Quantitative Proteomic Analysis of Eight Cartilaginous Tissues Reveals Characteristic Differences as well as Similarities between Subgroups.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2519602
- author
- Önnerfjord, Patrik LU ; Khabut, Areej LU ; Reinholt, Finn P ; Svensson, Olle and Heinegård, Dick LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 287
- issue
- 23
- pages
- 18913 - 18924
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000306411900004
- pmid:22493511
- scopus:84861749409
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M111.298968
- 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
- 84eb070b-9dd5-4e89-bc7c-635c2b402115 (old id 2519602)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/22493511?dopt=Abstract
- date added to LUP
- 2016-04-01 10:41:51
- date last changed
- 2022-04-28 00:22:18
@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 = {{American Society for Biochemistry and Molecular Biology}}, 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}}, doi = {{10.1074/jbc.M111.298968}}, volume = {{287}}, year = {{2012}}, }