Trehalose and 6-aminohexanoic acid stabilize and renature glucose-6-phosphate dehydrogenase inactivated by glycation and by guanidinium hydrochloride
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and
Abstract
A number of naturally occurring small organic molecules, primarily involved in maintaining osmotic pressure in the cell, display chaperone-like activity, stabilizing the native conformation of proteins and protecting them from various kinds of stress. Most of them are sugars, polyols, amino acids or methylamines. In addition to their intrinsic protein-stabilizing activity, these small organic stress molecules regulate the activity of some molecular chaperones, and may stabilize the folded state of proteins involved in unfolding or in misfolding diseases, such as Alzheimer's and Parkinson's diseases, or α1-antitrypsin deficiency and cystic fibrosis, respectively. Similar to molecular chaperones, most of these compounds have no substrate specificity, but some specifically stabilize certain proteins, e.g., 6-aminohexanoic acid (AHA) stabilizes apolipoprotein A. In the present work, the capacity of 6-aminohexanoic acid to stabilize non-specifically other proteins is demonstrated. Both trehalose and AHA significantly protect glucose-6-phosphate dehydrogenase (G6PD) against glycation-induced inactivation, and renatured enzyme already inactivated by glycation and by guanidinium hydrochloride (GuHCl). To the best of our knowledge, there are no data on the effect of these compounds on protein glycation. The correlation between the recovery of enzyme activity and structural changes indicated by fluorescence spectroscopy and Western blotting contribute to better understanding of the protein stabilization mechanism.
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Articles in the same Issue
- Signaling in Biochemical Pharmacology and Toxicology
- Oncogenic Ras in tumour progression and metastasis
- Phosphoinositide 3-kinase signaling in the cellular response to oxidative stress
- Doxorubicin induces EGF receptor-dependent downregulation of gap junctional intercellular communication in rat liver epithelial cells
- TGFβ-induced focal complex formation in epithelial cells is mediated by activated ERK and JNK MAP kinases and is independent of Smad4
- On the mechanism of alkylphosphocholine (APC)-induced apoptosis in tumour cells
- Self-organization versus Watchmaker: stochastic dynamics of cellular organization
- Varicella-zoster virus IE63 protein represses the basal transcription machinery by disorganizing the pre-initiation complex
- Trehalose and 6-aminohexanoic acid stabilize and renature glucose-6-phosphate dehydrogenase inactivated by glycation and by guanidinium hydrochloride
- Quercetin metabolism in vital and apoptotic human leukaemia cells
- One of the Ca2+ binding sites of recoverin exclusively controls interaction with rhodopsin kinase
- Enzymatic profiling of human kallikrein 14 using phage-display substrate technology
- A new selective substrate for cathepsin E based on the cleavage site sequence of α2-macroglobulin