Linked Life Data

18164932

Source:http://linkedlifedata.com/resource/pubmed/id/18164932

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-3-17
pubmed:abstractText
Dialysis related amyloidosis (DRA) is a progressive and serious complication in patients under long-term hemodialysis and mainly leads to osteo-articular diseases. Although beta(2)-microglobulin (beta2-m) is the major structural component of beta2-m amyloid fibrils, the initiation of amyloid formation is not clearly understood. Here, we have identified procollagen C-proteinase enhancer-1 (PCPE-1) as a new interacting protein with beta2-m by screening a human synovium cDNA library. The interaction of beta2-m with full-length PCPE-1 was confirmed by immunoprecipitation, solid-phase binding and pull-down assays. By yeast two-hybrid analysis and pull-down assay, beta2-m appeared to interact with PCPE-1 via the NTR (netrin-like) domain and not via the CUB (C1r/C1s, Uegf and BMP-1) domain region. In synovial tissues derived from hemodialysis patients with DRA, beta2-m co-localized and formed a complex with PCPE-1. beta2-m did not alter the basal activity of bone morphogenetic protein-1/procollagen C-proteinase (BMP-1/PCP) nor BMP-1/PCP activity enhanced by PCPE-1. PCPE-1 did not stimulate beta2-m amyloid fibril formation from monomeric beta2-m in vitro under acidic and neutral conditions as revealed by thioflavin T fluorescence spectroscopy and electron microscopy. Since PCPE-1 is abundantly expressed in connective tissues rich in type I collagen, it may be involved in the initial accumulation of beta2-m in selected tissues such as tendon, synovium and bone. Furthermore, since such preferential deposition of beta2-m may be linked to subsequent beta2-m amyloid fibril formation, the disruption of the interaction between beta2-m and PCPE-1 may prevent beta2-m amyloid fibril formation and therefore PCPE-1 could be a new target for the treatment of DRA.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0945-053X
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
211-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:18164932-Amino Acid Sequence, pubmed-meshheading:18164932-Amyloid, pubmed-meshheading:18164932-Bone Morphogenetic Protein 1, pubmed-meshheading:18164932-Bone Morphogenetic Proteins, pubmed-meshheading:18164932-Dose-Response Relationship, Drug, pubmed-meshheading:18164932-Enhancer Elements, Genetic, pubmed-meshheading:18164932-Extracellular Matrix Proteins, pubmed-meshheading:18164932-Gene Library, pubmed-meshheading:18164932-Glycoproteins, pubmed-meshheading:18164932-Humans, pubmed-meshheading:18164932-Metalloendopeptidases, pubmed-meshheading:18164932-Molecular Sequence Data, pubmed-meshheading:18164932-Protein Binding, pubmed-meshheading:18164932-Protein Structure, Tertiary, pubmed-meshheading:18164932-Recombinant Proteins, pubmed-meshheading:18164932-Two-Hybrid System Techniques, pubmed-meshheading:18164932-beta 2-Microglobulin
pubmed:year
2008
pubmed:articleTitle
Procollagen C-proteinase enhancer-1 (PCPE-1) interacts with beta2-microglobulin (beta2-m) and may help initiate beta2-m amyloid fibril formation in connective tissues.
pubmed:affiliation
Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Okayama 700-8558, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural