Altered patterns and synthesis of extracellular matrix macromolecules in early osteoarthritis.
(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:
https://lup.lub.lu.se/record/130924
- author
- Lorenzo, Pilar LU ; Bayliss, Michael T and Heinegård, Dick LU
- organization
- publishing date
- 2004
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151)
- 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
- 2016-04-01 15:51:09
- date last changed
- 2022-04-22 17:54:38
@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}},
keywords = {{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}},
doi = {{10.1016/j.matbio.2004.07.007}},
volume = {{23}},
year = {{2004}},
}