GENDER FEATURES OF LAMINA CONTENT IN HUMAN SKIN FIBROBLASTS IN A PROCESS OF CHRONOLOGICAL AGING
https://doi.org/10.15372/SSMJ20190409
Abstract
The purpose of the study was to investigate gender peculiarities of the content of fibroblasts immunopositive to lamins A, B1 and B2 in skin samples in a process of chronological aging. Material and methods. 331 skin samples at the period from 20 to 40 weeks of gestation and people from birth to 85 years were examined. The content of positively stained dermal fibroblasts and the expression level of lamins A, B1 and B2 in their nucleus was explored by immunohistochemistry. Results and discussion. The gradual decrease of fibroblasts with positive staining for lamin A and the expression level of lamin A after antenatal period and up to old age depends on the age, but does not have differences, which are related to gender. The lamin B1 positively fibroblasts content is declining reliably from birth to 40 years and then it is increasing as well as the expression level of lamina B1. The indicated changes don’t have reliable variances in gender. The change in the number of lamina B2-positively colored fibroblasts and the expression level of lamina B2 has no statistically valid correlation with gender and age. Thus, there are no gender differences in dynamical age related changes of the content and the expression level of protein-lamina in skin fibroblasts in a process of chronological aging.
About the Authors
N. N. GolubtsovaRussian Federation
candidate of biological sciences
428015, Cheboksary, Moskovsky av., 45
A. V. Bogdanov
Russian Federation
428015, Cheboksary, Moskovsky av., 45
A. G. Gunin
Russian Federation
doctor of medical sciences
428015, Cheboksary, Moskovsky av., 45
References
1. Vasilieva O.V., Golubtsova N.N., Filippov F.N., Gunin A.G. Connective tissue growth factor (CTGF) in the human dermis through ontogenesis. Ontogenez = Ontogenesis. 2016; 47 (2): 75–82. [In Russian]
2. Barton L.J., Soshnev A.A., Geyer P.K. Networking in the nucleus: a spotlight on LEM-domain proteins. Curr. Opin. Cell Biol. 2015; 34: 1–8.
3. Briand N., Cahyani I., Madsen-Østerbye J., Paulsen J., Rønningen T., Sørensen A.L., Collas P. Lamin A, chromatin and FPLD2: Not just a peripheral ménage-à-trois. Front. Cell Dev. Biol. 2018; 6: ID 73.
4. Briand N., Collas P. Laminopathy-causing lamin A mutations reconfigure lamina-associated domains and local spatial chromatin conformation. Nucleus. 2018; 9 (1): 216–226.
5. Burke B., Stewart C.L. The nuclear lamins: flexibility in function. Nat. Rev. Mol. Cell Biol. 2013; 14: 13–24.
6. Coolen N.A., Schouten K.C., Middelkoop E. Comparison between human fetal and adult skin. Arch. Dermatol. Res. 2010; 302 (1): 47–55.
7. Frantz C., Stewart K.M., Weaver V.M. The extracellular matrix at a glance. J. Cell Sci. 2010; 123 (24): 4195–4200.
8. Gesson K., Vidak S., Foisner R. Laminaassociated polypeptide (LAP)2α and nucleoplasmic lamins in adult stem cell regulation and disease. Semin. Cell. Dev. Biol. 2014; 29: 116–124.
9. Golubtsova N.N. Kornilova N.K., Gunin A.G. Age-related changes in serin-arginin protein kinase 1 (SRPK1) content in the human dermis. Adv. Gerontol. 2018; 8 (2): 147–152.
10. Gruenbaum Y., Medalia O. Lamins: the structure and protein complexes. Curr. Opin. Cell Biol. 2015; 32: 7–12.
11. Gunin A.G., Petrov V.V., Golubtsova N.N., Vasilieva O .V., Kornilova N.K. Age-related changes in angiogenesis in human dermis. Exp. Gerontol. 2014; 55: 143–151.
12. Hutchison C.J. B-type lamins in health and disease. Semin. Cell. Dev. Biol. 2014; 29 (100): 158–163.
13. Lund E., Collas P. Nuclear lamins: making contacts with promoters. Nucleus. 2013; 4 (6): 424–430.
14. Oh J.H., Kim Y.K., Jung J.Y., Shin J.E., Chung J.H. Changes in glycosaminoglycans and related proteoglycans in intrinsically aged human skin in vivo. Exp. Dermatol. 2011; 20 (5): 454–456.
15. Van Steensel B., Belmont A.S. Lamina-associated domains: Links with chromosome architecture, heterochromatin, and gene repression. Cell. 2017; 169: 780–791.