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Quantitative Proteomic Analysis of Eight Cartilaginous Tissues Reveals Characteristic Differences as well as Similarities between Subgroups.

Önnerfjord, Patrik LU ; Khabut, Areej LU ; Reinholt, Finn P; Svensson, Olle and Heinegård, Dick LU (2012) In Journal of Biological Chemistry 287(23). p.18913-18924
Abstract
Human synovial joints display a characteristic anatomic distribution of arthritis e.g. rheumatoid arthritis primarily affects the metacarpophalangeal and proximal finger joints, but rarely the distal finger joints, while osteoarthritis occur in the distal and proximal finger joints. Pelvospondylitis has a selective localization to the spine and sacroiliac joints. Is this tropism due to differences between the cartilages at the molecular level? To substantiate this concept the present study provides a background detailed compositional analysis by relative quantification of extracellular matrix proteins in articular cartilages, meniscus, intervertebral disc, rib and tracheal cartilages on samples from 5-6 different individuals using an... (More)
Human synovial joints display a characteristic anatomic distribution of arthritis e.g. rheumatoid arthritis primarily affects the metacarpophalangeal and proximal finger joints, but rarely the distal finger joints, while osteoarthritis occur in the distal and proximal finger joints. Pelvospondylitis has a selective localization to the spine and sacroiliac joints. Is this tropism due to differences between the cartilages at the molecular level? To substantiate this concept the present study provides a background detailed compositional analysis by relative quantification of extracellular matrix proteins in articular cartilages, meniscus, intervertebral disc, rib and tracheal cartilages on samples from 5-6 different individuals using an optimized approach for proteomics. Tissue extraction followed by trypsin digestion and 2D LC-separations coupled to tandem mass spectrometry, relative quantification with isobaric labeling, iTRAQ, was used to compare the relative abundance of about 150 proteins. There were clear differences in protein patterns between different kinds of cartilages. Matrilin-1 and epiphycan were specific for rib and trachea, while asporin was particularly abundant in the meniscus. Interestingly, lubricin was prominent in the intervertebral disc, especially in the nucleus pulposus. Fibromodulin and lumican showed distributions that were mirror images of one other. Analyses of the insoluble residues from guanidine extraction revealed that a fraction of several proteins remained unextracted e.g. asporin, CILP and COMP indicating crosslinking. Distinct differences in protein patterns may relate to different tissue mechanical properties, and to the intriguing tropism in different patterns of joint pathology. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
287
issue
23
pages
18913 - 18924
publisher
ASBMB
external identifiers
  • wos:000306411900004
  • pmid:22493511
  • scopus:84861749409
ISSN
1083-351X
DOI
10.1074/jbc.M111.298968
language
English
LU publication?
yes
id
84eb070b-9dd5-4e89-bc7c-635c2b402115 (old id 2519602)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/22493511?dopt=Abstract
date added to LUP
2012-05-06 14:52:49
date last changed
2017-10-22 03:21:05
@article{84eb070b-9dd5-4e89-bc7c-635c2b402115,
  abstract     = {Human synovial joints display a characteristic anatomic distribution of arthritis e.g. rheumatoid arthritis primarily affects the metacarpophalangeal and proximal finger joints, but rarely the distal finger joints, while osteoarthritis occur in the distal and proximal finger joints. Pelvospondylitis has a selective localization to the spine and sacroiliac joints. Is this tropism due to differences between the cartilages at the molecular level? To substantiate this concept the present study provides a background detailed compositional analysis by relative quantification of extracellular matrix proteins in articular cartilages, meniscus, intervertebral disc, rib and tracheal cartilages on samples from 5-6 different individuals using an optimized approach for proteomics. Tissue extraction followed by trypsin digestion and 2D LC-separations coupled to tandem mass spectrometry, relative quantification with isobaric labeling, iTRAQ, was used to compare the relative abundance of about 150 proteins. There were clear differences in protein patterns between different kinds of cartilages. Matrilin-1 and epiphycan were specific for rib and trachea, while asporin was particularly abundant in the meniscus. Interestingly, lubricin was prominent in the intervertebral disc, especially in the nucleus pulposus. Fibromodulin and lumican showed distributions that were mirror images of one other. Analyses of the insoluble residues from guanidine extraction revealed that a fraction of several proteins remained unextracted e.g. asporin, CILP and COMP indicating crosslinking. Distinct differences in protein patterns may relate to different tissue mechanical properties, and to the intriguing tropism in different patterns of joint pathology.},
  author       = {Önnerfjord, Patrik and Khabut, Areej and Reinholt, Finn P and Svensson, Olle and Heinegård, Dick},
  issn         = {1083-351X},
  language     = {eng},
  number       = {23},
  pages        = {18913--18924},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Quantitative Proteomic Analysis of Eight Cartilaginous Tissues Reveals Characteristic Differences as well as Similarities between Subgroups.},
  url          = {http://dx.doi.org/10.1074/jbc.M111.298968},
  volume       = {287},
  year         = {2012},
}