Linked Life Data

2215357

Source:http://linkedlifedata.com/resource/pubmed/id/2215357

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-11-8
pubmed:abstractText
Collagen composition and cross-linking in human keloid and normal skin tissues were analyzed biochemically. CNBr peptides were separated by 2-dimensional (2-D) mapping and high performance liquid chromatography (HPLC). The amounts of type I and type III collagen was quantified by 2-D scanning densitometry of fluorographs of 2-D maps derived from samples radioactively labelled in vitro by [3H]-NaBH4 in dimethylformamide. Keloid tissues contained 31.6 +/- 2.2 percent type III collagen as compared to 21.4 +/- 2.7 percent type III present in normal human skin dermis. HPLC profiles of CNBr peptides showed that approximately 5 percent of the high molecular weight material in keloids is mercaptoethanol reducible, compared to insignificant amounts in normal skin. 2-D maps derived from CNBr peptides of keloid collagen demonstrated thiol reduction sensitive alpha 1(III)-CB9 dimer as well as 24,000- and 32,000-dalton CNBr peptides, which were not mercaptoethanol reduction sensitive in normal skin due to cross-linking via the lysyl oxidase pathway. Also, a group of 20,000- to 25,000-dalton CNBr peptides, in the alpha 1(I)-CB6 cross-linking region were prominent in keloid tissues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0934-8832
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
172-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Alteration of collagen composition and cross-linking in keloid tissues.
pubmed:affiliation
Orthopedic Hospital, Los Angeles, CA 90007.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.