Linked Life Data

17113085

Source:http://linkedlifedata.com/resource/pubmed/id/17113085

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28-29
pubmed:dateCreated
2006-12-4
pubmed:abstractText
Flotillin-1 and arginase are both up-regulated in red blood cell membrane of type 2 diabetic patients. For studying why the soluble arginase can bind to the membrane and whether such binding would modify arginase activity, the arginase1 and related proteins were cloned and expressed. The results showed that flotillin-1 can interact with arginase1, and hence arginase activity was up-regulated by 26.8%. It was estimated that about 61% of arginase1 is bound to the membrane mediated by flotillin-1. The arginase activity in diabetic patients was significantly higher than that of the controls (752.4+/-38.5 U/mg protein vs 486.7+/-28.7 U/mg protein).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
580
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6561-4
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Arginase-flotillin interaction brings arginase to red blood cell membrane.
pubmed:affiliation
Department of Physiology and Biophysics, School of Life Sciences, Fudan University, Shanghai 200433, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't