Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon

Autor: David M. Hudson, Marilyn Archer, David R. Eyre, MaryAnn Weis, Jyoti Rai, Russell J. Fernandes
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Histology
QH301-705.5
Lysine
Biophysics
LCL
lateral collateral ligament
P3H2
prolyl 3-hydroxylase 2
Connective tissue
QT
quadriceps tendon
Degeneration (medical)
Biochemistry
Hydroxylation
ACL
Anterior cruciate ligament
chemistry.chemical_compound
LP
lysine pyridinoline
Full Length Article
Genetics
medicine
Ligament
Biology (General)
Molecular Biology
Process (anatomy)
P3H1
prolyl 3-hydroxylase 1
Tendon
HP
hydroxylysine pyridinoline
Mass spectrometry
LC
liquid chromatography
Cell Biology
musculoskeletal system
HLNL
hydroxylysinonorleucine
Hydroxylysine
medicine.anatomical_structure
PCL
posterior cruciate ligament
MS
mass spectrometry
chemistry
HHMD
histidinohydroxymerodesmosine
Collagen
DHLNL
dehydrohydroxylysinonorleucine
HHL
histidinohydroxylysinonorleucine
MCL
medial collateral ligament
Type I collagen
Cross-linking
Post-translational modifications
Zdroj: Matrix Biology Plus, Vol 12, Iss, Pp 100070-(2021)
Matrix Biology Plus
ISSN: 2590-0285
Popis: Highlights • Tendon and ligament collagens differ in their post-translational lysine and cross-linking chemistry. • In ligament collagen, hydroxylysyl aldehyde, permanent cross-linking dominates. • Tendon collagen has a mix of cross-links based on lysyl and hydroxylysyl aldehydes. • The profile in tendon appears more adapted to facilitating growth, structural remodeling and repair of the fibrillar matrix.
Tendons and ligaments tend to be pooled into a single category as dense elastic bands of collagenous connective tissue. They do have many similar properties, for example both tissues are flexible cords of fibrous tissue that join bone to either muscle or bone. Tendons and ligaments are both prone to degenerate and rupture with only limited capacity to heal, although tendons tend to heal faster than ligaments. Type I collagen constitutes about 80% of the dry weight of tendons and ligaments and is principally responsible for the core strength of each tissue. Collagen synthesis is a complex process with multiple steps and numerous post-translational modifications including proline and lysine hydroxylation, hydroxylysine glycosylation and covalent cross-linking. The chemistry, placement and quantity of intramolecular and intermolecular cross-links are believed to be key contributors to the tissue-specific variations in material strength and biological properties of collagens. As tendons and ligaments grow and develop, the collagen cross-links are known to chemically mature, strengthen and change in profile. Accordingly, changes in cross-linking and other post-translational modifications are likely associated with tissue development and degeneration. Using mass spectrometry, we have compared tendon and ligaments from fetal and adult bovine knee joints to investigate changes in collagen post-translational properties. Although hydroxylation levels at the type I collagen helical cross-linking lysine residues were similar in all adult tissues, ligaments had significantly higher levels of glycosylation at these sites compared to tendon. Differences in lysine hydroxylation were also found between the tissues at the telopeptide cross-linking sites. Total collagen cross-linking analysis, including mature trivalent cross-links and immature divalent cross-links, revealed unique cross-linking profiles between tendon and ligament tissues. Tendons were found to have a significantly higher frequency of smaller diameter collagen fibrils compared with ligament, which we suspect is functionally associated with the unique cross-linking profile of each tissue. Understanding the specific molecular characteristics that define and distinguish these specialized tissues will be important to improving the design of orthopedic treatment approaches.
Databáze: OpenAIRE
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