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from the I'll-stay-in-bed-just-in-case dept.
To get over the flu, all it might take is a little extra brain protein and a lot more sleep. Researchers at Washington State University at Spokane have been trying to come up with another way to treat influenza beyond yearly vaccinations. James Krueger, a professor of physiology at WSU, says they were interested in seeing if sleep could improve recovery from illness.
“Grandmothers, and most people, give the advice, ‘Sleep will do you good, you’ll recover,’ but there’s not much scientific research,” Krueger tells Popular Science. In a new study, Krueger was able to back up his grandmother's advice. The team looked to a protein found only in the brain and in neurons called AcPb and an accessory protein called interleukin 1 — proteins that Krueger has been studying for a number of years. Interleukin 1 regulates sleep in healthy mammals, and Krueger found that when the AcPb protein in a sick animal interacts with the interleukin 1, it sends a signal to the immune system. This signal tells the body to sleep longer, so it can better recover from the virus.
http://www.popsci.com/proteins-found-brain-might-help-speed-flu-recovery-while-you-sleep
[Abstract]: http://www.sciencedirect.com/science/article/pii/S0889159114005108
(Score: 4, Informative) by SlimmPickens on Thursday January 15 2015, @08:50PM
"Here's [nih.gov] the relationship between interlukin, AcPb and sleep.
Abstract
Interleukin (IL)-1β is involved in several brain functions, including sleep regulation. It promotes non-rapid eye movement (NREM) sleep via the IL-1 type I receptor. IL-1β/IL-1 receptor complex signaling requires adaptor proteins, e.g., the IL-1 receptor brain-specific accessory protein (AcPb). We have cloned and characterized rat AcPb, which shares substantial homologies with mouse AcPb and, compared with AcP, is preferentially expressed in the brain. Furthermore, rat somatosensory cortex AcPb mRNA varied across the day with sleep propensity, increased after sleep deprivation, and was induced by somnogenic doses of IL-1β. Duration of NREM sleep was slightly shorter and duration of REM sleep was slightly longer in AcPb knockout than wild-type mice. In response to lipopolysaccharide, which is used to induce IL-1β, sleep responses were exaggerated in AcPb knockout mice, suggesting that, in normal mice, inflammation-mediated sleep responses are attenuated by AcPb. We conclude that AcPb has a role in sleep responses to inflammatory stimuli and, possibly, in physiological sleep regulation.
According to this [wikipedia.org] IL-1α and IL-1β are heavily related and bind to the same receptor. The bits relating to those two are as follows:
IL-1α is a “dual-function cytokine”, which means it plays a role in the nucleus by affecting transcription, apart from its extracellular receptor-mediated effects as a classical cytokine. In this group also belongs IL-33.[11]
IL-1α is synthesized as a precursor protein and it is constitutively stored in the cytoplasm of cells with mesenchymal origin and in epithelial cells. On the contrary, monocytes and macrophages do not contain preformed IL-1α precursors, but instead require de novo synthesis. IL-1α precursor is processed to a mature 17-kDa protein by a Ca2+-activated protease, calpain, by liberating the 16-kDa N-terminal propiece cleavage product (ppIL-1α), which contains a nuclear localization sequence (NLS), translocates to the nucleus and functions as a transcription factor. The precursor form of IL-1α, which has both the N-terminal and C-terminal receptor interacting domains, acts as a damage-associated molecular pattern (DAMP) molecule. DAMPs, also known as alarmins, are recognized by innate immunity cells by pattern recognition receptors (PRRs) and functions as danger signals for the immune system. In short, DAMPs are released from stressed cells, which undertake immune not-silent death (such as necrosis or pyroptosis) and their intracellular components are released into extracellular space. Because of misfolding and other oxidative changes of these molecules in the context of altered pH, they are recognized by innate immunity as molecules that should not be in extracellular space in physiological consequences. The reasons why the cell could be stressed are infection, injury, ischemia, hypoxia, acidosis and complement lysis. The IL-33 precursor form acts in the same way as a DAMP molecule.[11]
Interestingly, the inflammatory responses in the absence of infection (such as ischemia) are only dependent on IL-1α signaling via the Interleukin-1 receptor (IL-1R), rather than TLRs signaling. IL-1α also stimulates transcription and secretion of IL-1β from monocytes, so the initiator of immune responses is likely IL-1α precursor by induction of neutrophil infiltration. IL-1β seems to be an amplifier of inflammation by recruiting of macrophages in the context of sterile inflammation.[11][12][13]
IL-1α precursor and mature IL-1β lack a signal peptide which should direct them into the endoplasmic/Golgi-dependent secretion pathway and they are secreted by an unconventional protein secretion pathway, of which the mechanism and regulation are not known.[10]
IL-1β is synthesized as a precursor form protein only after stimulation, in contrast to IL-1α. Its expression is induced by transcription factor NF-κB after exposure of innate immune cells to alarmins. This occurs, for instance, after exposure of macrophages and dendritic cells to lipopolysaccharide (LPS), which binds to TLR4 and acts as pathogen-associated molecular pattern, which is another group of alarmins.[10][13]
The synthesis of IL-1β precursor (and IL-18) is induced by stimulation of innate immune cells by Toll-like receptors (TLRs) or RIG-like receptors (RLRs), but to gain the ability to bind to IL-1 receptor, the IL-1β precursor has to be cleaved by a cysteine protease called caspase-1. Caspase-1 needs to be activated by a formation called the inflammasome which is mediated by cytoplasmic pattern recognition receptor signaling. So, the secretion of IL-1β needs these two steps and activation of different receptors to be activated. Under special circumstances IL-1β can be processed also by other proteases, like during high neutrophilic inflammation.[10][14]
IL-18 is also synthesized as a precursor which is cleaved by caspase-1.[10]
So maybe this is why people with sleep deprivation suffer increased mortality.