Age- and position-related heterogeneity of equine tendon extracellular matrix composition.
Abstract: The digital flexor tendons of the neonate and adult horse have been compared with respect to variation in extracellular matrix composition along their length. Two pepsin-sensitive, acetic acid soluble proteins, molecular weight (Mr) 52 kD (np 52) and Mr 54 kD (np 54), were prominent throughout the length of neonatal tendons. In adult tendon, np 52 and np 54 were less abundant and restricted to the cannon (metacarpal) region. In contrast, a single pepsin- and collagenase-resistant protein of Mr 55 kD (fp 55) was exclusive to the fetlock (metacarpophalangeal joint) region regardless of age, although more distinct in the adult. Pepsin extracted fp 55 precipitated at 2.0 M sodium chloride: 0.5 M acetic acid and was further purified to homogeneity by bacterial collagenase digestion. Analysis of fp 55 amino acid composition revealed the presence of a large proportion of glycine residues (379 of 1001), suggesting a possible homology with the collagen family. These data demonstrate that the composition of equine digital flexor tendons varies with age, is heterogeneous along its length, and suggests that variation in tendon extracellular matrix composition is influenced by functional requirements.
Publication Date: 1990-05-01 PubMed ID: 2113705
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article investigates how the composition of equine (horse) tendon extracellular matrix varies with age and anatomical position. It highlights that these variations could be linked to tendon’s functional needs.
Research Objective
- The researchers aimed to explore the composition of the digital flexor tendons of horses, with a focus on possible differences based on the tendon’s age and location in the body.
Methods and Findings
- The study compared two types of proteins (np 52 and np 54) present in the tendons of neonate and adult horses. These proteins were abundant throughout the neonatal tendons but were less common and confined to the metacarpal/cannon region in the adult tendons.
- In contrast, a different protein (fp 55) was found exclusively in the fetlock (metacarpophalangeal joint) region, regardless of the horse’s age. This protein was more prominent in adult horses.
- The research team made use of pepsin to extract fp 55, which was found to precipitate under specific conditions of sodium chloride and acetic acid. This extraction was purified further using bacterial collagenase digestion.
- The composition analysis of this protein revealed a high proportion of glycine residues, suggesting a possible relationship with the collagen family of proteins.
Conclusion
- The findings indicated that the composition of the equine digital flexor tendons changes with age and also varies along its length.
- This variability in tendon extracellular matrix composition could be a result of the tendon’s functional requirements, reflecting the environmental pressures and expectations from the tendon at various stages of the horse’s life and different regions of the body.
Cite This Article
APA
Jones AJ, Bee JA.
(1990).
Age- and position-related heterogeneity of equine tendon extracellular matrix composition.
Res Vet Sci, 48(3), 357-364.
Publication
Researcher Affiliations
- Department of Veterinary Medicine and Animal Husbandry, Royal Veterinary College, North Mymms, Hatfield, Hertfordshire.
MeSH Terms
- Acetates
- Acetic Acid
- Aging
- Amino Acids / analysis
- Animals
- Animals, Newborn
- Extracellular Matrix / analysis
- Horses / anatomy & histology
- Pepsin A / metabolism
- Proteins / analysis
- Solubility
- Tendons / analysis
Citations
This article has been cited 3 times.- Shen Y, Cai J. The Importance of Using Exosome-Loaded miRNA for the Treatment of Spinal Cord Injury.. Mol Neurobiol 2023 Feb;60(2):447-459.
- Wagner FC, Reese S, Gerlach K, Böttcher P, Mülling CKW. Cyclic tensile tests of Shetland pony superficial digital flexor tendons (SDFTs) with an optimized cryo-clamp combined with biplanar high-speed fluoroscopy.. BMC Vet Res 2021 Jun 25;17(1):223.
- Södersten F, Hultenby K, Heinegård D, Johnston C, Ekman S. Immunolocalization of collagens (I and III) and cartilage oligomeric matrix protein in the normal and injured equine superficial digital flexor tendon.. Connect Tissue Res 2013;54(1):62-9.
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