Proteomic characterization of the normal human medial meniscus body using data-independent acquisition mass spectrometry
Folkesson, Elin LU ; Turkiewicz, Aleksandra LU ; Rydén, Martin LU
; Hughes, Harini Velocity
LU
; Ali, Neserin
LU
; Tjörnstrand, Jon
LU
; Önnerfjord, Patrik
LU
and Englund, Martin
LU
(2020)
In Journal of Orthopaedic Research
38(8).
p.1735-1745
- Abstract
Recent research suggests an important role of the meniscus in the development of knee osteoarthritis. We, therefore, aimed to analyze the proteome of the normal human meniscus body, and specifically to gain new knowledge on global protein expression in the different radial zones. Medial menisci were retrieved from the right knees of 10 human cadaveric donors, from which we cut a 2 mm radial slice from the mid-portion of the meniscal body. This slice was further divided into three zones: inner, middle, and peripheral. Proteins were extracted and prepared for mass spectrometric analysis using data-independent acquisition. We performed subsequent data searches using Spectronaut Pulsar and used fixed-effect linear regression models for... (More)
Recent research suggests an important role of the meniscus in the development of knee osteoarthritis. We, therefore, aimed to analyze the proteome of the normal human meniscus body, and specifically to gain new knowledge on global protein expression in the different radial zones. Medial menisci were retrieved from the right knees of 10 human cadaveric donors, from which we cut a 2 mm radial slice from the mid-portion of the meniscal body. This slice was further divided into three zones: inner, middle, and peripheral. Proteins were extracted and prepared for mass spectrometric analysis using data-independent acquisition. We performed subsequent data searches using Spectronaut Pulsar and used fixed-effect linear regression models for statistical analysis. We identified 638 proteins and after statistical analysis, we observed the greatest number of differentially expressed proteins between the inner and peripheral zones (163 proteins) and the peripheral and middle zones (136 proteins), with myocilin being the protein with the largest fold-change in both comparisons. Chondroadherin was one of eight proteins that differed between the inner and middle zones. Functional enrichment analyses showed that the peripheral one-third of the medial meniscus body differed substantially from the two more centrally located zones, which were more similar to each other. This is probably related to the higher content of cells and vascularization in the peripheral zone, whereas the middle and inner zones of the meniscal body appear to be more similar to hyaline cartilage, with high levels of extracellular matrix proteins such as aggrecan and collagen type II.
(Less)
- author
- Folkesson, Elin
LU
; Turkiewicz, Aleksandra
LU
; Rydén, Martin
LU
; Hughes, Harini Velocity
LU
; Ali, Neserin
LU
; Tjörnstrand, Jon
LU
; Önnerfjord, Patrik
LU
and Englund, Martin
LU
- organization
- publishing date
- 2020-08
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- data-independent acquisition, meniscus, proteomics
- in
- Journal of Orthopaedic Research
- volume
- 38
- issue
- 8
- pages
- 11 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:85078850544
- pmid:31989678
- ISSN
- 0736-0266
- DOI
- 10.1002/jor.24602
- language
- English
- LU publication?
- yes
- id
- 02550121-4aeb-4a80-a549-b2c6f88117c4
- date added to LUP
- 2020-02-13 16:16:27
- date last changed
- 2024-05-01 05:05:23
@article{02550121-4aeb-4a80-a549-b2c6f88117c4,
abstract = {{<p>Recent research suggests an important role of the meniscus in the development of knee osteoarthritis. We, therefore, aimed to analyze the proteome of the normal human meniscus body, and specifically to gain new knowledge on global protein expression in the different radial zones. Medial menisci were retrieved from the right knees of 10 human cadaveric donors, from which we cut a 2 mm radial slice from the mid-portion of the meniscal body. This slice was further divided into three zones: inner, middle, and peripheral. Proteins were extracted and prepared for mass spectrometric analysis using data-independent acquisition. We performed subsequent data searches using Spectronaut Pulsar and used fixed-effect linear regression models for statistical analysis. We identified 638 proteins and after statistical analysis, we observed the greatest number of differentially expressed proteins between the inner and peripheral zones (163 proteins) and the peripheral and middle zones (136 proteins), with myocilin being the protein with the largest fold-change in both comparisons. Chondroadherin was one of eight proteins that differed between the inner and middle zones. Functional enrichment analyses showed that the peripheral one-third of the medial meniscus body differed substantially from the two more centrally located zones, which were more similar to each other. This is probably related to the higher content of cells and vascularization in the peripheral zone, whereas the middle and inner zones of the meniscal body appear to be more similar to hyaline cartilage, with high levels of extracellular matrix proteins such as aggrecan and collagen type II.</p>}},
author = {{Folkesson, Elin and Turkiewicz, Aleksandra and Rydén, Martin and Hughes, Harini Velocity and Ali, Neserin and Tjörnstrand, Jon and Önnerfjord, Patrik and Englund, Martin}},
issn = {{0736-0266}},
keywords = {{data-independent acquisition; meniscus; proteomics}},
language = {{eng}},
number = {{8}},
pages = {{1735--1745}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Orthopaedic Research}},
title = {{Proteomic characterization of the normal human medial meniscus body using data-independent acquisition mass spectrometry}},
url = {{http://dx.doi.org/10.1002/jor.24602}},
doi = {{10.1002/jor.24602}},
volume = {{38}},
year = {{2020}},
}