Denovo glomerulonephritis associated with IgA anti-GBM alloantibodies after kidney transplantation in Alport syndrome: A case report with diagnostic implications.

Alport syndrome (AS) is a hereditary disorder caused by pathogenic variants in COL4A3, COL4A4, or COL4A5 genes expressing α3, α4, and α5 chains of basement membrane type IV collagen (COL4). The triple-helical α3α4α5(IV) protomer is a major component of the mature glomerular basement membrane (GBM) whose defective formation in AS leads to structural GBM disruption and kidney dysfunction, often resulting in kidney replacement therapy. A genetically intact renal graft exposes the immune system to a non-tolerized α3α4α5(IV) component and an alloimmune response eventually ensues.

Collagen IV dysfunction in glomerular basement membrane diseases. III. A functional framework for α345 hexamer assembly.

We identified a genetic variant, an 8-residue appendage, of the α345 hexamer of collagen IV present in patients with glomerular basement membrane diseases, Goodpasture's disease and Alport syndrome, and determined the long-awaited crystal structure of the hexamer. We sought to elucidate how variants cause glomerular basement membrane disease by exploring the mechanism of the hexamer assembly. Chloride ions induced in vitro hexamer assembly in a composition-specific manner in the presence of equimolar concentrations of α3, α4, and α5 NC1 monomers.

Erratum: Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. Corrigendum.

[This corrects the article DOI: 10.1107/S2052252518012459.].

Postoperative Management of Corneal Abrasions and Clinical Implications: a Comprehensive Review.

Purpose Of Review: Total patient care is of extreme importance during the administration of anesthesia. Proper care of the eye is necessary during all anesthetic administrations, especially during the administration of general anesthesia or monitored anesthesia care. By paying attention to details, the likelihood of an occurrence of eye injuries is reduced.

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly.

Basement membranes are extracellular structures of epithelia and endothelia that have collagen IV scaffolds of triple α-chain helical protomers that associate end-to-end, forming networks. The molecular mechanisms by which the noncollagenous C-terminal domains of α-chains direct the selection and assembly of the α1α2α1 and α3α4α5 hetero-oligomers found remain obscure. Autoantibodies against the noncollagenous domains of the α3α4α5 hexamer or mutations therein cause Goodpasture's or Alport's syndromes, respectively.