» Articles » PMID: 6733772

Morphometric Analysis of Loading-induced Changes in Collagen-fibril Populations in Young Tendons

Overview
Journal Cell Tissue Res
Date 1984 Jan 1
PMID 6733772
Citations 28
Authors
Affiliations
Soon will be listed here.
Abstract

This study was designed to gain more detailed morphological information on skeletal tendons in the course of adaptation to physical loading. The effect on collagen fibrils was investigated in 6-week-old mice by means of electron microscopy. Physical loading was performed on a treadmill 5 days a week for 1, 3, 5, 7 and 10 weeks. Morphometric analysis of collagen fibrils revealed the mean diameter, the diameter distribution, the number and the cross-sectional area. The principal observations included: 1. After one week of physical loading an increase in mean fibril diameter (30%, p less than or equal to 0.01), in number (15%, p less than or equal to 0.05), and in cross-sectional area (15%, p less than or equal to 0.05), as well as a change in mean fibril diameter distribution. 2. From the third to the seventh week a fall under the level of the controls in mean diameter (26%, p less than or equal to 0.01), in number (26%, p less than or equal to 0.01), and a reduced cross-sectional area (17%, p less than or equal to 0.01), accompanied by signs of splitting of individual collagen fibrils. 3. In the long-term study an increase in fibril number (29%, p less than or equal to 0.01), a fall in mean diameter from 189 nm in the controls to 179 nm (p less than or equal to 0.05) but no statistically significant change in the relative cross-sectional area (32%) per unit in comparison to unloaded tendons. The possible physiological implications of the findings are discussed in the light of several regulatory mechanisms known to appear during the course of physical loading in connective tissues.

Citing Articles

Neural network auto-segmentation of serial-block-face scanning electron microscopy images exhibit collagen fibril structural differences with tendon type and health.

Bloom E, Sabanayagam C, Benson J, Lin L, Ross J, Caplan J J Orthop Res. 2024; 43(1):5-13.

PMID: 39180281 PMC: 11756596. DOI: 10.1002/jor.25961.


Overload in a Rat In Vivo Model of Synergist Ablation Induces Tendon Multiscale Structural and Functional Degeneration.

Bloom E, Lin L, Locke R, Giordani A, Krassan E, Peloquin J J Biomech Eng. 2023; 145(8).

PMID: 37184932 PMC: 10782872. DOI: 10.1115/1.4062523.


Tendon Extracellular Matrix Assembly, Maintenance and Dysregulation Throughout Life.

Siadat S, Zamboulis D, Thorpe C, Ruberti J, Connizzo B Adv Exp Med Biol. 2021; 1348:45-103.

PMID: 34807415 DOI: 10.1007/978-3-030-80614-9_3.


Tendinopathy and tendon material response to load: What we can learn from small animal studies.

Williamson P, Freedman B, Kwok N, Beeram I, Pennings J, Johnson J Acta Biomater. 2021; 134:43-56.

PMID: 34325074 PMC: 8542586. DOI: 10.1016/j.actbio.2021.07.046.


Measuring collagen fibril diameter with differential interference contrast microscopy.

Siadat S, Silverman A, DiMarzio C, Ruberti J J Struct Biol. 2021; 213(1):107697.

PMID: 33545351 PMC: 8754585. DOI: 10.1016/j.jsb.2021.107697.


References
1.
Parry D, Craig A, Barnes G . Tendon and ligament from the horse: an ultrastructural study of collagen fibrils and elastic fibres as a function of age. Proc R Soc Lond B Biol Sci. 1978; 203(1152):293-303. DOI: 10.1098/rspb.1978.0106. View

2.
Roth S, Freund I . Optical second-harmonic scattering in rat-tail tendon. Biopolymers. 1981; 20(6):1271-90. DOI: 10.1002/bip.1981.360200613. View

3.
Parry D, FLINT M, Gillard G, Craig A . A role for glycosaminoglycans in the development of collagen fibrils. FEBS Lett. 1982; 149(1):1-7. DOI: 10.1016/0014-5793(82)81060-0. View

4.
Byrd R . The effect of controlled, mild exercise on the rate of physiological ageing of rats. J Sports Med Phys Fitness. 1973; 13(1):1-3. View

5.
Light N, Bailey A . Changes in crosslinking during aging in bovine tendon collagen. FEBS Lett. 1979; 97(1):183-8. DOI: 10.1016/0014-5793(79)80080-0. View