Bansi Badan Mukherjee

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Osteopontin (OP) is a component of extracellular, bone, and urinary stone matrices, but the mechanism by which it is stably incorporated into such matrices remains unknown. By SDS-PAGE analysis of [125I]OP, treated with a catalytic amount of TG, we first demonstrate both intra- and intermolecular covalent cross-linking of OP. Most importantly, the analysis(More)
Osteopontin (OPN) is a 34-kDa, highly-phosphorylated glycoprotein with cell attachment properties that is a prominent constituent of the bone matrix. To aid in elucidating the function of this protein we have studied the cellular expression of OPN mRNA during the formation, growth and maturation of rat calvarial (membranous) and tibial (endochondral) bone.(More)
Awareness among the general population of the risk factors and warning symptoms of stroke is essential for preventative purposes and for immediate effective treatment. The aim of the present study was to assess the awareness, among the general population and stroke survivors, of the risk factors and warning symptoms of stroke, to develop an educational(More)
We have reported previously that the 69-kDa major phosphoprotein, secreted by normal rat kidney (NRK) cells, is osteopontin, a glycosylated bone matrix protein. Here we show that this 69-kDa osteopontin is secreted by NRK cells in both phosphorylated (pp69) and nonphosphorylated (np69) forms, with estimated isoelectric points of 3.8 and 4.5, respectively.(More)
BACKGROUND AND PURPOSE The prevalence rate of epilepsy in India ranges between 4.15 and 7.03 per 1000 population. In the developing countries, the major problems of epilepsy are lying in the treatment gap and discontinuation of treatment due to various adverse socio-economic factors. The objective of this study was to evaluate the rate of discontinuation of(More)
Osteopontin (OPN) is a sialic acid-rich, adhesive, extracellular matrix (ECM) protein with Arg-Gly-Asp cell-binding sequence that interacts with several integrins, including alpha(v)beta(3). Since the ECM is a key regulator of mammary gland morphogenesis, and mammary epithelial cells express OPN at elevated levels, we sought to determine whether this(More)
Elevated expression of osteopontin (OPN), a secreted adhesive phosphoglycoprotein, is frequently associated with many transformed cell lines of epithelial and stromal origin. Moreover, several clonal lines of preneoplastic JB6 cells derived from Balb/c mouse epidermal cultures (Colburn et al., 1978, 1979), upon treatment with 12-O-tetradecanoyl(More)
Osteopontin (OP), purified from rat bone, binds Ca2+ but whether different molecular forms of OPs derived from non-osteogenic sources and non-phosphorylated OP also possess this property remains to be determined. Furthermore, it is not known which specific site or sites of the molecule bind Ca2+. In the present study, following an established procedure,(More)
In a previous study we have shown that normal rat kidney (NRK) cells in vitro secrete a 69-kDa osteopontin in both phosphorylated (pp69) and nonphosphorylated (np69) forms. Only pp69 interacts with the cell surface and np69 forms a heat-dissociable complex with plasma fibronectin, suggesting functional modulation of osteopontin by phosphorylation. Using(More)
Using immunoprecipitation and tryptic peptide microsequencing we confirmed the identity of normal rat kidney (NRK) cell-secreted 69-kDa major phosphoprotein as osteopontin (OP). We then immunoselected a 1.4-kilobase pair (kb) OP cDNA from a lambda gt11 library prepared from Kirsten sarcoma virus-transformed NRK (KNRK) cellular mRNA, using rabbit anti-69-kDa(More)