Maurice B. Feinstein
Professor
Department of Cell Biology
University of Connecticut Health Center
Farmington, CT 06032
phone 860 679 3705
fax 860 679 3693
email feinstein@nso1.uchc.edu
Education
B.S., Columbia University, College of Pharmaceutical Sciences
M.S., Columbia University, College of Pharmaceutical Sciences
Ph.D., State University of New York Health Science Center at Brooklyn
Research interests
Platelets are essential for normal blood clotting and primary hemostasis, but under pathological conditions can lead to thrombosis as in myocardial infarction and stroke. Platelet reactivity to stimuli is regulated in part by calcium ion, prostaglandins and thromboxanes (metabolites of arachidonic acid), nitric oxide and cyclic nucleotides (e.g., cyclic AMP, cyclicGMP). Particular attention in this laboratory was devoted to understanding how platelet aggregating agents acting at cell surface receptors cause the formation of intracellular second messengers that initiate or modulate the biochemical reactions that lead to secretion of platelet products and aggregation of platelets. These studies involved investigations of signal transduction events such as the mechanisms for intracellular Ca2+ mobilization, formation of InsP3, and release of arachidonic acid from phospholipids. A major focus was on protein phosphorylation mechanisms involved in the activation of phospholipase A2 to liberate arachidonic acid, and phosphoinositide metabolism related to the formation of the Ca2+ -releasing second messenger InsP3. In addition, the mechanisms by which cAMP opposes platelet activation have been investigated.
In recent years we cloned and sequenced the cDNA for a protein designated as CHERP/Scaf6 based on early evidence that it might participate in regulation of Ca2+ signaling.. The protein expressed by the gene located on chromosome 19 appears to shuttle between nucleus and cytoplasmic compartments, and may associate with the endoplasmic reticulum. Based on its primary structure this protein has unique features but belongs to the extended family of RS proteins, and may serve in part to regulate mRNA splicing. However, it may have other functions, especially in the extranuclear compartment, that affect cell proliferation and mechanisms involving Ca2+ signaling. The laboratory has employed molecular biological, biochemical and biophysical techniques (e.g. cDNA cloning, PCR, RT-PCR, Northern blotting, siRNA knockout of genes, ligand binding assays, immunocytochemistry and fluorescence imaging of Ca2+ transients).
Department of Cell Biology Faculty
