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Full-Text Articles in Social and Behavioral Sciences
Endogenous Redox Activity In Mouse Spermatozoa And Its Role In Regulating The Tyrosine Phosphorylation Events Associated With Sperm Capacitation, Heath W. Ecroyd, Russell C. Jones, Robert J. Aitken
Endogenous Redox Activity In Mouse Spermatozoa And Its Role In Regulating The Tyrosine Phosphorylation Events Associated With Sperm Capacitation, Heath W. Ecroyd, Russell C. Jones, Robert J. Aitken
Heath Ecroyd
We investigated the role of endogenous redox activity in regulating the signal transduction pathway leading to tyrosine phosphorylation in mouse spermatozoa. Endogenous redox activity was monitored using a luminol-peroxidase chemiluminescent probe. Chemiluminescence increased in spermatozoa that were actively undergoing cAMP-mediated tyrosine phosphorylation events associated with capacitation and was inhibited in a dose-dependent manner by addition of catalase or diphenylene iodonium, both of which also inhibited tyrosine phosphorylation within the cell at points downstream of cAMP. Excluding bicarbonate from the incubation medium reduced the redox activity of sperm by 80-90% and dramatically reduced tyrosine phosphorylation. This study provides the first evidence …
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 Two Faced Nature Of Milk Casein Proteins: Amyloid Fibril Formation And Chaperone-Like Activity, David Thorn, Heath Ecroyd, John Carver
The Two Faced Nature Of Milk Casein Proteins: Amyloid Fibril Formation And Chaperone-Like Activity, David Thorn, Heath Ecroyd, John Carver
Heath Ecroyd
Molecular chaperones are a diverse group of proteins that stabilise partially folded target proteins to prevent their misfolding, aggregation and potential precipitation under conditions of cellular stress, e.g. elevated temperature. Protein aggregation, particularly the formation of highly ordered protein aggregates termed amyloid fibrils, is of considerable research interest because of its intimate association with a wide range of debilitating diseases, including Alzheimer's, Parkinson's and Huntington's diseases and type II diabetes. In this review, we discuss the ability of the milk casein proteins to act in a chaperone-like manner. This property is of biological importance since at least two of the …
Mimicking Phosphorylation Of Alphab-Crystallin Affects Its Chaperone Activity, Heath W. Ecroyd, Sarah Meehan, J Horwitz, Andrew Aquilina, J L Benesch, C V Robinson, Cait Macphee, John Carver
Mimicking Phosphorylation Of Alphab-Crystallin Affects Its Chaperone Activity, Heath W. Ecroyd, Sarah Meehan, J Horwitz, Andrew Aquilina, J L Benesch, C V Robinson, Cait Macphee, John Carver
Heath Ecroyd
No abstract provided.