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- W2890119973 abstract "Nature is always the best inspiration for basic research. A family with severe thrombosis and antithrombin deficiency, the strongest anticoagulant, carried a new mutation affecting the translation-start codon of SERPINC1, the gene encoding antithrombin. Expression of this variant in a eukaryotic cell system produced three different antithrombins. Two downstream methionines were used as alternative initiation codons, generating highly expressed small aglycosylated antithrombins with cytoplasmic localization. Wild-type antithrombin was generated by the use of the mutated AUU as initiation codon. Actually, any codon except for the three stop codons might be used to initiate translation in this strong Kozak context. We show unexpected consequences of natural mutations affecting translation-start codons. Downstream alternative initiation AUG codons may be used when the start codon is mutated, generating smaller molecules with potential different cell localization, biochemical features and unexplored consequences. Additionally, our data further support the use of other codons apart from AUG for initiation of translation in eukaryotes." @default.
- W2890119973 created "2018-09-27" @default.
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- W2890119973 date "2018-09-04" @default.
- W2890119973 modified "2023-10-16" @default.
- W2890119973 title "Biochemical and cellular consequences of the antithrombin p.Met1? mutation identified in a severe thrombophilic family" @default.
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- W2890119973 doi "https://doi.org/10.18632/oncotarget.26059" @default.
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