Upregulated Phospholipase D Activity Towards Glycosylphosphatidylinositol-Anchored Proteins in Micelle-Like Serum Complexes in Diabetic/Obese Rats and Humans.

Upregulated Phospholipase D Activity Towards Glycosylphosphatidylinositol-Anchored Proteins in Micelle-Like Serum Complexes in Diabetic/Obese Rats and Humans. Am J Physiol Endocrinol Metab. 2020 Jan 21;: Authors: Müller GA, Tschöp MH, Müller TD Abstract Glycosylphosphatidylinositol-anchored proteins (GPI-AP) with the complete glycolipid anchor attached are present in rat and human serum at amounts which are lower in insulin-resistant/obese rats compared to normal ones. These findings prompted further evaluation of the potential of full-length GPI-AP for the prediction and stratification of metabolically deranged states. A comparison of the signatures of horizontal surface acoustic waves which were generated by full-length GPI-AP in course of their specific capture by and subsequent dissociation from a chip-based sensor between those from rat serum and those reconstituted into lipidic structures strongly argues for expression of full-length GPI-AP in serum in micelle-like complexes in concert with phospholipids, lysophospholipids and cholesterol. Both the reconstituted and the rat serum complexes were highly sensitive towards mechanical forces, such as vibration. Furthermore, full-length GPI-AP reconstituted into micelle-like complexes represented efficient substrates for cleavage by serum glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD). Serum GPI-PLD activity towards full-length GPI-AP in micelle-like complexes, bu...
Source: Am J Physiol Endocri... - Category: Endocrinology Authors: Tags: Am J Physiol Endocrinol Metab Source Type: research