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V M Dixit

Publications and source records attributed to V M Dixit.

189 records · Page 11Linked to original sources
PubMed1984

Isolation and characterization of a heparin-binding domain from the amino terminus of platelet thrombospondin.

Calcium-replete thrombospondin has been purified from outdated platelets using heparin-Sepharose affinity chromatography, gelatin-Sepharose to remove fibronectin, and gel filtration to eliminate low-molecular-weight heparin-binding proteins. Edman degradation of six different preparations revealed the amino-terminal sequence of thrombospondin (TSP) to be Asn-Arg-Ile-Pro-Glu-Ser-Gly-Gly-Asp-Asn-Ser-Val-Phe-. This sequence was obtained in initial yields as high as 85%, indicating that no blocked chains are present. Cleavage of calcium-replete TSP with thermolysin or plasmin results in the production of relatively stable fragments. Chromatography of these digests on heparin-Sepharose followed by elution with 0.6 M NaCl affords purification of an Mr 25,000 fragment from the thermolysin digest and an Mr 35,000 fragment from the plasmin digest. The binding of these fragments to heparin-Sepharose does not require divalent metal ions. Neither fragment is disulfide-bonded to other fragments present in the digests. The heparin-binding domains from both digests have similar amino acid compositions and their tryptic peptide maps on high performance liquid chromatography are identical with the exception of one peptide unique to each fragment. Automated Edman degradation in a vapor-phase sequenator of the thermolytic heparin-binding domain electroeluted from sodium dodecyl sulfate-gels indicates that the heparin-binding domain resides at the amino terminus of the Mr 180,000 TSP peptide chain.

Amino Acid Sequence↗
PubMed1984

Isolation of the fibrinogen-binding region of platelet thrombospondin.

Purified platelet thrombospondin binds to immobilized fibrinogen if both Ca++ and Mg++ are present. Digestion of the purified molecule with thermolysin results in a limited number of discrete proteolytic fragments. When such digests are subjected to affinity chromatography on immobilized fibrinogen, only the fragments with Mr of 120,000 and 140,000 are specifically bound and subsequently eluted by the addition of EDTA to the column buffer. Examination by SDS-PAGE under both reducing and nonreducing conditions reveals that the fibrinogen-binding domain is derived from the region of the thrombospondin molecule containing the interchain disulfide bonds. The requirement for Ca++ and Mg++ for optimal binding to fibrinogen is also manifest by the Mr 120,000/140,000 thermolytic fragments.

Blood Platelets↗
PubMed1981

A study of subacute sclerosing panencephalitis in Kenya.

A retrospective study was made over a five-year period of 53 patients at the Kenyatta National Hospital, Kenya, who presented with subacute sclerosing panencephalitis. The clinical, EEG and serological findings are similar to those found in other studies. As identified by epidemiological studies elsewhere, the factors which are likely to have a bearing on the aetiology of the disease are prevalent throughout the Kenya, yet there is a strong rural distribution of cases in this study. No cases have been reported from the Masai tribe. These features are discussed with regard to the possible implications for the aetiology of the disease.

Adolescent↗
PubMed1979

The mechanism of hyperlipidaemia in the nephrotic syndrome.

The mechanism of hyperlipidaemia in the nephrotic syndrome has not been fully established. We propose that it results from hypoalbuminaemia due to inhibition of the reaction catalysed by lecithin cholesterol acyltransferase converting cholesterol of high density lipoproteins to cholesterol esters and to an inhibition of high density lipoprotein particle formation from very low density lipoproteins due to reduced activity of lipoprotein lipase.

Child↗
PubMedDate not supplied

Characterization of thrombospondin synthesis, secretion and cell surface expression by human tumor cells.

Previous studies have shown that thrombospondin (TSP) is an adhesion factor for some human tumor cells. The previous studies have shown further that tumor cells which utilize TSP as an adhesion factor also synthesize it. This study continues the effort to understand how TSP production and expression are regulated in human tumor cells and the consequences of this for the cells. It is shown that differences among cell lines in their capacity to biosynthesize TSP are associated with differences in TSP specific mRNA levels. This indicates that biosynthesis is regulated at the transcriptional level. There is also a direct relationship between TSP biosynthesis and secretion into the culture medium and expression at the cell surface. The cells which are the most biosynthetically active secrete amounts of TSP into the culture medium that are sufficient to elicit a detectable response in the cell-substrate adhesion assay. The kinetics of TSP secretion by these cells are in accord with the kinetics of attachment and spreading of the same cells in the absence of exogenous adhesion factors. These data are consistent with the idea that endogenously produced TSP promotes the adhesion of the cells which synthesize it in an autocrine manner.

Blotting, Northern↗
PubMedDate not supplied

Thrombospondin binds falciparum malaria parasitized erythrocytes and may mediate cytoadherence.

Plasmodium falciparum infected erythrocytes containing mature trophozoites and schizonts sequester along venular endothelium and are not in the peripheral circulation of patients with malaria. Knobs appear on infected erythrocytes and are the points of attachment to endothelium. Sequestration may protect the parasite from splenic destruction and may play a role in the pathogenesis of cerebral malaria. Correlates of sequestration have been developed in vitro using cultured human endothelium and an amelanotic melanoma cell line. Knobless strains (K-) of P. falciparum fail to sequester in vivo and to bind to cells in vitro. We now present evidence that the receptor for cytoadherence is the glycoprotein, thrombospondin. Aotus monkey or human erythrocytes containing knobby (K+) but not Aotus erythrocytes containing knobless strains of P. falciparum bind to immobilized thrombospondin. Neither binds to the adhesive proteins laminin, fibronectin, factor VIII/von Willebrand factor or vitronectin. Both soluble thrombospondin and anti-thrombospondin antibodies inhibit binding of parasitized Aotus erythrocytes to immobilize thrombospondin and to melanoma cells which secrete thrombospondin.

Animals↗
PubMedDate not supplied

Solid-phase extraction and GC/MS confirmation of barbiturates from human urine.

A highly selective and sensitive procedure has been developed for isolating and identifying barbiturates in human urine. With a new disposable bonded silica gel solid-phase extraction (SPE) column and hexobarbital as an internal standard (IS), amobarbital, butabarbital, pentobarbital, phenobarbital, secobarbital, and methaqualone were selectively isolated from endogenous urine components. Capillary gas chromatography/ion trap mass spectrometry (GC/MS) analysis of the extracts generated a full mass spectrum for the detection, identification, and quantitation of barbiturates. Linear quantitative response curves for the drugs have been generated over a concentration range of 20-500 ng/mL. Overall extraction efficiencies for drugs averaged greater than 90%, and the quantitative response curves exhibited correlation coefficients of 0.996 to 0.999.

Amobarbital↗