Pub. Date : 2016 Feb 15
PMID : 26647313
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Aberrant disulphide bonding contributes to the ER retention of alpha1-antitrypsin deficiency variants. | disulphide | serine (or cysteine) preptidase inhibitor, clade A, member 1B | Mus musculus |
| 2 | We show in Hepa1.6 cells that the mildly polymerogenic I (Arg39Cys) AAT mutant forms aberrant inter- and intra-molecular disulphide bonds involving the acquired Cys39 and the only cysteine residue in the wild-type (M) sequence (Cys232). | disulphide | serine (or cysteine) preptidase inhibitor, clade A, member 1B | Mus musculus |
| 3 | Substitution of Cys39 to serine partially restores secretion, showing that disulphide bonding contributes to the intracellular retention of I AAT. | disulphide | serine (or cysteine) preptidase inhibitor, clade A, member 1B | Mus musculus |
| 4 | Prevention of such disulphide linkage through the introduction of the Cys232Ser mutation or by treatment of cells with reducing agents increases Z AAT secretion. | disulphide | serine (or cysteine) preptidase inhibitor, clade A, member 1B | Mus musculus |
| 5 | Our results reveal that disulphide interactions enhance intracellular accumulation of AAT mutants and implicate the oxidative ER state as a pathogenic co-factor. | disulphide | serine (or cysteine) preptidase inhibitor, clade A, member 1B | Mus musculus |