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Development of systems of medicines with sustained action on the basis of biodegradable polymers is a promising trend in modern pharmacology. Polyhydroxyalkanoates (POA) attract increasing attention due to their biodegradability and high biocompatibility, which make them suitable for development of novel drug dosage forms. We obtained microspheres on the basis of poly(3-hydroxybutyrate) (PHB) loaded with the antitumor drug paclitaxel. Morphology, drug release kinetics and effect on tumor cells in vitro of microspheres were studied. The data on the kinetics of drug release, biocompatibility and biological activity of the biopolymer microspheres in vitro showed that the studied system of prolonged drug release had lower toxicity and higher efficiency compared to the traditional dosage forms of paclitaxel.

Mutations in the C-terminal domain of tissue inhibitor of metalloproteinases-3 (TIMP-3) lead to autosomal dominant hereditary disease of the retina (Sorsby fundus dystrophy). Mouse knock-out and heterozygous knock-in fibroblasts and fibroblasts from patients with Sorsby fundus dystrophy exhibit some characteristics of myofibroblasts. Genetic changes in the timp-3 gene (TIMP-3) lead to a shift towards the myofibroblast phenotype in the fibroblast culture. It is hypothesized that Timp-3 (TIMP-3) plays a role of antitransformation agent preventing myofibroblast transformation in vivo and that the pathogenesis of Sorsby fundus dystrophy is associated with the loss of the antitransformation function by the mutant protein.

Mutations in the C-terminal domain of tissue inhibitor of metalloproteinases-3 (TIMP-3) are linked with Sorsby fundus dystrophy (autosomal dominant retinal dystrophy). Experiments on timp-3 gene knock-out and knock-in mice, carriers of dystrophy-linked Timp-3S156C mutation, showed that expression of mutant Timp-3S156C, in contrast to the normal one, is not regulated by phorbol-myristate-12-acetate and is retained at a high level in a medium without FCS. The mutant protein is not transported into the nucleus, while fibroblasts expressing it survive without FCS and other growth factors. It is hypothesized that normal Timp-3 is involved in the regulation of expression of its own timp-3 gene and, probably, other genes associated with growth and proliferation. The absence of this characteristic in mutant Timp-3S156C is presumably responsible for its accumulation in the extracellular matrix.

Matrix metalloproteinases belong to the key molecules of tissue remodeling involved in physiological and pathological processes of the female reproductive system. Adequate levels of their expression in the endometrium are essential for effective implantation and uneventful pregnancy. Chronic inflammatory process in the endometrium is associated with low tissue expression of metalloproteinase-9. Histologically verified chronic endometritis is associated with low serum activities of metalloproteinases 2 and 9, which are restored after combined etiotropic therapy. We measured serum levels of metalloproteinases in patients with chronic endometritis concomitant with sterility and its changes during the first days after magnetotherapy.

Mutations in the C-terminal domain of tissue inhibitor of metalloproteinases-3 (TIMP-3) are linked with Sorsby fundus dystrophy (autosomal dominant retinal dystrophy). Experiments on timp-3 gene knock-out and knock-in mice, carriers of dystrophy-linked Timp-3S156C mutation, showed that expression of mutant Timp-3S156C, in contrast to the normal one, is not regulated by phorbol-myristate-12-acetate and is retained at a high level in a medium without FCS. The mutant protein is not transported into the nucleus, while fibroblasts expressing it survive without FCS and other growth factors. It is hypothesized that normal Timp-3 is involved in the regulation of expression of its own timp-3 gene and, probably, other genes associated with growth and proliferation. The absence of this characteristic in mutant Timp-3S156C is presumably responsible for its accumulation in the extracellular matrix.

Three-stage treatment using a day hospital instead of a sanatorium with regards to the pattern of a tuberculosis process can achieve the results of closure of decay and abacillation cavities, which are not inferior to those with the conventional treatment, by reducing the basic regimen through the length of a hospital stage. The efficiency of two-stage treatment (day hospital--outpatient clinic) of lung tissue decay and culture-positive patients depends on the duration of the basic regimen, patient compliance, and the presence of a concomitant abnormality.

Mutations in the C-terminal domain of tissue inhibitor of metalloproteinases-3 (TIMP-3) lead to autosomal dominant hereditary disease of the retina (Sorsby fundus dystrophy). Mouse knock-out and heterozygous knock-in fibroblasts and fibroblasts from patients with Sorsby fundus dystrophy exhibit some characteristics of myofibroblasts. Genetic changes in the timp-3 gene (TIMP-3) lead to a shift towards the myofibroblast phenotype in the fibroblast culture. It is hypothesized that Timp-3 (TIMP-3) plays a role of antitransformation agent preventing myofibroblast transformation in vivo and that the pathogenesis of Sorsby fundus dystrophy is associated with the loss of the antitransformation function by the mutant protein.

Mutations in the C-terminal domain of tissue inhibitor of metalloproteinases-3 (TIMP-3) are linked with Sorsby fundus dystrophy (autosomal dominant retinal dystrophy). Experiments on timp-3 gene knock-out and knock-in mice, carriers of dystrophy-linked Timp-3S156C mutation, showed that expression of mutant Timp-3S156C, in contrast to the normal one, is not regulated by phorbol-myristate-12-acetate and is retained at a high level in a medium without FCS. The mutant protein is not transported into the nucleus, while fibroblasts expressing it survive without FCS and other growth factors. It is hypothesized that normal Timp-3 is involved in the regulation of expression of its own timp-3 gene and, probably, other genes associated with growth and proliferation. The absence of this characteristic in mutant Timp-3S156C is presumably responsible for its accumulation in the extracellular matrix.