological function
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MMP-9 significantly induced Smad3 phosphorylation and subsequent fibroblast proliferation. MMP cleaves membrane-bound precursor proteins and releases epidermal growth factor-like ligands that subsequently bind to epidermal growth factor receptor, and it stimulates the airway epithelium to produce fibrogenic mediators through activation of membrane-bound receptors. MMP-9 is required to cleave membrane-bound growth factors
physiological function
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MMP-9 soluble pro-enzyme is implicated in pathological events including cancer invasion. During skin wound healing, MMP-9 is expressed by the migrating leading-edge keratinocytes upon re-epithelialization of the wound
physiological function
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MMPs can promote cancer cell invasion by degradation of various extracellular matrix components resulting in release of growth factor and cytokines
physiological function
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neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis
physiological function
because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and beta-cell loss. Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide, the constituent of amyloid deposits in Alzheimer's disease
physiological function
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enzyme matrix metalloproteinase 9/gelatinase B is required for neural crest cell migration, which are neuroepithelial progenitors that convert into mesenchyme and migrate along defined paths throughout the embryo. The enzyme plays a role during neural crest cell detachment from the neural tube, overview
physiological function
matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide, the constituent of amyloid deposits in Alzheimer's disease
physiological function
the enzyme act as important oncogenes that improve invasiveness of cancer cells. MMP-9 activity is constitutively heightened in tissue samples from primary glioblastoma multiforme, the most common and aggressive malignant primary brain tumor in humans
physiological function
matrix metalloproteinase-9 is a phase-specific effector molecule, independent from Fas, in experimental autoimmune encephalomyelitis. MMP-9 triggers multiple sclerosis and the animal model of experimental autoimmune encephalomyelitis by the breakdown of the blood-brain barrier
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
variations in MMP-9 isoforms are observed, which coincide with the progression of tuberculosis infection. MMP-9 isoforms might influence the formation and progression of granuloma
physiological function
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matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide, the constituent of amyloid deposits in Alzheimer's disease
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physiological function
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enzyme matrix metalloproteinase 9/gelatinase B is required for neural crest cell migration, which are neuroepithelial progenitors that convert into mesenchyme and migrate along defined paths throughout the embryo. The enzyme plays a role during neural crest cell detachment from the neural tube, overview
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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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neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis
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additional information
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specific inhibition of MMP-9 leads to reduced extents of HIV-1 antigen presentation activity
additional information
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digestion of the intact enzyme with chondroitinase decreases the size of the molecule to 80 kDa
additional information
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enzyme MMP9 promotes neural crest cell emigration from the neural tube by enhancing breakage of laminin at the basement-membrane, mechanism of activity, overview
additional information
enzymes MMP1, MMP3, and MMP9 are synthesized and secreted by granulosa cells of different follicles in the chicken ovary, overview. The three MMP genes (MMP1, MMP3, and MMP9) are significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, MMP1 expression (both mRNA and protein) remains low in prehierarchical and preovulatory follicles but increases in postovulatory follicles (POFs). Both MMP3 and MMP9 expression levels increase during follicular maturation. MMP3 reaches maximal expression in the first largest follicle (F1), while MMP9 levels continue to rise in POF1 and POF2 after ovulation
additional information
the enzyme cleaves many substrates and is produced by most cell types as a zymogen, proMMP-9, in complex with the tissue inhibitor of metalloproteinases-1, TIMP-1, molecular modelling, overview
additional information
four isoforms of MMP-9 have been reported: the first is a latent form, a zymogen of 92 kDa. The second is obtained by cutting the prodomain of the latent form, resulting in a product of 82 kDa, which produces the active form of the enzyme. The third isoform is a heterodimer that originates from the binding of MMP-9 with the inhibitor TIMP-1, generating a product of 220 kDa. Finally, the fourth isoform corresponds to a 125 kDa heterodimer, made up of MMP-9 associated with lipocalin. Analysis of MMP-9 isoforms identification and determination of activities
additional information
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four isoforms of MMP-9 have been reported: the first is a latent form, a zymogen of 92 kDa. The second is obtained by cutting the prodomain of the latent form, resulting in a product of 82 kDa, which produces the active form of the enzyme. The third isoform is a heterodimer that originates from the binding of MMP-9 with the inhibitor TIMP-1, generating a product of 220 kDa. Finally, the fourth isoform corresponds to a 125 kDa heterodimer, made up of MMP-9 associated with lipocalin. Analysis of MMP-9 isoforms identification and determination of activities
additional information
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enzymes MMP1, MMP3, and MMP9 are synthesized and secreted by granulosa cells of different follicles in the chicken ovary, overview. The three MMP genes (MMP1, MMP3, and MMP9) are significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, MMP1 expression (both mRNA and protein) remains low in prehierarchical and preovulatory follicles but increases in postovulatory follicles (POFs). Both MMP3 and MMP9 expression levels increase during follicular maturation. MMP3 reaches maximal expression in the first largest follicle (F1), while MMP9 levels continue to rise in POF1 and POF2 after ovulation
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additional information
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enzyme MMP9 promotes neural crest cell emigration from the neural tube by enhancing breakage of laminin at the basement-membrane, mechanism of activity, overview
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