Overview of sialylation status in human nervous and skeletal muscle tissues during aging

xlomafota13 shared this article with you from Inoreader Overview of sialylation status in human nervous and skeletal muscle tissues during aging Via histochem Acta Histochem. 2021 Nov 6;123(8):151813. doi: 10.1016/j.acthis.2021.151813. Online ahead of print. ABSTRACT Sialic acids (Sias) are a large and heterogeneous family of electronegatively charged nine-carbon monosaccharides containing a carboxylic acid and are mostly found as terminal residues in glycans of glycoproteins and glycolipids such as gangliosides. They are linked to galactose or N-acetylgalactosamine via α2,3 or α2,6 linkage, or to other Sias via α2,8 or more ra rely α2,9 linkage, resulting in mono, oligo and polymeric forms. Given their characteristics, Sias play a crucial role in a multitude of human tissue biological processes in physiological and pathological conditions, ranging from development and growth to adult life until aging. Here, we review the sialylation status in human adult life focusing on the nervous and skeletal muscle tissues, which both display significant structural and functional changes during aging, strongly impacting on the whole human body and, therefore, on the quality of life. In particular, this review highlights the fundamental roles played by different types of glycoconjugates Sias in several cellular biological processes in the nervous and skeletal muscle tissues during adult life, also discussing how changes in Sia content during aging may contribute to the physiological decline of physical and nervous functions and to the development of age-related degenerative pathologies. Based on our current knowledge, further in-depth investigations could help to develop novel prophylactic strategies and therapeutic approaches that, by maintaining and/or restoring the correct sialylation status in the nervous and skeletal muscle tissues, could contribute to aging slowing and the prevention of age-related pathologies. PMID:34753032 | DOI:10.1016/j.acthis.2021.151813 View on the web Inoreader. Take back control of your news feed. Follow us on Twitter and Facebook.