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This study tried to compare the morphological changes of collagen fibrils between disused and denervated old rat Achilles tendons with those of young rats through quantitative analyses of collagen fibril diameters by transmission electron microscopy (TEM).
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Objective:
The study aimed to assess tendon thickness in patients with chronic occupational lead exposure by using ultrasonography.
Methods:
Twenty-seven male workers (mean age 32.9 ± 6.2 years, range 25-44 years) with occupational lead exposure and 27 age- and body mass index (BMI)-matched healthy male subjects (mean age 33.1 ± 5.6 years, range...
Citations
... This is in line with the findings of Andrzej., et al, 1994 and In-Sik Lee, 2018, who concluded that, the fibrils formed with extracted collagen under physiological conditions tended to narrow and irregular in diameter, and that they lacked the tightly structured appearance of fibrils in sittu. [24] Therefore, the observed pattern of the continuous increase in the length of fibrils formed from the collagen of animals with ageing was the result of age-related characteristic features of processing, and consequently, the nature of cross-linking. [20,17] The preferential formation of intermolecular crosslinks that bind molecules in fibrils, beginning with the end, in adult and aged animals was the reason behind the increase in diameter of fibrils formed from the collagen of these animals, which was less than the increase in their length. ...
... Obtained results could be explained thus, type I collagen molecule is a rigid rod-shaped triple helix of polypeptide chains with a diameter and a length of about 0.15 and 300nm, respectively. [24,26,27] The biological role or significance of the direction of age-related changes in the self-assembling of fibrils from the skin collagen of young animals lies in the fact that, during this period of development, after a slowdown in growth of the feotus before birth (in early postnatal ontogenesis) during the period up to three (3) months, there is a rapid growth of the newly born organism, and because of this phenomenon, intercellular complexes with high structural stability and rigidity are unfavourable for cellular differentiation and migration, and successful morphogenesis. ...
In most parts of postnatal ontogenesis, structural stability of collagenous formations rises; this is considered as one of the mechanisms of adaptation of connective tissue mechanical properties to an increase in body weight and muscular strength of an organism in the course of its growth and development. The purpose of the study was to investigate the metabolic and functional justifications (changes in the self-assembly of collagen fibrils) to the decrease in the structural stability of matrix sub-molecular complexes of the connective tissue in early postnatal ontogenesis. Investigations were carried out using the dorsal skin of 20 male Wistar rats that were divided into four (4) groups according to their ages. Self-assembly of collagen fibrils was carried out by monitoring their spontaneous formation in saline solution after 1, 3, 10 and 20 days of storage; the presence of fibrils in solution was observed under the microscope. It was found out that, temporary changes in the morphology of fibrils formed from type I collagen of animals of different age groups were significantly different from each other. It was concluded that fibrils formed from the collagen of younger rats were shorter and had smaller diameters than those formed in the collagen of middle-aged and elderly rats; and that, the observed pattern of continued increase in length of fibrils with ageing is the result of age-related characteristic features of processing, and consequently, the nature of cross-linking; during the period up to three (3) months, there is a rapid growth of the newly born organism; because of this, intercellular complexes with high structural stability and rigidity are unfavourable for cellular differentiation and migration, and successful morphogenesis.
