pubmed-article:9915807 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9915807 | lifeskim:mentions | umls-concept:C0023270 | lld:lifeskim |
pubmed-article:9915807 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
pubmed-article:9915807 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:9915807 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
pubmed-article:9915807 | lifeskim:mentions | umls-concept:C1166645 | lld:lifeskim |
pubmed-article:9915807 | lifeskim:mentions | umls-concept:C0332285 | lld:lifeskim |
pubmed-article:9915807 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
pubmed-article:9915807 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:9915807 | pubmed:dateCreated | 1999-3-3 | lld:pubmed |
pubmed-article:9915807 | pubmed:abstractText | Four lines of evidence indicate that a specific high affinity binding site on the surface of Leishmania donovani promastigotes mediates rapid internalization and degradation of hemoglobin. 1) Binding and uptake of 125I-hemoglobin by Leishmania followed saturation kinetics and were competed by unlabeled hemoglobin but not by globin or hemin or other heme- or iron-containing proteins. 2) Immunogold labeling studies revealed that, at 4 degreesC, hemoglobin binding was localized in the flagellar pocket of the promastigotes. Indirect immunofluorescence assays showed that, at 37 degreesC, the bound hemoglobin in such cells entered an endocytic compartment within 2 min and dispersed throughout the cell body by 15 min. 3) After incubation with hemoglobin-gold conjugates at 25 degreesC or 37 degreesC, the particles accumulated in discrete intracellular vesicles. 4) A single biotinylated protein of 46 kDa was revealed when solubilized membranes from surface biotinylated intact Leishmania adsorbed by hemoglobin-agarose beads were subjected to SDS-polyacrylamide gel electrophoresis and Western blotting with avidin-horseradish peroxidase. Considered together, these data indicate that this 46-kDa protein on the cell surface of L. donovani promastigotes mediates the binding of hemoglobin and its rapid internalization through a vesicular pathway characteristic of receptor-mediated endocytosis. | lld:pubmed |
pubmed-article:9915807 | pubmed:language | eng | lld:pubmed |
pubmed-article:9915807 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9915807 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9915807 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9915807 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9915807 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9915807 | pubmed:month | Jan | lld:pubmed |
pubmed-article:9915807 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9915807 | pubmed:author | pubmed-author:BasuS KSK | lld:pubmed |
pubmed-article:9915807 | pubmed:author | pubmed-author:SenguptaSS | lld:pubmed |
pubmed-article:9915807 | pubmed:author | pubmed-author:TandonRR | lld:pubmed |
pubmed-article:9915807 | pubmed:author | pubmed-author:MukhopadhyayA... | lld:pubmed |
pubmed-article:9915807 | pubmed:author | pubmed-author:RoyR PRP | lld:pubmed |
pubmed-article:9915807 | pubmed:author | pubmed-author:RajaAA | lld:pubmed |
pubmed-article:9915807 | pubmed:author | pubmed-author:TripathiJJ | lld:pubmed |
pubmed-article:9915807 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9915807 | pubmed:day | 29 | lld:pubmed |
pubmed-article:9915807 | pubmed:volume | 274 | lld:pubmed |
pubmed-article:9915807 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9915807 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9915807 | pubmed:pagination | 2758-65 | lld:pubmed |
pubmed-article:9915807 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:meshHeading | pubmed-meshheading:9915807-... | lld:pubmed |
pubmed-article:9915807 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:9915807 | pubmed:articleTitle | Hemoglobin endocytosis in Leishmania is mediated through a 46-kDa protein located in the flagellar pocket. | lld:pubmed |
pubmed-article:9915807 | pubmed:affiliation | National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India. | lld:pubmed |
pubmed-article:9915807 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9915807 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9915807 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9915807 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9915807 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9915807 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9915807 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9915807 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9915807 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9915807 | lld:pubmed |