Advanced

Altered patterns and synthesis of extracellular matrix macromolecules in early osteoarthritis.

Lorenzo, Pilar LU ; Bayliss, Michael T and Heinegård, Dick LU (2004) In Matrix Biology 23(6). p.381-391
Abstract
The synthesis and contents of extracellular non-collagenous matrix macromolecules was studied in early and late human osteoarthritic (OA) cartilage obtained at surgery for sarcomas in the lower extremities (normal and early OA) or for total knee replacement (late stage OA). The early OA samples were those that had some fibrillation in the joint by visual examination. One group had fibrillation in the area sampled and the other group had no fibrillation. Cartilage was taken from the same topographical area on the medial femoral condyle in all the samples, labeled with [3H]leucine and [35S]sulfate for 4 h at 37 °C and extracted with 4 M guanidine–HCl. Analysis of the extracts showed that the total amount of proteoglycans relative to... (More)
The synthesis and contents of extracellular non-collagenous matrix macromolecules was studied in early and late human osteoarthritic (OA) cartilage obtained at surgery for sarcomas in the lower extremities (normal and early OA) or for total knee replacement (late stage OA). The early OA samples were those that had some fibrillation in the joint by visual examination. One group had fibrillation in the area sampled and the other group had no fibrillation. Cartilage was taken from the same topographical area on the medial femoral condyle in all the samples, labeled with [3H]leucine and [35S]sulfate for 4 h at 37 °C and extracted with 4 M guanidine–HCl. Analysis of the extracts showed that the total amount of proteoglycans relative to hydroxyproline content was higher in the early and late OA than in the normal cartilage. These proteoglycans showed a relatively lower [35S]sulfate incorporation into GAG chains and a higher [3H]leucine incorporation. The pattern of newly synthesized proteins was altered similarly in early and late OA. Notably, synthesis of cartilage oligomeric matrix protein (COMP), fibronectin, and cartilage intermediate layer protein (CILP) was increased, also reflected in their abundance as determined by enzyme-linked immunosorbent assay (ELISA). Collagen synthesis appeared significantly increased only in the late stage OA. The observed altered composition and pattern of biosynthesis indicate that the joint undergoes metabolic alterations early in the disease process, even before there is overt fibrillation of the tissue. The early OA samples studied appear to represent two distinct groups of early lesions in different stages of the process of cartilage deterioration as shown by their differences in relative rates of synthesis and abundance of proteins. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Osteoarthritis, Proteoglycan, Matrix proteins
in
Matrix Biology
volume
23
issue
6
pages
381 - 391
publisher
Elsevier
external identifiers
  • pmid:15533759
  • wos:000225383400007
  • scopus:7944226150
ISSN
1569-1802
DOI
10.1016/j.matbio.2004.07.007
language
English
LU publication?
yes
id
df9a30f6-5b2c-4ba7-85e3-0229b380f60c (old id 130924)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15533759&dopt=Abstract
date added to LUP
2007-07-17 09:51:57
date last changed
2017-12-10 04:28:10
@article{df9a30f6-5b2c-4ba7-85e3-0229b380f60c,
  abstract     = {The synthesis and contents of extracellular non-collagenous matrix macromolecules was studied in early and late human osteoarthritic (OA) cartilage obtained at surgery for sarcomas in the lower extremities (normal and early OA) or for total knee replacement (late stage OA). The early OA samples were those that had some fibrillation in the joint by visual examination. One group had fibrillation in the area sampled and the other group had no fibrillation. Cartilage was taken from the same topographical area on the medial femoral condyle in all the samples, labeled with [3H]leucine and [35S]sulfate for 4 h at 37 °C and extracted with 4 M guanidine–HCl. Analysis of the extracts showed that the total amount of proteoglycans relative to hydroxyproline content was higher in the early and late OA than in the normal cartilage. These proteoglycans showed a relatively lower [35S]sulfate incorporation into GAG chains and a higher [3H]leucine incorporation. The pattern of newly synthesized proteins was altered similarly in early and late OA. Notably, synthesis of cartilage oligomeric matrix protein (COMP), fibronectin, and cartilage intermediate layer protein (CILP) was increased, also reflected in their abundance as determined by enzyme-linked immunosorbent assay (ELISA). Collagen synthesis appeared significantly increased only in the late stage OA. The observed altered composition and pattern of biosynthesis indicate that the joint undergoes metabolic alterations early in the disease process, even before there is overt fibrillation of the tissue. The early OA samples studied appear to represent two distinct groups of early lesions in different stages of the process of cartilage deterioration as shown by their differences in relative rates of synthesis and abundance of proteins.},
  author       = {Lorenzo, Pilar and Bayliss, Michael T and Heinegård, Dick},
  issn         = {1569-1802},
  keyword      = {Osteoarthritis,Proteoglycan,Matrix proteins},
  language     = {eng},
  number       = {6},
  pages        = {381--391},
  publisher    = {Elsevier},
  series       = {Matrix Biology},
  title        = {Altered patterns and synthesis of extracellular matrix macromolecules in early osteoarthritis.},
  url          = {http://dx.doi.org/10.1016/j.matbio.2004.07.007},
  volume       = {23},
  year         = {2004},
}