{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T16:38:23Z","timestamp":1770827903366,"version":"3.50.1"},"reference-count":20,"publisher":"Springer Science and Business Media LLC","issue":"8","license":[{"start":{"date-parts":[[2023,6,15]],"date-time":"2023-06-15T00:00:00Z","timestamp":1686787200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2023,6,15]],"date-time":"2023-06-15T00:00:00Z","timestamp":1686787200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"National Research Centre Egypt"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Biol Rep"],"published-print":{"date-parts":[[2023,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec>\n                <jats:title>Background<\/jats:title>\n                <jats:p>Congenital muscular dystrophies (CMDs) result from genetically inherited defects in the biosynthesis and\/or the posttranslational modification (glycosylation) of laminin-\u03b12 and \u03b1-dystroglycan (\u03b1-DG), respectively.\u00a0The interaction between both proteins is responsible for the stability and integrity of the muscle cell. We aimed to study the expression profiles of both proteins in two classes of CMDs.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Subjects and methods<\/jats:title>\n                <jats:p>Whole-exome sequencing (WES) was done for four patients with neuromuscular manifestations. The expression of core \u03b1-DG and laminin-\u03b12 subunit in skin fibroblasts and MCF-7 cells was assessed by western blot.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>WES revealed two cases with nonsense mutations; c.2938G\u2009&gt;\u2009T and c.4348\u00a0C\u2009&gt;\u2009T, in <jats:italic>LAMA2<\/jats:italic> encodes laminin-\u03b12. It revealed also two cases with mutations in <jats:italic>POMGNT1<\/jats:italic> encode protein O-mannose beta-1,2-N-acetylglucosaminyltransferase mutations. One patient had a missense mutation c.1325G\u2009&gt;\u2009A, and the other had a synonymous variant c.636\u00a0C\u2009&gt;\u2009T. Immunodetection of core \u03b1-DG in skin fibroblasts revealed the expression of truncated forms of core \u03b1-DG accompanied by reduced expression of laminin-\u03b12 in POMGNT1-CMD patients and one patient with LAMA2-CMD. One patient with LAMA2-CMD had overexpression of laminin-\u03b12 and expression of a low level of an abnormal form of increased molecular weight core \u03b1-DG. MCF-7 cells showed truncated forms of core \u03b1-CDG with an absent laminin-\u03b12.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusion<\/jats:title>\n                <jats:p>A correlation between the expression pattern\/level of core \u03b1-DG and laminin-\u03b12 could be found in patients with different types of CMD.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1007\/s11033-023-08500-7","type":"journal-article","created":{"date-parts":[[2023,6,15]],"date-time":"2023-06-15T11:01:45Z","timestamp":1686826905000},"page":"6373-6379","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["An atypical expression of core \u03b1-Dystroglycan and Laminin-\u03b12 in skin fibroblasts of patients with congenital muscular dystrophies"],"prefix":"10.1007","volume":"50","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0607-6842","authenticated-orcid":false,"given":"Sahar","family":"Sabry","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mahmoud Y","family":"Issa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohamed S","family":"Abdel-Hamid","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Noura R","family":"Eissa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sherif F","family":"Abdel-Ghafar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mona M","family":"Ibrahim","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maha S","family":"Zaki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2023,6,15]]},"reference":[{"key":"8500_CR1","doi-asserted-by":"crossref","unstructured":"Yoshida-Moriguchi T, Campbell KP (2015) \u201cMatriglycan: a novel polysaccharide that links dystroglycan to the basement membrane,\u201d Glycobiology, vol.\u00a025, no. 7, pp.\u00a0702\u2013713, Jul.","DOI":"10.1093\/glycob\/cwv021"},{"issue":"5","key":"8500_CR2","doi-asserted-by":"publisher","first-page":"783","DOI":"10.1016\/S1097-2765(00)80388-3","volume":"4","author":"E Hohenester","year":"1999","unstructured":"Hohenester E, Tisi D, Talts JF, Timpl R (1999) The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin. 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Written informed consent was obtained from the patient\u2019s legal guardians.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Written informed consent was obtained from the parent.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to participate"}},{"value":"was obtained from the patients\u2019 legal guardians.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}}]}}