Nucleotide sequence of ovine macrophage interleukin-1 beta cDNA.

We have cloned and sequenced the cDNA for the coding region of ovine alveolar macrophage interleukin-1 beta. At the nucleotide level, the ovine cDNA shares 95, 74 and 71% homology with the bovine, human and murine cDNA equivalents or homologs. Comparison at the amino acid level revealed 95% homology with bovine IL-1 beta and approximately 57% with the human and murine homologs.     

The effect of spike mutations on SARS-CoV-2 neutralization

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The effect of chronic acid/base disturbances on renal amino acid clearances in the rat

Since the few data available concerning the effect of acid/base disturbances on renal amino acid reabsorption were conflicting, and there were sound theoretical reasons for an effect, we have studied the clearance of endogenous amino acids in the rat in vivo under control conditions and after induction of either metabolic acidosis or alkalosis by administration of NH4Cl or NaHCO3, respectively. The effectiveness of treatment was assessed by examination of plasma and urinary levels of HCO3, Cl, Na and K. It was found that the renal clearance of amino acids, measured during acidosis or alkalosis, did not differ from those found under control conditions, the majority of values being less than 1% of the glomerular filtration rate. Thus, the amino acid reabsorptive mechanism appears unaffected by changes in the pH of the glomerular filtrate and/or by changes in tubular hydrogen ion secretion which would accompany such disturbances. These data are thus in agreement with findings during acidosis in man and in both acidosis and alkalosis in the dog. The findings are contrary to earlier reports from in vitro studies in the rat, and suggest the presence of severe functional impairment in the isolated perfused kidneys used in these earlier studies where very large changes in amino acid clearance were obtained.     

Structural Insights into Cdk5 activation by a neuronal Cdk5 activator.

Although Cdk5 shows high sequence identity to Cdk1 and Cdk2, it can be fully activated by its neuronal activators p35/p25(nck5a) and p39(nck5ai) in a phosphorylation-independent manner. To understand structural basis of the Cdk5/p25(nck5a) activation, the complex is modelled to assume either an obstructed or an opened conformation based on X-ray structures of the unphosphorylated or the phosphorylated Cdk2/cyclin A complex, respectively. Comparison and analysis of the two models, along with mutagenesis studies of p25(nck5a), suggest that the opened form represents more closely the structure of active Cdk5/p25(nck5a). The results provide a rationale basis for understanding the phosphorylation-independent activation of Cdk5/p25(nck5a).