Medicine and Health Sciences | Open Access Articles

Probiotics: 100 Years (1907-2007) After Elie Metchnikoff's Observations, Kingsley Anukam, Gregor Reid

Kingsley C Anukam

No abstract provided.

Invited Review: Heat Shock Proteins And Exercise: A Primer, Earl Noble, Kevin Milne, C.W. Melling

Jamie Melling

Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this review …

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Structural And Dynamic Basis Of Phospholamban And Sarcolipin Inhibition Of Ca2+-Atpase, Nathaniel J. Traaseth, Kim N. Ha, Raffaello Verardi, Lei Shi, Jarrod J. Buffy, Larry R. Masterson, Gianluigi Veglia

Larry Masterson

Phospholamban (PLN) and sarcolipin (SLN) are two single-pass membrane proteins that regulate Ca2+-ATPase (SERCA), an ATP-driven pump that translocates calcium ions into the lumen of the sarcoplasmic reticulum, initiating muscle relaxation. Both proteins bind SERCA through intramembrane interactions, impeding calcium translocation. While phosphorylation of PLN at Ser-16 and/or Thr-17 reestablishes calcium flux, the regulatory mechanism of SLN remains elusive. SERCA has been crystallized in several different states along the enzymatic reaction coordinates, providing remarkable mechanistic information; however, the lack of high-resolution crystals in the presence of PLN and SLN limits the current understanding of the regulatory mechanism. This …