835 S. Wolcott Ave., (M/C 901)
Chicago, IL 60612-7342
312-996-7620 phone
312-996-1414 fax

Kate Bárány, Ph.D.
Professor Emerita

Our research deals with the regulation of smooth muscle contraction focusing on the role of protein phosphorylation. We have previously demonstrated that myosin light chain phosphorylation is a prerequisite of smooth muscle contraction. We have recently shown that in addition to the myosin light chain, other proteins, such as the intermediate filament proteins desmin and vimentin, and a new 28-kDa protein of unknown origin, are also phosphorylated in intact smooth muscle. The extent of phosphorylation of these proteins in activated, contracting and relaxing muscles is determined to establish the relationship between protein phosphorylation and mechanical activity of smooth muscle. A particular aspect of this functional study is the comparison of phosphoproteins between pregnant and nonpregnant uterine muscles to delineate the pathway which leads to the increased force production of the uterus during fetus delivery.

There is a large variation in the physiological and pharmacological behavior of smooth muscles. We postulate that a contributing factor is the existence of protein isoforms. Therefore, we are involved in the characterization of myosin light chain isoforms from various tissues and different species.

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