Linked Life Data

2470544

Source:http://linkedlifedata.com/resource/pubmed/id/2470544

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1989-6-30
pubmed:abstractText
1. Protein constituents were determined in eight amyloid deposits from eight patients (five male and three female), 53 +/- 4 years of age, treated by haemodialysis for 9-20 years using only cuprophane membranes and operated for carpal tunnel syndrome. 2. Soluble proteins were removed by solubilization in phosphate-buffered saline after osmotic lysis. The proteins of the insoluble fibrils were characterized by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and two-dimensional gel electrophoresis, and immunologically identified by Western blotting. 3. In addition to beta 2-microglobulin, alpha 2-macroglobulin was identified in the fibrillar material. The presence of these two proteins in amyloid deposits was confirmed by immunofluorescent microscopic studies. 4. Our data confirm the presence of beta 2-microglobulin in haemodialysis-associated amyloidosis, and also suggest a possible role for alpha 2-microglobulin: it may protect beta 2-microglobulin from proteolytic digestion, leading to its accumulation in intact form and to amyloid fibril formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0143-5221
pubmed:author
pubmed:issnType
Print
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
547-52
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
High-molecular-mass proteins in haemodialysis-associated amyloidosis.
pubmed:affiliation
INSERM Unit 249, Centre de Recherche Biochimie Macromoléculaire, CNRS, Montpellier, France.
pubmed:publicationType
Journal Article