Identification and characterization of an Ecl1-family gene in Saccharomyces cerevisiae.

We found that YGR146C of Saccharomyces cerevisiae encodes a functional homolog of Ecl1 that is involved in the chronological lifespan of Schizosaccharomyces pombe. When YGR146C is overexpressed, it extends the viability of wild-type S. cerevisiae cells after entry into the stationary phase, as in the case of Ecl1.

Identification of Ecl family genes that extend chronological lifespan in fission yeast.

In fission yeast, we identified two genes, named ecl2+ and ecl3+, that are paralogous to ecl1+, which extends the chronological lifespan. Both ecl2+ and ecl3+ extend the chronological lifespan when overexpressed as ecl1+. ecl2+ and ecl3+ encode 84- and 89-amino acid polypeptides respectively that are not annotated in the current database.

A novel gene, ecl1(+), extends the chronological lifespan in fission yeast.

We have identified a novel gene from Schizosaccharomyces pombe that we have named ecl1(+) (extender of the chronological lifespan). When ecl1(+) is provided on a high-copy number plasmid, it extends the viability of both the Deltasty1 MAP kinase mutant and the wild-type cells after entry into the stationary phase. ecl1(+) encodes an 80-amino acid polypeptide that had not been annotated in the current database.

Identification of a fatty acyl-CoA synthetase gene, lcf2+, which affects viability after entry into the stationary phase in Schizosaccharomyces pombe.

The lcf1(+) gene, which encodes a long chain fatty acyl-CoA synthetase, is necessary for the maintenance of viability after entry into the stationary phase in Schizosaccharomyces pombe. In this study, we analyzed a paralogous gene, SPBP4H10.11c (named lcf2(+)), and we present evidence that the gene encodes a new fatty acyl-CoA synthetase.

Demonstration of the expression and the enzymatic activity of N-acetylglucosaminyltransferase IX in the mouse brain.

We recently reported on a brain-specific beta1,6-N-acetylglucosaminyltransferase IX (GnT-IX, also referred to as GnT-VB), a GnT-V homologue, which acts on alpha-linked mannose of N-glycans and O-mannosyl glycans. To distinguish functions of GnT-IX with GnT-V, we examined the distribution of GnT-IX and GnT-V transcripts in mouse tissues by Northern blot analysis. The two enzymes were differentially expressed as has previously been observed in human tissues.

A novel mechanism for the inhibition of hyaluronan biosynthesis by 4-methylumbelliferone.

Specific inhibitors of hyaluronan (HA) biosynthesis can be valuable therapeutic agents to prevent cancer invasion and metastasis. We have found previously that 4-methylumbelliferone (MU) inhibits HA synthesis in human skin fibroblasts and in group C Streptococcus. In this paper, the inhibition mechanism in mammalian cells was investigated using rat 3Y1 fibroblasts stably expressing HA synthase (HAS) 2.