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Regulation of matrix metalloproteinase activity in health and disease
TLDR
Knowledge about regulation of MMP activity is essential for understanding various physiological processes and pathogenesis of diseases, as well as for the development of new MMP targeting drugs. Expand
A Key Role for Mast Cell Chymase in the Activation of Pro-matrix Metalloprotease-9 and Pro-matrix Metalloprotease-2*
TLDR
A key role for mast cell chymase is indicated in the regulation of pro-MMP-2 and -9 activities and the results suggest an important role in regulating connective tissue homeostasis. Expand
Medium- and short-chain dehydrogenase/reductase gene and protein families
TLDR
It seems that while mammals evolved with a medium-chain alcohol dehydrogenase family (MDR), fruit flies utilized an ancestral SDR enzyme to aid them in colonizing the emerging ecological niches that appeared around 65 million years ago. Expand
S100A4 involvement in metastasis: deregulation of matrix metalloproteinases and tissue inhibitors of matrix metalloproteinases in osteosarcoma cells transfected with an anti-S100A4 ribozyme.
TLDR
S100A4 may exert its effect on metastasis formation not only by stimulating the motility of tumor cells but also by affecting their invasive properties through influencing the expression of MMPs and their endogenous inhibitors. Expand
The role of liver alcohol dehydrogenase isoenzymes in the oxidation of glycolethers in male and female rats.
TLDR
The results indicated that only the ADH-3 isoenzyme effectively oxidized the glycolethers in rat liver, suggesting that the activity of ADH is higher in female than in male rat liver. Expand
Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF.
TLDR
The high activity observed with secondary alcohols and especially with (R)-(+)-cis-verbenol, indicates that these flies can metabolize terpenes and may be part of the pheromone system in the flies with D. melanogaster alcohol dehydrogenase playing a role in pherOMone metabolism. Expand
Macrophages secrete matrix metalloproteinase 9 covalently linked to the core protein of chondroitin sulphate proteoglycans.
TLDR
A new heterodimer complex is described, in which proMMP-9 is covalently linked to the core protein of chondroitin sulphate proteoglycan (CSPG) through one or more disulphide bridges. Expand
In vitro reconstitution of complexes between pro‐matrix metalloproteinase‐9 and the proteoglycans serglycin and versican
TLDR
This paper shows that reduction‐sensitive and SDS‐stable heteromers may be reconstituted in vitro by mixing proMMP‐9 with either serglycin, versican or CSPGs isolated from various monocytic cell lines, and shows that different regions in the PEX domain are involved formation of these heteromers. Expand
Calcium-induced activation and truncation of promatrix metalloproteinase-9 linked to the core protein of chondroitin sulfate proteoglycans.
TLDR
The results indicate that the interaction between the MMP-9 and the core protein of the CSPG was the causal factor in the calcium-induced activation and truncation of the gelatinase, and that this process was not due to a general electrostatic effect. Expand
Matrix metalloproteinases in subjects with type 1 diabetes
TLDR
The authors' MMP analysis of serum from a limited number of patients with type 1 diabetes suggest that such analysis is potentially useful as markers in studies of people at risk of progression to chronic kidney disease. Expand
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