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The sera of 40 patients with gastric cancer and 11 patients as the control group were studied for the detection of matrix metalloproteinases. The malignant behavior of tumor cells mainly depends on the capability of invasion and the metastasis of cancer cells. After the components of the extracellular matrix (ECM) are degraded, tumor cells invade the surrounding tissue and the vascular or lymphatic vessels to form metastasis colonies at distant sites. Extracellular proteolytic enzymes implicate the invasion and metastasis of cancer. Proteolytic enzymes from tumors lead to the breakdown of basement membranes and the ECM, thereby, facilitating cancer cell invasion into the surrounding normal tissue. Proteinase activity is overexpressed in the serum of stage 3 and 4 tumors compared to stage 1 and 2 tumors. ProMMP-9 was detected in the serum of patients of gastric cancer by SDS polyacrylamide gel electrophoresis (SDS-PAGE) and SDS-PAGE zymography, with its molecular mass of 92 kDa. MMP-9 in serum plays an important role in the progression of gastric cancer.

When exposed to cadmium a highly resistant strain P. aeruginosa san ai responds by an increased metalloprotein expression (particularly denitrification proteins), an enhanced respiration, and a pronounced thiol-disulfide protein modifications.

The Pseudomonas aeruginosa san ai strain was investigated for its capability to degrade the 2,6-di-tertbutylphenol (2,6-DTBP) plastic additive, a hazardous and toxic substance for aquatic life. This investigation was performed under different parameter values: 2,6-DTBP concentration, inoculum size, pH, and temperature. The GC-MS study showed that P. aeruginosa efficiently degraded 2,6-DTBP in the pH range of 5-8 at higher temperatures. Under exposure to 2,6-DTBP concentrations of 2, 10, and 100 mg L À1 , the strain degraded by 100, 100, and 85%, respectively, for 7 days. Crude enzyme preparation from the biomass of P. aeruginosa san ai showed higher efficiency in 2,6-DTBP removal than that shown by whole microbial cells. Gene encoding for the enzymes involved in the degradation of aromatic compounds in P. aeruginosa san ai was identified. To complement the genomic data, a comparative proteomic study of P. aeruginosa san ai grown on 2,6-DTBP or sunflower oil was conducted by means of nanoLC-MS/MS. The presence of aromatic substances resulted in the upregulation of aromatic ring cleavage enzymes, whose activity was confirmed by enzymatic tests; therefore, it could be concluded that 2,6-DTBP might be degraded by ortho-ring cleavage. A comparative proteomics study of P. aeruginosa san ai indicated that the core molecular responses to aromatic substances can be summarized as the upregulation of proteins responsible for amino acid metabolism with emphasized glutamate metabolism and energy production with upregulated enzymes of glyoxylate bypass. P. aeruginosa san ai has a high capacity to efficiently degrade aromatic compounds, and therefore its whole cells or enzymes could be used in the treatment of contaminated areas.

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