In order to clarify the relationship between salt-tolerance of Zygosaccharomyces rouxii and the function of Na+/H(+)-antiporter, a gene was isolated from Z. rouxii which exhibited homology to the Na+/H(+)-antiporter gene (sod2) from Schizosaccharomyces pombe. This newly isolated gene (Z-SOD2) encoded a product of 791 amino acids, which was larger than the product encoded by its Sz. pombe homologue. The predicted amino-acid sequence of Z-Sod2p was highly homologous to that of the Sz. pombe protein, but included an extra-hydrophilic stretch in the C-terminal region. The expression of Z-SOD2 was constitutive and independent of NaCl-shock. Z-SOD2-disruptants of Z. rouxii did not grow in media supplemented with 3 M-NaCl, but grew well in the presence of 50% sorbitol, indicating that the function of Z-SOD2 was closely related to the salt-tolerance of Z. rouxii. Several genes are also compared and discussed in relation to the salt-tolerance of Z. rouxii.

To determine the effects of the multifunctional iron-binding glycoprotein, lactoferrin (LF) and related compounds on the growth of leukemic cells, human myeloid leukemic cells (HL-60) were exposed to bovine lactoferrin (bLF) and proteolytic hydrolysates of bLF. Pepsin hydrolysates of bLF showed a greater growth suppressive effect than tryptic hydrolysates or mature bLF. Four peptides with proliferation inhibition activity were purified from pepsin hydrolysates by ion-exchange chromatography, reverse-phase HPLC, and gel-filtration. All peptides were from the N-terminal end, in a region where lactoferricin B (Lfcin B), an antibacterial peptide, is located. Among the four peptides, peptide 1 (pep1) was found to exhibit highest activity and corresponded to residues 17 to 38 of bLF, with a molecular weight of 2753.88. The IC50 value of this peptide was 6.3 micrograms/ml. Three other peptides were less active and corresponded to sequences 1 to 16 and 45 to 48, linked by disulfide-bridge (pep2, molecular mass of 2430.13), 1 to 15 and 45 to 46 linked by disulfide bridge (pep3, molecular mass of 2017,92) and from residues 1 to 13 (pep4, molecular mass of 1558.73). Cell proliferation inhibition activity of the peptides was thought to be due to induction of apoptosis, which was evaluated by DNA ladder formation, DNA fragmentation, enhanced expression of phosphatidyl serine, and morphological changes. The IC50 values of the three peptides were confirmed using synthetic peptides and were consistent with those of purified peptides.

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The ZrGPD1 and ZrGPD2 genes encoding putative glycerol-3-phosphate dehydrogenases were isolated from the salt-tolerant yeast, Zygosaccharomyces rouxii. Both genes are homologous to GPD1 of Saccharomyces cerevisiae and are constitutively expressed in Z. rouxii cells. Putative glycerol dehydrogenase genes, ZrGCY1 and ZrGCY2, which are highly homologous to GCY1 of S. cerevisiae, were also isolated. Since the level of transcripts of ZrGCY1 and ZrGCY2 increased in Z. rouxii cells subjected to salt stress, it is suggested that the pathway of the signal transduction of salt stress controls the expression of these genes. The Accession Nos of these sequences in GenBank are as follows: ZrGPD1, AB047394; ZrGPD2, AB047395; ZrGCY1, AB047396; ZrGCY2, AB047397.

We continuously measured body composition in HCV-infected patients who received DAA therapy and found that skeletal muscle mass was significantly increased, associated with an elevation of serum Alb levels and/or body weight or reduction in VFA, but only in patients who presented with LSM before DAA therapy.