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Nikolay A. Zorin

Publications and source records attributed to Nikolay A. Zorin.

2 recordsLinked to original sources

Alpha2-Macroglobulin Modulates Interactions between Lymphocytes and Fibroblasts.

The aim of the present study was to evaluate the influence of apha2-macroglobulin (alpha(2)M) on lymphocyte adhesion to fibroblasts. Peripheral blood lymphocytes from healthy donors and two fibroblast lines (human diploid embryo fibroblasts M-19 and mouse transformed fibroblasts L929) were used in the experiments. alpha(2)M treatment of fibroblast monolayer appeared to result in the enhancement of lymphocyte adhesion to fibroblasts. The number of attached lymphocytes was increased by 2-2.5 times. It should be noted that the effect of alpha(2)M didn't depend on the conformational molecule changes, since either native or methylamine or plasmin transformed alpha(2)M approximately at the same fashion increased the lymphocyte adhesion to both allogeneic and xenogeneic fibroblasts. B lymphocytes were predominant cells that were attached to fibroblast monolayer without alpha(2)M treatment. However the percentage of adherent T lymphocytes was increased substantially after the fibroblast monolayer treatment by alpha(2)M. Subpopulation analysis has shown that fibroblast pretreatment by alpha(2)M didn't result in a selective adhesion of CD4(+) or CD8(+) T lymphocytes, but increased the adhesiveness for both T lymphocyte subpopulations. The data obtained demonstrate that besides its participation in the processes of fibroblast adhesion alpha(2)M is capable to modify the contact interaction of these cells with lymphocytes that may have an influence on the functional consequences of this process.

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Adhesion of Fibroblasts to Immobilized alpha(2)-Macroglobulin.

This study examines effects of alpha(2)-macroglobulin (alpha(2)M) on adhesion of fibroblasts. Native alpha(2)M and transformed form of alpha(2)M, alpha(2)M-plasmin, were bound to plastic. Adhesion of mouse L929 and human embryo M-19 fibroblasts to immobilized alpha(2)M was estimated under various conditions by counting adherent cells using videomicroscopy and computer-assisted image analysis. alpha(2)M-plasmin, bound to plastic, induced adhesion and spreading of mouse L929 and human M-19 fibroblasts. Neither native alpha(2)M nor plasmin alone did not induce fibroblast adhesion. The adhesion to alpha(2)M-plasmin was undetectable at 4 degrees C, as well as when sodium azide was added or divalent ions were removed. These findings provide novel information on alpha(2)M functions. On the basis of these observations we hypothesized that alpha(2)M, immobilized in the extracellular matrix, can participate in the regulation of microenvironment effects on the cells, and, in particular, influence on fibroblast adhesion.

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