Chemical composition of B-type supergiants in the OB 8, OB 10, OB 48, OB 78 associations of M 31

Absolute and differential chemical abundances are presented for the largest group of massive stars in M31 studied to date. These results were derived from intermediate resolution spectra of seven B-type supergiants, lying within four OB associations covering a galactocentric distance of 5-12 kpc. The results are mainly based on an LTE analysis, and we additionally present a full non-LTE, unified model atmosphere analysis of one star (OB 78-277) to demonstrate the reliability of the differential LTE technique. A comparison of the stellar oxygen abundance with that of previous nebular results shows that there is an off set of between similar to0.15-0.4 dex between the two methods which is critically dependent on the empirical calibration adopted for the R 23 parameter with [O/H]. However within the typical errors of the stellar and nebular analyses (and given the strength of dependence of the nebular results on the calibration used) the oxygen abundances determined in each method are fairly consistent. We determine the radial oxygen abundance gradient from these stars, and do not detect any systematic gradient across this galactocentric range. We find that the inner regions of M31 are not, as previously thought, very "metal rich". Our abundances of C, N, O, Mg, Si, Al, S and Fe in the M31 supergiants are very similar to those of massive stars in the solar neighbourhood.

Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins.

Advanced glycation endproducts (AGEs) are derivatives of nonenzymatic reactions between sugars and protein or lipids, and together with AGE-specific receptors are involved in numerous pathogenic processes associated with aging and hyperglycemia. Two of the known AGE-binding proteins isolated from rat liver membranes, p60 and p90, have been partially sequenced. We now report that the N-terminal sequence of p60 exhibits 95% identity to OST-48, a 48-kDa member of the oligosaccharyltransferase complex found in microsomal membranes, while sequence analysis of p90 revealed 73% and 85% identity to the N-terminal and internal sequences, respectively, of human 80K-H, a 80- to 87-kDa protein substrate for protein kinase C. AGE-ligand and Western analyses of purified oligosaccharyltransferase complex, enriched rough endoplasmic reticulum, smooth endoplasmic reticulum, and plasma membranes from rat liver or RAW 264.7 macrophages yielded a single protein of approximately 50 kDa recognized by both anti-p60 and anti-OST-48 antibodies, and also exhibited AGE-specific binding. Immunoprecipitated OST-48 from rat rough endoplasmic reticulum fractions exhibited both AGE binding and immunoreactivity to an anti-p60 antibody. Immune IgG raised to recombinant OST-48 and 80K-H inhibited binding of AGE-bovine serum albumin to cell membranes in a dose-dependent manner. Immunostaining and flow cytometry demonstrated the surface expression of OST-48 and 80K-H on numerous cell types and tissues, including mononuclear, endothelial, renal, and brain neuronal and glial cells. We conclude that the AGE receptor components p60 and p90 are identical to OST-48, and 80K-H, respectively, and that they together contribute to the processing of AGEs from extra- and intracellular compartments and in the cellular responses associated with these pathogenic substances.