{"id":10710,"date":"2022-10-26T12:31:44","date_gmt":"2022-10-26T03:31:44","guid":{"rendered":"https:\/\/www.emukk.com\/WP\/?p=10710"},"modified":"2022-10-27T06:50:39","modified_gmt":"2022-10-26T21:50:39","slug":"interactions-between-galectins-and-o-mannosylated-core-m1-glycopeptides-of-%ce%b1-dystroglycan","status":"publish","type":"post","link":"https:\/\/www.emukk.com\/WP\/en\/interactions-between-galectins-and-o-mannosylated-core-m1-glycopeptides-of-%ce%b1-dystroglycan\/","title":{"rendered":"Interactions between galectins and O-mannosylated core M1 glycopeptides of \u03b1-dystroglycan"},"content":{"rendered":"

A group from Frontier Research Center for Advanced Material and Life Science, Hokkaido University, Sapporo, Japan, etc. has reported about interactions between galectins and O-mannosylated glycopeptides of \u03b1-dystroglycan, especially focusing on its core M1 structure.
\nhttps:\/\/www.nature.com\/articles\/s41598-022-22758-0<\/a><\/p>\n

The O-linked mannose (O-Man) exists in a limited number of proteins that are required for normal development and have vital functions in muscle and neural physiology. The \u03b1-dystroglycan (\u03b1-DG) is the extracellular component of dystroglycan (DG), and is the most extensively studied mammalian O-Man glycoprotein. It is ubiquitously expressed in the skeletal muscles and the brain and is associated with cell adhesion, muscle integrity, and neurological development. \u03b1-DG possesses unique glycans, LacNac-terminated three kind of core structures (M1, M2, and M3), in its mucin (MUC)\u2013like domain.<\/p>\n

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In this study, it was shown that Human Gal-1, -4, and -9 (except -3) can strongly recognize O-Man LacNAc-terminated glycoconjugates, and the presence of an \u03b12,3-sialylated terminus led to a major reduction in the affinity of galectin, suggesting that this type of extension can fine-tune galectin activity towards this type of O-Man glycans. These interactions were significantly inhibited by lactose, establishing that the \u03b1-DG core M1-type glycans bind to the canonical sugar-binding site (S-face) of galectin, thus serving as a receptor for galectins.<\/p>\n

And further, it was shown in microarray experiments that Gal-1 revealed trans-bridging capabilities, linking laminin-111, -121, -211, and -221 (but little -511) and core M1 \u03b1-DG glycopeptides as shown below, providing a new insight on the therapeutic application of this galectin in muscular dystrophy.<\/p>\n

\"\"<\/a>
\nFluorescence images of M1 glycoconjugates microarrays with laminins plus galectins<\/p>\n","protected":false},"excerpt":{"rendered":"

A group from Frontier Research Center for Advanced Material and Life Science, Hokkaido University, Sapporo, Ja<\/p><\/div>\n

\u7d9a\u304d\u3092\u8aad\u3080<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[70,7],"tags":[],"class_list":["post-10710","post","type-post","status-publish","format-standard","hentry","category-nature-en","category-technology-en"],"aioseo_notices":[],"aioseo_head":"\n\t\t\n\t\n\t\n\t\n\t\n\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t