Matrix metalloproteinase-9 (MMP-9), also known as gelatinase B, is a zinc-dependent endopeptidase critical for extracellular matrix (ECM) remodeling. In rats, MMP-9 plays pivotal roles in physiological processes and pathological conditions, including cardiovascular remodeling, neuroinflammation, and cancer progression. Its expression is tightly regulated, and dysregulation is implicated in diseases such as atherosclerosis, traumatic brain injury (TBI), and stroke .
Vascular Remodeling: Overexpression in Fischer rats enhances smooth muscle cell (SMC) migration, leading to luminal dilation and reduced extracellular matrix content post-injury .
Atherosclerosis and Aneurysms: Elevated MMP-9 activity promotes plaque instability and aneurysm formation. Inhibition via doxycycline reduces aortic inflammation and aneurysm growth .
Cerebral Ischemia: MMP-9 expression peaks 24 hours post-middle cerebral artery occlusion (MCAO), localizing to endothelial cells and neutrophils. Inhibition reduces infarct size .
Traumatic Brain Injury (TBI): MMP-9 levels rise post-injury, correlating with edema and neuronal damage. Minocycline administration reduces MMP-9 by 9.5% in Wistar rats, mitigating injury severity .
Epilepsy: MMP-9 knockout rats exhibit reduced seizure susceptibility, while overexpression accelerates epileptogenesis .
Tumor Progression: MMP-9 facilitates angiogenesis and ECM degradation, promoting metastasis. Its activity is modulated by chemokine cleavage (e.g., CXCL12 degradation) .
Feature | Human MMP9 | Rat MMP9 |
---|---|---|
Pro-domain | Cysteine residue (binds lipocalin) | Serine residue (altered binding) |
Linker Domain | Shorter, less glycosylation | Longer, 23 additional amino acids |
Molecular Weight | 92 kDa (pro), 88 kDa (active) | 105 kDa (pro), 95 kDa (active) |
Neurological Role | Synaptic remodeling, neuroinflammation | Epileptogenesis, TBI recovery |
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
HEK293 Cells.
APHQRQPTYV VFPRDLKTSN LTDTQLAEDY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS ETLKAIRSPR CGVPDVGKFQ TFEGDLKWHH HNITYWIQSY TEDLPRDVID DSFARAFAVW SAVTPLTFTR VYGLEADIVI QFGVAEHGDG YPFDGKDGLL AHAFPPGPGI QGDAHFDDDE LWSLGKGAVV PTYFGNANGA PCHFPFTFEG RSYLSCTTDG RNDGKPWCGT TADYDTDRKY GFCPSENLYT EHGNGDGKPC VFPFIFEGHS YSACTTKGRS DGYRWCATTA NYDQDKLYGF CPTRADVTVT GGNSAGEMCV FPFVFLGKQY STCTGEGRSD GRLWCATTSN FDADKKWGFC PDQGYSLFLV AAHEFGHALG LDHSSVPEAL MYPMYHYHED SPLHEDDIKG IQHLYGRGSK PDPRPPATTA AEPQPTAPPT MCPTAPPMAY PTGGPTVAPT GAPSPGPTGP PTAGPSEAPT ESSTPVDNPC NVDVFDAIAD IQGALHFFKD GRYWKFSNHG GSQLQGPFLI ARTWPALPAK LNSAFEDPQS KKIFFFSGRK MWVYTGQTVL GPRSLDKLGL GSEVTLVTGL LPRRGGKALL ISRERIWKFD LKSQKVDPQS VTRLDNEFSG VPWNSHNVFH YQDKAYFCHD KYFWRVSFHN RVNQVDHVAY VTYDLLQCPH HHHHH.
Matrix Metalloproteinase-9 (MMP-9), also known as gelatinase B, is a member of the matrix metalloproteinase (MMP) family. These enzymes are zinc and calcium-dependent endopeptidases capable of degrading various components of the extracellular matrix (ECM), such as collagen, elastin, and proteoglycans . MMP-9 is particularly notable for its role in both physiological and pathological processes, including tissue remodeling, inflammation, and cancer metastasis .
MMP-9 is initially produced as an inactive zymogen (proMMP-9) that requires activation to become enzymatically functional . The activation process involves the cleavage of the pro-domain, which masks the catalytic site of the enzyme. This cleavage can be mediated by other proteases, oxidative modifications, or conformational changes due to substrate binding .
MMP-9 plays a crucial role in various biological processes:
MMP-9 is implicated in several pathological conditions:
Recombinant MMP-9 (Rat) is a laboratory-produced version of the enzyme, often used in research to study its functions and interactions. The recombinant form allows for controlled experiments to understand the enzyme’s role in various biological and pathological processes.