The role of processing in age-related changes of collagen thermo-stability
Abstract
The connection between the degree of proline hydroxylation, of lysine and hydroxylysine ε-NH2-groups in collagen oxidative delamination and thermo-stability of the collagen sub-molecular structures in the skin of Wistar rats during postnatal ontogenesis, was in vitro studied. It was shown that, after an increase in these free ε-NH2-groups in collagen towards the age of 3-months, their content further remained constant while at the same time, the content of COH-groups steadily decreases with age, beginning from 1-month. Due to this, inter-molecular cross-linking in collagenous sub-molecular structures decreases from 1 to 3 months of age and afterward, continuously rises up to the age of 24 months. The content of hydroxyproline in collagen continuously decreases during postnatal ontogenesis. The joint action of both effects leads to a decrease in the thermo-stability of collagenous sub-molecular structures in the skin from 1 to 3 months of age, with its further increase up to the age of 24 months.
Downloads
References
2. Обысов А.С. Надёжность биологических тканей. – М.; Медицина. – 1971. – 103 с.
3. Vogel M. G. Influence of maturation and ageing on mechanical and biochemical properties of connective tissue in rats // Mech. Ageing and Dev. – 1980. – Vol. 14, № 3. – 4. – P. 283 – 292.
4. Jenkins C.L., Raines R.T. Insights on the conformational stability of collagen // Nat. Prod. Rep. – 2002. – Vol. 19. – P. 49 – 59.
5. Berisio R., Vitagliano L., Mazzarella L., Zagari A. Crystal structure of a collagen-like polypeptide with repeating sequence Pro-Hyp-Gly at 1,4 A resolution: implications for collagen hydration // Biopolymers. – 2000 – 2001. – Vol. 56, № 1. – Р. 8 – 13.
6. Борискина Е.П. Энергии водородных связей, стабилизирующие конформацию гидратированных коллагеновых структур: Дис. канд. физ.-мат. наук. – Харьков.: - Харьковский национальный университет им. В.Н.Каразина. – 2007. – 147 с.
7. Berg R.A., Prockop D.J. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen // Biochem. Biophys. Res. Commun. – 1973. – Vol. 152, № 1. – P. 115 – 120.
8. Nishi Y., Uchiyama S., Nishiuchi Y., Nakazawa T., Ohkubo T., Kobayashi Y. Different effects of 4- hydroxyproline and 4-fluoroproline jn the stability of collagen triple helix // Biochemistry. – 2005. – Vol. 44, № 16. – Р. 6034 – 6042. 9. Eyre D.R., Wu J. – J. Collagen Cross – Links // Topics in Current Chemistry. – 2005. – Vol. 247. – P. 207 – 229.
10. Bailey A.Y., Paul R.G. The mechanisms and consequences of the maturation and ageing of collagen // Proc. Indian Acad. Sci. (Chem. Sci.). – 1999. – Vol. 111, № 1. – P. 57 – 69.
11. Перский Е. Э., Никитина Н.А., Наглов А.В., Кот Ю.Г. Возрастные особенности индукции синтеза и интенсивности некоторых стадий процессинга коллагена в соединительной ткани под действием механической нагрузки // Биологический вестник. – 2006 . – Т.10, № 2. – С. 126 – 129.
12. Yamauchi M., Masashi М. Post-translational Modifications of Proteins: Lysine Hydroxylation and Cross-linking of collagen // Tools for Functional Proteomics. – Series: Methods in Molecular Biology. – 2008. – Vol. 445. P. 95 – 108.
13. И. Клотц. Энергетика биохимических реакций.- М.: Мир.–1970.– 112 с.
14. Гарбузенко О.Б., Емец Е.Б., Перский Е.Э. Влияние деформации на обмен белков и механические свойства аорты и кожи крыс in vitro // Вестн. пробл. биол. и мед. - 1997. - № 25. - С. 12-18.
15. Бейли Дж. Методы химии белков – М.: Мир, 1965. – 284 с.
16. Дубинина Е.Е. Окислительная модификация белков плазмы крови больных с психиатрическими расстройствами // Вопр. мед. химии. – 2000. – №4. – С. 36 – 47.
17. Утевская Л.А., Перский Е.Э. Простой метод определения суммарного и свободного оксипролина // Вестн. Харьк. ун-та. – 1982. – № 226. – С. 18 – 20.
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
- Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).