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Interleukin 1: The patterns of translation and intracellular distribution support alternative secretory mechanisms by Frazier T. Stevenson; Frank Torrano; Richard M. Locksley; David H. Lovett is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Interleukin‐1 (IL‐1) is synthesized as a 31 kDa precursor protein, whose multiple extracellular activities are attributed to receptor binding of a processed, carboxyterminal 17 kDa peptide. Unlike other secreted proteins, the IL‐1 precursor lacks a hydrophobic leader sequence and is not found in organelles composing the classical secretory pathway. In order to further clarify the intracellular processing of IL‐1, we studied its site of synthesis in human monocytes. Secreted and integral membrane proteins are translated on membrane‐bound polyribosomes, while intracellular proteins are translated on free polyribosomes. Free and membrane‐bound polysomes were isolated from Lipid A‐stimulated monocyte lysates and immunoblotted using antibodies specific to the N‐terminal regions of the IL‐1α and β precursors. Free polysome fractions showed multiple small bands consistent with nascent peptide chains; membrane‐bound polysomes yielded no detectable IL‐1. Polysome fractions were then analyzed by immunoelectron microscopy; nascent IL‐1α and β peptide chains were readily seen emerging from cytoskeletal‐associated free polyribosomes, but not membrane‐bound polyribosomes. Electron mi

Who reads Interleukin 1: The patterns of translation and intracellular distribution support alternative secretory mechanisms?

Author

Frazier T. Stevenson; Frank Torrano; Richard M. Locksley; David H. Lovett

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0021-9541)

Published

1992

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)