Linked Life Data

12799065

Source:http://linkedlifedata.com/resource/pubmed/id/12799065

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-6-11
pubmed:abstractText
We found a dipeptidyl aminopeptidase activity in the parasitic protozoan Giardia lamblia with properties similar to the lysosomal cathepsin C of rat-liver lysosomes. Subcellular fractionation of this parasite indicated that the cathepsin C activity is located in organelles not distinguishable from the ones containing acid phosphatase, a known marker enzyme of Giardia lysosome-like peripheral vesicles. Contrary to the rat lysosomal enzyme, Giardia cathepsin C behaved like a membrane protein. Moreover, the enzyme was not solubilized by Triton X-100 or Triton X-100/SDS at 0 degrees C but could be substantially solubilized by octylglucoside, Triton X-100 at 37 degrees C or by a pretreatment with the cholesterol complexing agent beta-cyclodextrin before the Triton/SDS treatment carried out at 0 degrees C. These observations suggest that binding/anchorage of this enzyme to membranes occurs in cholesterol-rich microdomains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0248-4900
pubmed:author
pubmed:issnType
Print
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-105
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:articleTitle
The acid phosphatase positive organelles of the Giardia lamblia trophozoite contain a membrane bound cathepsin C activity.
pubmed:affiliation
Department of Physiological Chemistry, University of Namur (FUNDP), 61, rue de Bruxelles, B-5000, Namur, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't