Breaking the curse of the AGEs

Article Abstract:

AGEs or advanced-glycation end-products, formed when initial glycation products (protein adducts) attach irreversibly to stable proteins, represent exposure to glucose over time. Proteins modified by the AGEs cause tissue damage at the molecular level. This is accelerated in diabetic patients. In animal models of diabetes, aminoguanidine can prevent AGE formation by trapping the initial glycation adducts. N-phenacylthiazolium bromide cleaves the diketone bridge and breaks the crosslinks in the AGE structure. These methods may be useful in relieving the effects of non-diabetic aging.

Care and treatment, Analysis, Diabetes, Diabetes mellitus, Blood sugar, Blood glucose

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A signature motif in transcriptional co-activators mediates binding to nuclear receptors

Article Abstract:

The transcriptional and DNA-binding properties of the nuclear-receptor superfamily is modified by the binding of retinoids, vitamins and lipophilic hormones, producing inhibition or activation of target genes. Ligand-binding encourages nuclear receptor changes and induces their association with a variety of nuclear proteins, including SRC-1. A study designed to show that a signature motif, LXXLL, present in various nuclear proteins, facilitates binding to liganded nuclear receptors is presented.

Cell nuclei, Cell nucleus, DNA binding proteins

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Engineering galactose-binding activity into a C-type mannose-binding protein

Article Abstract:

Switching the position of a single amide group in the sequence of a mannose-binding carbohydrate recognition domain (CRD) can alter its binding activity so it has a higher binding affinity for galactose than for mannose. These experiments on calcium-dependent CRDs show the importance of sequence residues in the selection and binding of sugars.

Carbohydrate metabolism, Galactose metabolism

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