Kinetic Analysis of the Binding of Hemopexin-Like Domain of Gelatinase B Cloned and Expressed in Pichia pastoris to Tissue Inhibitor of Metalloproteinases-1

Stute, Jörg; Pourmotabbed, Tayebeh; Tschesche, Harald

doi:10.1023/b:jopc.0000005499.51466.50

Cited by 6 publications

(5 citation statements)

References 22 publications

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“…MMP-9 has a complex domain structure, with a signal peptide at the N-terminus, followed by a propeptide, a catalytic domain with a zinc ion binding site, three fibronectin type II inserts, a proline-rich and heavily O -glycosylated linker, and a hemopexin domain located at the C-terminus of the protein (Stute et al, 2003). The propeptide contains an evolutionarily conserved PRCGVPDV domain that binds the zinc ion in the catalytic domain and blocks the activity of the enzyme until it is cleaved (Van Wart and Birkedal-Hansen, 1990; Becker et al, 1995).…”

Section: Matrix Metalloproteinase-9mentioning

confidence: 99%

Matrix metalloproteinase-9 involvement in the structural plasticity of dendritic spines

2014

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Dendritic spines are the locus for excitatory synaptic transmission in the brain and thus play a major role in neuronal plasticity. The ability to alter synaptic connections includes volumetric changes in dendritic spines that are driven by scaffolds created by the extracellular matrix (ECM). Here, we review the effects of the proteolytic activity of ECM proteases in physiological and pathological structural plasticity. We use matrix metalloproteinase-9 (MMP-9) as an example of an ECM modifier that has recently emerged as a key molecule in regulating the morphology and dysmorphology of dendritic spines that underlie synaptic plasticity and neurological disorders, respectively. We summarize the influence of MMP-9 on the dynamic remodeling of the ECM via the cleavage of extracellular substrates. We discuss its role in the formation, modification, and maintenance of dendritic spines in learning and memory. Finally, we review research that implicates MMP-9 in aberrant synaptic plasticity and spine dysmorphology in neurological disorders, with a focus on morphological abnormalities of dendritic protrusions that are associated with epilepsy.

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Section: Matrix Metalloproteinase-9mentioning

confidence: 99%

Matrix metalloproteinase-9 involvement in the structural plasticity of dendritic spines

2014

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“…The activity of MMPs is specifically inhibited by the tissue inhibitors of metalloproteinases (TIMPs), which bind to the highly conserved zinc‐binding site of active MMPs. TIMPs also form complexes with progelatinases via their hemopexin‐like domain (12). The hemopexin domain of MMP‐9 is important for association with TIMP‐1 (12) and TIMP‐3 (13).…”

Section: Discussionmentioning

confidence: 99%

“…TIMPs also form complexes with progelatinases via their hemopexin‐like domain (12). The hemopexin domain of MMP‐9 is important for association with TIMP‐1 (12) and TIMP‐3 (13). In addition, the hemopexin domain of MMP‐9 has a high‐affinity binding site for gelatin (14).…”

Section: Discussionmentioning

confidence: 99%

Association of a nonsynonymous single‐nucleotide polymorphism of matrix metalloproteinase 9 with giant cell arteritis

Rodríguez-Pla

Beaty

Savino

et al. 2008

Arthritis & Rheumatism

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Objective. Giant cell arteritis (GCA) is the most common type of primary vasculitis. Matrix metalloproteinase 9 (MMP-9) is present in arterial lesions of GCA and may be involved in its pathogenesis. We investigated whether certain genotypes of 4 single-nucleotide polymorphisms (SNPs) of MMP-9 are overrepresented in patients with histologically confirmed GCA.Methods. Four SNPs of MMP-9, rs3918242 in the promoter region and 3 nonsynonymous coding SNPs (rs3918252, rs17576, and rs2250889) were genotyped by polymerase chain reaction-restriction fragment length polymorphism analysis in 58 white patients for whom there was a clinical suspicion of GCA. Thirty of these patients had histologically confirmed GCA (group 1), and 28 patients had negative results of a temporal artery biopsy for GCA (group 2). Estimates of the genotype distributions of each of these SNPs in a white population were determined using publicly available genotype data for a panel of 23 individuals (group 3).Results. Although 1 SNP was monomorphic in all 3 groups, we observed statistically significant differences in the genotype distributions for rs2250889 between group 1 and group 2 (P ‫؍‬ 0.005) and between group 1 and group 3 (P ‫؍‬ 0.009), but not between groups 2 and 3 (P ‫؍‬ 0.965).Conclusion. These data derived from a sample of patients with GCA suggest that the G allele of MMP-9 polymorphism rs2250889 is overrepresented in patients with histologically confirmed GCA. Clearly, larger sample sizes will be necessary to confirm this suggestive association and better characterize a possible linkage disequilibrium structure among polymorphisms.

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“…It is an enzyme that breaks down the ECM. The major structure of MMP-9 (gelatinase B) (EC3.4.24.25) includes a signal peptide, propeptide, catalytic domain, three tandem repeats of fibronectin type II inserts within the catalytic domain, a proline-rich and extensively O-glycosylated linker, and a hemopexin-like domain (10). MMP-9 plays a significant role in the penetration of human cytotrophoblast cells into the endometrium, as well as in embryo implantation and development (11).…”

Section: Key Pointmentioning

confidence: 99%

The association of matrix metalloproteinase-9 and fetal fibronectin in the first trimester threatened miscarriage

Maki,

Ali,

Rawi

2024

Immunopathol Persa

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Introduction: Vaginal bleeding during the first trimester of pregnancy, accompanied by a positive fetal heart rate and a closed cervix, is medically referred to as a threatened miscarriage. This condition is considered the most common complication within the first 12 weeks of pregnancy. It is important to note that, this condition is a potential indication of danger to the fetus, and therefore; requires immediate medical attention and monitoring. Objectives: To evaluate the association of putative biomarkers matrix metalloproteinase-9 (MMP-9) and fetal fibronectin (fFN) in threatened miscarriage. Patients and Methods: A case-control study on threatened miscarriage was conducted at Alkarama hospital and Ibn al Balady Hospital in Baghdad. Serum levels of fFN and MMP-9 were analyzed in 91 pregnant women with matching gestational ages, divided into two groups of threatened miscarriage (patient: n=30) and healthy pregnant women (control: n=61). The differences in serum concentration of fFN and MMP-9 between the two groups, as well as their correlation with clinical outcomes, were statistically evaluated. Results: There were variations in serum concentrations of matrix metalloproteinase9 between the threatened miscarriage group (49.34±1.08 pg/mL) and the control group (12.19±4.90 pg/mL). Statistical analysis showed a p-value of 0.009. FFN levels were found to be higher in the threatened miscarriage patient group (467.85±6.22 pg/mL) compared to the control group (230.66±37.44 pg/mL), with a P-value of 0.003. A positive correlation was observed between MMP-9 and fFN (r=0.877, P=0.001). The 95% confidence interval for fFN was (0.9-0.992) and for MMP-9 was (0.78-0.96). Conclusion: Increased levels of MMP-9 and fFN have been associated with a higher risk of fetal demise.

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Kinetic Analysis of the Binding of Hemopexin-Like Domain of Gelatinase B Cloned and Expressed in Pichia pastoris to Tissue Inhibitor of Metalloproteinases-1

Cited by 6 publications

References 22 publications

Matrix metalloproteinase-9 involvement in the structural plasticity of dendritic spines

Matrix metalloproteinase-9 involvement in the structural plasticity of dendritic spines

Association of a nonsynonymous single‐nucleotide polymorphism of matrix metalloproteinase 9 with giant cell arteritis

The association of matrix metalloproteinase-9 and fetal fibronectin in the first trimester threatened miscarriage

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