Linked Life Data

10551365

Source:http://linkedlifedata.com/resource/pubmed/id/10551365

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-12-23
pubmed:databankReference
pubmed:abstractText
Pure populations of early and late endosomes of Entamoeba histolytica were isolated by magnetic fractionation and characterized. It was shown that these vesicles were enriched in acid phosphatase and cysteine protease activities. An important virulence factor, a 27-kDa cysteine protease, was also enriched in early and late endosomes of E. histolytica. These data suggest that E. histolytica hydrolases reside in compartments that are part of or communicate with the endosomal pathway. To begin to identify the role of Rab GTPases in E. histolytica, an oligonucleotide approach was employed to screen an E. histolytica cDNA library for genes encoding Rab-like proteins. cDNAs encoding a Rab11-like protein (EhRab11) and a novel Rab protein (EhRabA) were isolated and characterized. The EhRab11 cDNA predicts a polypeptide of at least 206 amino acids with a molecular mass of at least 23.2 kDa. Phylogenetic analysis and alignment of EhRab11 with other Rab proteins demonstrated that EhRab11 shared significant homology at the amino acid level with Rab11-like proteins from a number of other eukaryotes, suggesting that EhRab11 is a Rab11 homolog for E. histolytica. The EhRabA clone predicts a polypeptide of 219 amino acids with a molecular mass of at least 24.5 kDa. EhRabA shared only limited homology at the amino acid level with other Rab proteins, suggesting that it is a novel member of this family of GTP-binding proteins. Finally, Western blot analysis demonstrated that EhRab11 and a previously described Rab7-like GTPase from E. histolytica was enriched in magnetically purified endosomal compartments of this organism.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
225-41
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10551365-Acid Phosphatase, pubmed-meshheading:10551365-Amino Acid Sequence, pubmed-meshheading:10551365-Animals, pubmed-meshheading:10551365-Base Sequence, pubmed-meshheading:10551365-Cell Fractionation, pubmed-meshheading:10551365-Cloning, Molecular, pubmed-meshheading:10551365-Conserved Sequence, pubmed-meshheading:10551365-Cysteine Endopeptidases, pubmed-meshheading:10551365-DNA, Complementary, pubmed-meshheading:10551365-Endosomes, pubmed-meshheading:10551365-Entamoeba histolytica, pubmed-meshheading:10551365-Iron, pubmed-meshheading:10551365-Magnetics, pubmed-meshheading:10551365-Molecular Sequence Data, pubmed-meshheading:10551365-Phylogeny, pubmed-meshheading:10551365-Pinocytosis, pubmed-meshheading:10551365-Sequence Analysis, DNA, pubmed-meshheading:10551365-Sequence Homology, Amino Acid, pubmed-meshheading:10551365-rab GTP-Binding Proteins, pubmed-meshheading:10551365-ras Proteins
pubmed:year
1999
pubmed:articleTitle
Early and late endosomal compartments of Entamoeba histolytica are enriched in cysteine proteases, acid phosphatase and several Ras-related Rab GTPases.
pubmed:affiliation
Feist-Weiller Cancer Center, Shreveport, LA 71130, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't