Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-9-29
pubmed:abstractText
Protein glycation may play a role in the pathogenesis of diabetic complications. alpha-Lipoate (1,2-dithiolane-3-pentanoate) has been reported to prevent glycation and structural modification of bovine serum albumin (BSA). To elucidate the protective mechanism, we tested the effects of enantiomerism, thiol moiety and hydrophobicity of alpha-lipoate on glycation of BSA and low density lipoprotein (LDL). When BSA (1 mM) was incubated with 500 mM glucose in the presence of alpha-lipoate homologues or dihydrolipoate (6,8-dimercaptooctanoate, DHLA) at 37 degrees C for 72 h, both alpha-lipoate (racemic, R- and S-forms) and DHLA inhibited BSA glycation similarly, but tetranorlipoate (1,2-dithiolane-3-carboxylate) did not. However, under similar conditions, alpha-lipoate did not inhibit LDL glycation. Scatchard plot analysis demonstrated that 6 mol of alpha-lipoate bind to 1 mol of BSA with a formation constant of 8.7 x 10(4) M-1. Therefore, we concluded that alpha-lipoate protects BSA glycation by hydrophobic binding near the glycation sites of BSA.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
203
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-104
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Alpha-lipoate can protect against glycation of serum albumin, but not low density lipoprotein.
pubmed:affiliation
Department of Molecular & Cell Biology, University of California, Berkeley 94720-3200.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't