ABSTRACT. In order to obtain basic information about bovine interleukin-1 (IL-1β), levels of IL-1β in sera and milk of clinically normal mature Holstein cattle before and after parturition and in sera of newborn calves were examined by ELISA. The level of IL-1β was undetectable in sera of mature cattle around the time of artificial insemination, but the concentration gradually increased and reached a peak at parturition and then decreased again to an undetectable level. IL-1β in milk was detected on the day of parturition but not thereafter. IL-1β mRNA was detected by reverse transcription-polymerase chain reaction in the cells from milk collected during 20 days before and 2 to 3 days after parturition, but was not detected thereafter. Although IL-1β was not detected in all the sera of newborn calves, the concentration transiently increased with peak titers on day 3 and became undetectable by day 14 after birth. Newborns that showed serum IL-1β on day 3 had been fed on colostrum in which the IL-1β concentration was significantly higher than that in colostrum that had been fed to newborns having no detectable IL-1β on day 3. These results indicate that IL-1β is induced in association with pregnancy in healthy dairy cattle and that the cytokine might be transferred to neonates via colostrum. -KEY WORDS: cattle, colostrum, interleukin-1, pregnancy.
Amyotrophic lateral sclerosis (ALS) is the most common fatal motor neuron disease. It has been generally accepted that the proapoptotic property of the familial ALS (FALS)-linked mutant SOD1 genes plays an important role in the pathogenesis of some FALS cases. We found here that expression of N19S-SOD1, a novel SOD1 mutant originally found in a sporadic ALS patient, induces lower grade death in NSC34 cells than FALS-linked mutant SOD1. In agreement, intracytoplasmic aggregate formation and SOD1 polymerization are less prominently induced by ectopic expression of N19S-SOD1 than FALS-linked mutant SOD1. We further found that additional cell stresses, such as inhibition of proteasomal activity or up-regulation of intracellular oxidative stress, enhance N19S-SOD1-induced aggregate formation and polymerization of N19S-SOD1. Such analysis of the intracellular polymerization and the ubiquitination of N19S-SOD1 have further suggested that it is recognized as a misfolded protein, like FALS-linked mutant SOD1, whereas wild-type SOD1 is not. Altogether, it is speculated that the N19S mutation of SOD1 in cooperation with associated cell stresses contributes to the onset of ALS as a risk factor.
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