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Full-Text Articles in Life Sciences
Spider Silk: A Brief Review And Prospectus On Research Linking Biomechanics And Ecology In Draglines And Orb Webs, Todd Blackledge
Spider Silk: A Brief Review And Prospectus On Research Linking Biomechanics And Ecology In Draglines And Orb Webs, Todd Blackledge
Todd A. Blackledge
Spiders construct a wide variety of silk structures, ranging from draglines to prey capture webs. Spider silks rank among the toughest materials known to science, and these material properties are critical for understanding how silk structures, such as webs, function. However, the mechanics of spider silk are often ignored in the study of webs. This review aims to show how the material properties of silk proteins, the structural properties of silk threads, and the architectures of webs ultimately interact to determine the function of orb webs during prey capture. I first provide a brief introduction into spider silk and how …
Structural Characterization Of Clusterin-Chaperone Client Protein Complexes, Amy Wyatt, Justin Yerbury, Mark Wilson
Structural Characterization Of Clusterin-Chaperone Client Protein Complexes, Amy Wyatt, Justin Yerbury, Mark Wilson
Mark R Wilson
Clusterin (CLU) is a potent extracellular chaperone that inhibits protein aggregation and precipitation otherwise caused by physical or chemical stresses (e.g. heat, reduction). This action involves CLU forming soluble high molecular weight (HMW) complexes with the client protein. Other than their unquantified large size, the physical characteristics of these complexes were previously unknown. In this study, HMW CLU-citrate synthase (CS), HMW CLU-fibrinogen (FGN), and HMW CLU-glutathione S-transferase (GST) complexes were generated in vitro, and their structures studied using size exclusion chromatography (SEC), ELISA, SDS-PAGE, dynamic light scattering (DLS), bisANS fluorescence, and circular dichroism spectrophotometry (CD). Densitometry of …
Effects Of Diets High In Whey, Soy, Red Meat And Milk Protein On Body Weight Maintenance In Diet-Induced Obesity In Mice, Xu-Feng Huang, Y Liu, Gita Rahardjo, Peter Mclennan, Linda Tapsell, William Buttemer
Effects Of Diets High In Whey, Soy, Red Meat And Milk Protein On Body Weight Maintenance In Diet-Induced Obesity In Mice, Xu-Feng Huang, Y Liu, Gita Rahardjo, Peter Mclennan, Linda Tapsell, William Buttemer
Xu-Feng Huang
This study examined the effects of different food sources of protein on energy intake, body weight maintenance, and on the responses of plasma leptin, insulin and adiponectin in chronic high-fat diet-induced obese mice. Obesity was induced in 47 mice with a high-fat diet for 20 weeks. They were divided into five diet groups to test the effects of a higher protein proportion (30% energy), achieved at the expense of carbohydrate. For the next eight weeks, four of the groups were fed diets of chow formulated with whey, soy, red meat or milk while the control group continued on their high-fat …
The Effect Of Small Molecules In Modulating The Chaperone Activity Of Alpha B-Crystallin Against Ordered And Disordered Protein Aggregation, Heath Ecroyd, John Carver
The Effect Of Small Molecules In Modulating The Chaperone Activity Of Alpha B-Crystallin Against Ordered And Disordered Protein Aggregation, Heath Ecroyd, John Carver
Heath Ecroyd
Protein aggregation can proceed via disordered or ordered mechanisms, with the latter being associated with amyloid fibril formation, which has been linked to a number of debilitating conditions including Alzheimer's, Parkinson's and Creutzfeldt-Jakob diseases. Small heat-shock proteins (sHsps), such as alpha B-crystallin, act as chaperones to prevent protein aggregation and are thought to play a key role in the prevention of protein-misfolding diseases. In this study, we have explored the potential for small molecules such as arginine and guanidine to affect the chaperone activity of alpha B-crystallin against disordered (amorphous) and ordered (amyloid fibril) forms of protein aggregation. The effect …
The Chaperone Action Of Clusterin And Its Putative Role In Quality Control Of Extracellular Protein Folding, Amy Wyatt, Justin Yerbury, Stephen Poon, Rebecca Dabbs, Mark Wilson
The Chaperone Action Of Clusterin And Its Putative Role In Quality Control Of Extracellular Protein Folding, Amy Wyatt, Justin Yerbury, Stephen Poon, Rebecca Dabbs, Mark Wilson
Mark R Wilson
The function(s) of clusterin may depend upon its topological location. A variety of intracellular "isoforms" of clusterin have been reported but further work is required to better define their identity. The secreted form of clusterin has a potent ability to inhibit both amorphous and amyloid protein aggregation. In the case of amorphous protein aggregation, clusterin forms stable, soluble high-molecular-weight complexes with misfolded client proteins. Clusterin expression is increased during many types of physiological and pathological stresses and is thought to function as an extracellular chaperone (EC). The pathology of a variety of serious human diseases is thought to arise as …
Heat Shock Protein 70 Inhibits Alpha-Synuclein Fibril Formation Via Preferential Binding To Prefibrillar Species, Mark Wilson, M. M. Dedmon, J. Christodoulou, Christopher Dobson
Heat Shock Protein 70 Inhibits Alpha-Synuclein Fibril Formation Via Preferential Binding To Prefibrillar Species, Mark Wilson, M. M. Dedmon, J. Christodoulou, Christopher Dobson
Mark R Wilson
No abstract provided.
The Acute Phase Protein Haptoglobin Is A Mammalian Extracellular Chaperone With An Action Similar To Clusterin, Justin Yerbury, Mark S Rybchyn, Simon B Easterbrook-Smith, C. Henriques, Mark Wilson
The Acute Phase Protein Haptoglobin Is A Mammalian Extracellular Chaperone With An Action Similar To Clusterin, Justin Yerbury, Mark S Rybchyn, Simon B Easterbrook-Smith, C. Henriques, Mark Wilson
Mark R Wilson
Haptoglobin (Hp) is an acidic glycoprotein present in most body fluids of humans and other mammals. Although the functions of Hp are not yet fully understood, the available evidence indicates that it is likely to play an important role in suppressing inflammatory responses. Some earlier work suggested that Hp might be a newly identified member of a small group of extracellular chaperones found at significant levels in human body fluids. Previously, the only well-characterized member of this group was clusterin, which shares functional similarities with the small heat-shock proteins. We report here that Hp specifically inhibited the precipitation of a …