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• W2000573257 abstract "Because the cytokine interleukin-1 beta (IL-1 beta) lacks a classical hydrophobic signal sequence, it has been unclear how it is released from cells, and whether release proceeds via a novel mechanism or through non-specific leakage. To address this issue, we have examined the secretion of the recombinant forms of human IL-1 beta from COS monkey kidney cells, which express low levels of endogenous IL-1 beta. Four proteins were expressed: precursor and mature IL-1 beta and precursor and mature IL-1 beta fused to an amino terminal hydrophobic signal sequence from human tissue plasminogen activator. By monitoring the appearance of a known cytosolic protein (ATP citrate lyase) in the medium, we find that the unmodified IL-1 beta s are non-specifically released in very small quantities from the cytosol. On the other hand, the signal sequence-modified IL-1 beta s are glycosylated and efficiently secreted by the ER/Golgi pathway. The secreted, modified-mature protein is also biologically active, suggesting that this pathway has been bypassed for reasons other than maintaining the structural integrity of IL-1 beta. More likely the alternative pathway is a critical aspect of IL-1 biology. The differences in kinetics and quantity of IL-1 beta release from monocytic and COS cells suggest that COS cells lack critical components for the rapid release seen in monocytes." @default.
• W2000573257 created "2016-06-24" @default.
• W2000573257 creator A5058090183 @default.
• W2000573257 creator A5076433485 @default.
• W2000573257 date "1992-03-01" @default.
• W2000573257 modified "2023-10-17" @default.
• W2000573257 title "Further aspects of IL-1β secretion revealed by transfected monkey kidney cells" @default.
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• W2000573257 doi "https://doi.org/10.1016/1043-4666(92)90048-v" @default.
• W2000573257 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1633262" @default.
• W2000573257 hasPublicationYear "1992" @default.
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