Linked Life Data

7986814

Source:http://linkedlifedata.com/resource/pubmed/id/7986814

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-1-12
pubmed:abstractText
Human erythrocytes were oxidized with xanthine/xanthine oxidase/ferric ion or ADP/ferric ion at 37 degrees C for several hours. Band 3 protein and spectrin of the oxidized cells were found to be significantly modified as analyzed by radiolabeling with tritiated borohydride. Sodium dodecylsulfate-polyacrylamide gel electrophoresis of the xanthine/xanthine oxidase/ferric iron-oxidized cells and subsequent immunoblotting with anti band 3 protein showed that band 3 protein was fragmented into smaller molecular-weight fragments. When the cell membrane obtained from the oxidized cells were incubated at pH 7.4 and 37 degrees C for several hours in the presence of alpha-tocopherol, extensive degradation of band 3 protein and spectrin was observed. Band 3 protein was found to be most susceptible to the degradation. Degradation of band 3 protein was also observed after similar incubation of the membrane from the ADP/ferric ion-oxidized cells. Membrane-bound serine- and metalloproteinases were responsible for the degradation of band 3 protein, because the degradation was remarkably inhibited by diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride, and partially by ethylenediaminetetraacetic acid. Hence, the membrane proteins became susceptible to membrane-bound proteinases by oxidative stress. This observation suggests that these membrane-bound proteinases exist to remove oxidatively damaged proteins from the cell membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
1196
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
81-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Presence of membrane-bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary antioxidant defense.
pubmed:affiliation
Tokyo College of Pharmacy, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't