prikaz prve stranice dokumenta A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome
  Preuzmi
PDF 5.63 MB
Znanstveni rad - Izvorni znanstveni rad
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 Više autora...

Citirajte ovaj rad

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, i sur.. A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome. Matrix Biology Plus [Internet]. 02.2021. [pristupljeno 07.10.2024.];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, Veljača 2021. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:105:615901. [Citirano: 07.10.2024.]

Za citiranje koristite ovu mrežnu adresu: https://urn.nsk.hr/urn:nbn:hr:105:615901
Prijavite se u repozitorij kako biste mogli spremiti objekt u svoju listu.
Podaci o radu
Naslov (engleski)A glycine substitution in the collagenous domain of Col4a3 in mice recapitulates late onset Alport syndrome
AutorChristoforos Odiatis
AutorIsavella Savva
AutorMyrtani Pieri
AutorPavlos Ioannou
AutorPetros Petrou
AutorGregory Papagregoriou
AutorKyriaki Antoniadou
AutorNeoklis Makrides
AutorCharalambos Stefanou
AutorDanica Galešić Ljubanović
AutorGeorgios Nikolaou
AutorDorin-Bogdan Borza
AutorKostas Stylianou
AutorOliver Gross
AutorConstantinos Deltas
Autorova ustanovaSveučilište u Zagrebu
Medicinski fakultet
(KATEDRA ZA PATOLOGIJU)
Znanstveno / umjetničko
područje, polje i grana		BIOMEDICINA I ZDRAVSTVO
Kliničke medicinske znanosti
Patologija
Sažetak (engleski)
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.
Ključne riječi (engleski)
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaMatrix Biology Plus
Brojčani podacivol. 9, 100053
e-ISSN2590-0285
DOIhttps://doi.org/10.1016/j.mbplus.2020.100053
URN:NBNurn:nbn:hr:105:615901
Datum objave publikacije2021-02
URL dokumentahttps://linkinghub.elsevier.com/retrieve/pii/S259002852030034X
Vrsta resursaTekst
Prava pristupaOtvoreni pristup
Uvjeti korištenjaIkona licence Imenovanje-Nekomercijalno-Bez prerada 4.0 međunarodna (CC BY-NC-ND 4.0)
Datum i vrijeme pohrane2021-06-18 08:57:44