Impaired protein folding, dimer formation, and heterotetramer assembly cause intra- and extracellular instability of a Y283C mutant of the A subunit for coagulation factor XIII.

Abstract excerpt

Factor XIII (XIII) is a heterotetramer consisting of two catalytic A subunits (XIIIA) and two noncatalytic B subunits (XIIIB). We examined the molecular mechanisms of a Y283C mutation which had previously been identified in a patient with XIIIA deficiency. The recombinant Y283C protein was labile when expressed in MEG-01 cells, which can endogenously synthesize XIIIA. We also included two other mutants, G562R and...

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