Enzymatic test for the detection of a riboflavin deficiency. NADPH-dependent glutathione reductase of red blood cells and its activation by FAD in vitro

Zusammenfassung Die NADPH-spezifische Glutathion-reduktaseaktivität hämolysierter Erythrozyten erscheint brauchbar als Parameter zur Erfassung von Riboflavin-mangelzuständen. Die Enzymaktivität wird in vitro durch einen Zusatz von FAD bei Riboflavinmangelratten wesentlich stärker erhöht als bei Kontrollratten. Untersuchungen mit menschlichen Erythrozyten deuten darauf hin, dass auch hier die Aktivierbarkeit des Enzyms durch FAD vom Riboflavinstatus abhängt.

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The following abbreviations are used: NADPH, reduced form of nicotinamide adenine dinucleotide phosphate (triphosphopyridine nucleotide); FAD, flavin adenine dinucleotide.     

The FN3 and BRCT motifs in the exomer component Chs5p define a conserved module that is necessary and sufficient for its function

Chs5p is a component of the exomer, a coat complex required to transport the chitin synthase Chs3p from the trans-Golgi network to the plasma membrane. The Chs5p N-terminal region exhibits fibronectin type III (FN3) and BRCT domains. FN3 domains are present in proteins that mediate adhesion processes, whereas BRCT domains are involved in DNA repair. Several fungi—including Schizosaccharomyces pombe, which has no detectable amounts of chitin—have proteins similar to Chs5p. Here we show that the FN3 and BRCT motifs in Chs5p behave as a module that is necessary and sufficient for Chs5p localization and for cargo delivery. The N-terminal regions of S. cerevisiae Chs5p and S. pombe Cfr1p are interchangeable in terms of Golgi localization, but not in terms of exomer assembly, showing that the conserved function of this module is protein retention in this organelle and that the interaction between the exomer components is organism-specific.