Post-transcriptional regulation of transferrin receptor mRNA levels by iron is mediated by a portion of the 3' untranslated region (UTR) of the mRNA. We

It is generally accepted that short (C 2 -C 5 ) and medium (C 6 -C 11 ) chain volatile fatty acids (VFAs) are among the primary causal molecules of axillary malodour. It is also widely acknowledged that malodour generation is attributable to the biotransformation of odourless natural secretions, into volatile odorous products, by cutaneous bacteria. However, little information is available on the biochemical origins of VFAs on axillary skin. In these studies, assay systems were developed to investigate the generation of VFAs from lipid substrates readily available to the bacteria resident on axillary skin. A major route to short and medium chain VFAs in the axilla was shown to be the partial catabolism of structurally unusual (e.g. methyl-branched) longer chain fatty acids by a previously uncharacterized sub-group of the Corynebacterium genus, corynebacteria (A). In contrast, corynebacteria (B) are incapable of growth on fatty acid. Structurally unusual fatty acids originate from the triacylglycerol component of sebum, and probably also apocrine sweat, by the action of bacterial lipases. Interestingly, VFA formation in the axilla is a dynamic process, with some cutaneous microorganisms, specifically micrococci and brevibacteria, capable of fully catabolizing these odorants. The results of these studies provide new understanding on the biochemical origins of VFA-based axillary malodour.

RNA editing plays a central role in the life cycle of hepatitis D virus (HDV), a subviral human pathogen.

These data provide new in vivo evidence for an antiinflammatory role for SP-D in response to noninfectious, subacute lung injury via modulation of oxidative-nitrative stress.

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Surfactant protein A (SP-A Increases in SP-D content, gamma interferon, interleukin-4, interleukin-5, and tumor necrosis factor alpha in BAL fluid occurred but were attenuated in PCP-infected SP-A؊/؊ mice compared to WT mice. There were increases in total BAL NO levels in both infected groups, but nitrite levels were higher in SP-A ؊/؊ mice, indicating a reduction in production of higher oxides of nitrogen that was also reflected in lower levels of 3-nitrotyrosine staining in the SP-A ؊/؊ group. We conclude that despite increases in inflammatory cells, SP-A-deficient mice infected with P. carinii exhibit an enhanced susceptibility to the organism and attenuated production of proinflammatory cytokines and reactive oxygen-nitrogen species. These data support the concept that SP-A is a local effector molecule in the lung host defense against P. carinii in vivo.

The yeast Candida cloacae is capable of growing on alkanes and fatty acids as sole carbon sources. Transfer of cultures from a glucose medium to one containing oleic acid induced seven proteins of M r 102,000, 73,000, 61,000, 54,000, and 46,000 and two in the region of M r 45,000 and repressed a protein of M r 64,000. The induction of the M r 73,000 protein reached a 7-fold maximum 24 h after induction. The protein was confirmed by its enzyme activity to be a long-chain fatty-acid alcohol oxidase (LC-FAO) and purified to homogeneity from microsomes by a rapid procedure involving hydrophobic chromatography. An internal peptide of 30 amino acids was sequenced. A 1100-base pair cDNA fragment containing the LC-FAO peptide coding sequence was used to isolate a single exon genomic clone containing the full-length coding sequence of an LC-FAO (fao1). The fao1 gene product was expressed in Escherichia coli and was translated as a functional long-chain alcohol oxidase, which was present in the membrane fraction. In addition, full-length coding sequences for a Candida tropicalis LC-FAO (faoT) and a second C. cloacae LC-FAO (fao2) were isolated. The DNA sequences obtained had open reading frames of 2094 (fao1), 2091 (fao2), and 2112 (faoT) base pairs. The derived amino acid sequences of fao2 and faoT showed 89.4 and 76.2% similarities to fao1. The fao1 gene is much more highly induced on alkane than is fao2. Although this study describes the first known DNA sequences encoding LC-FAOs from any source, there are unassigned Arabidopsis sequences and an unassigned Mycobacterium sequence in the GenBank TM Data Bank that show strong homology to the described LC-FAO sequences. The conservation of sequence between yeast, plants, and bacteria suggests that an as yet undescribed family of long-chain fattyacid oxidases exists in both eukaryotes and prokaryotes.