prikaz prve stranice dokumenta A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome
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Scientific paper - Original scientific paper
A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome
Matrix Biology Plus, 9 (2021); 100053. https://doi.org/10.1016/j.mbplus.2020.100053
Odiatis, Christoforos; Savva, Isavella; Pieri, Myrtani; Ioannou, Pavlos; Petrou, Petros; Papagregoriou, Gregory; Antoniadou, Kyriaki; Makrides, Neoklis; Stefanou, Charalambos; Galešić Ljubanović, Danica; Nikolaou, Georgios; Borza, Dorin-Bogdan; Stylianou, Kostas; Gross, Oliver; Deltas, Constantinos More authors...

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Odiatis, C., Savva, I., Pieri, M., Ioannou, P., Petrou, P., Papagregoriou, G. ... Deltas, C. (2021). A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome. Matrix Biology Plus, 9.. doi: 10.1016/j.mbplus.2020.100053

Odiatis, Christoforos, et al. "A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome." Matrix Biology Plus, vol. 9, 2021. https://doi.org/10.1016/j.mbplus.2020.100053

Odiatis, Christoforos, Isavella Savva, Myrtani Pieri, Pavlos Ioannou, Petros Petrou, Gregory Papagregoriou, Kyriaki Antoniadou, et al. "A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome." Matrix Biology Plus 9 (2021). https://doi.org/10.1016/j.mbplus.2020.100053

Odiatis, C., et al. (2021) 'A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome', Matrix Biology Plus, 9. doi: 10.1016/j.mbplus.2020.100053

Odiatis C, Savva I, Pieri M, Ioannou P, Petrou P, Papagregoriou G, and sur.. A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome. Matrix Biology Plus [Internet]. 2021 February [cited 2025 April 24];9. doi: 10.1016/j.mbplus.2020.100053

C. Odiatis, et al., "A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome", Matrix Biology Plus, vol. 9, February 2021. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:105:615901. [Accessed: 24 April 2025]

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Metadata
Title (english)A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome
AuthorChristoforos Odiatis
AuthorIsavella Savva
AuthorMyrtani Pieri
AuthorPavlos Ioannou
AuthorPetros Petrou
AuthorGregory Papagregoriou
AuthorKyriaki Antoniadou
AuthorNeoklis Makrides
AuthorCharalambos Stefanou
AuthorDanica Galešić Ljubanović
AuthorGeorgios Nikolaou
AuthorDorin-Bogdan Borza
AuthorKostas Stylianou
AuthorOliver Gross
AuthorConstantinos Deltas
Author's institutionUniversity of Zagreb
School of Medicine
(Department of Pathology)
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Clinical Medical Sciences
Pathology
Abstract (english)
Alport syndrome (AS) is a severe inherited glomerulopathy caused by mutations in the genes encoding the α-chains of type-IV collagen, the most abundant component of the extracellular glomerular basement membrane (GBM). Currently most AS mouse models are knockout models for one of the collagen-IV genes. In contrast, about half of AS patients have missense mutations, with single aminoacid substitutions of glycine being the most common. The only mouse model for AS with a homozygous knockin missense mutation, Col4a3-p.Gly1332Glu, was partly described before by our group. Here, a detailed in-depth description of the same mouse is presented, along with another compound heterozygous mouse that carries the glycine substitution in trans with a knockout allele. Both mice recapitulate essential features of AS, including shorten lifespan by 30-35%, increased proteinuria, increased serum urea and creatinine, pathognomonic alternate GBM thinning and thickening, and podocyte foot process effacement. Notably, glomeruli and tubuli respond differently to mutant collagen-IV protomers, with reduced expression in tubules but apparently normal in glomeruli. However, equally important is the fact that in the glomeruli the mutant α3-chain as well as the normal α4/α5 chains seem to undergo a cleavage at, or near the point of the mutation, possibly by the metalloproteinase MMP-9, producing a 35 kDa C-terminal fragment. These mouse models represent a good tool for better understanding the spectrum of molecular mechanisms governing collagen-IV nephropathies and could be used for pre-clinical studies aimed at better treatments for AS.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review
Publication versionPublished version
Journal titleMatrix Biology Plus
Numberingvol. 9, 100053
e-ISSN2590-0285
DOIhttps://doi.org/10.1016/j.mbplus.2020.100053
URN:NBNurn:nbn:hr:105:615901
Publication2021-02
Document URLhttps://linkinghub.elsevier.com/retrieve/pii/S259002852030034X
Type of resourceText
Access conditionsOpen access
Terms of useLicence Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) icon
Created on2021-06-18 08:57:44