Learn More
Binding of different regulatory subunits and methylation of the catalytic (C) subunit carboxy-terminal leucine 309 are two important mechanisms by which protein phosphatase 2A (PP2A) can be regulated. In this study, both genetic and biochemical approaches were used to investigate regulation of regulatory subunit binding by C subunit methylation. Monoclonal(More)
Carboxymethylation of proteins is a highly conserved means of regulation in eukaryotic cells. The protein phosphatase 2A (PP2A) catalytic (C) subunit is reversibly methylated at its carboxyl terminus by specific methyltransferase and methylesterase enzymes which have been purified, but not cloned. Carboxymethylation affects PP2A activity and varies during(More)
Chemerin is a potent chemoattractant for cells expressing the serpentine receptor CMKLR1 (chemokine-like receptor 1), such as plasmacytoid dendritic cells and tissue macrophages. The bioactivity of chemerin is post-translationally regulated; the attractant circulates in blood in a relatively inactive form (prochemerin) and is activated by carboxyl-terminal(More)
Chemerin is a chemoattractant involved in immunity that may also function as an adipokine. Chemerin circulates as an inactive precursor (chem163S), and its activation requires proteolytic cleavages at its C terminus, involving proteases involved in coagulation, fibrinolysis, and inflammation. However, the key proteolytic steps in prochemerin activation in(More)
Angiogenesis is a highly organized process controlled by a series of molecular events. While much effort has been devoted to identifying angiogenic factors and their reciprocal receptors, far less information is available on the molecular mechanisms underlying directed endothelial cell migration. To search for novel proteins that participate in this(More)
Chemerin is a novel chemoattractant recognized by chemokine-like receptor 1 (CMKLR1), a serpentine receptor expressed primarily by plasmacytoid dendritic cells, natural killer cells, and macrophages. Human prochemerin circulates in plasma as an inactive precursor. Its chemotactic activity is expressed upon cleavage of the C-terminal amino acid residues by(More)
Osteopontin (OPN), which is highly expressed in malignant glioblastoma (GBM), possesses inflammatory activity modulated by proteolytic cleavage by thrombin and plasma carboxypeptidase B2 (CPB2) at a highly conserved cleavage site. Full-length OPN (OPN-FL) was elevated in cerebrospinal fluid (CSF) samples from all cancer patients compared with noncancer(More)
Chemerin is a chemoattractant involved in innate and adaptive immunity as well as an adipokine implicated in adipocyte differentiation. Chemerin circulates as an inactive precursor in blood whose bioactivity is closely regulated through proteolytic processing at its C terminus. We developed methodology for production of different recombinant chemerin(More)
The chemopreventive effects of Bowman-Birk protease inhibitor (BBI), a soybean polypeptide, and its palmitic acid conjugate, Pal-BBI, on 7,12-dimethylbenz[a]anthracene (DMBA)-induced transformation were investigated by using an in vitro whole organ culture system of mouse mammary glands. The transformation incidence was measured as the number of glands(More)
1 CHEMERIN 158K IS THE DOMINANT CHEMERIN ISOFORM IN SYNOVIAL AND CEREBROSPINAL FLUIDS BUT NOT IN PLASMA. Lei Zhao, Yasuto Yamaguchi, Shadi Sharif, Xiao-Yan Du, David M. Lee, Lawrence D. Recht, William H. Robinson, Jason J. Song, John Morser and Lawrence L.K. Leung 6* From the Division of Hematology and Division of Immunology and Rheumatology, Department of(More)