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Age-dependent membrane release and degradation of full-length glycosylphosphatidylinositol-anchored proteins in rats.
Mech Ageing Dev. 2020 Jul 03; 190:111307.MA

Abstract

Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) are associated with the surface of eucaryotic cells only through a covalently coupled carboxy-terminal GPI glycolipid structure which is anchored at the outer leaflet of plasma membranes. This mode of membrane association may be responsible for the recent observations that full-length GPI-APs harbouring the complete GPI anchor are (i) released from isolated rat adipocytes in vitro and (ii) expressed in rat and human serum. The upregulation of the adipocyte release in response to increased cell size and blood glucose/insulin levels of the donor rats and downregulation of the expression in serum of insulin resistant and diabetic rats have been reconciled with enhanced degradation of the full-length GPI-APs released into micelle-like complexes together with (lyso) phospholipids and cholesterol by serum GPI-specific phospholipase D (GPI-PLD). Here by using a sensitive and reliable sensing method for full-length GPI-APs, which relies on surface acoustic waves propagating over microfluidic chips, the upregulation of (i) the release of the full-length GPI-APs CD73, alkaline phosphatase and CD55 from isolated adipocyte plasma membranes monitored in a "lab-on-the-chip" configuration, (ii) their release from isolated rat adipocytes into the incubation medium and (iii) the lipolytic cleavage of their GPI anchors in serum was demonstrated to increase with age (3-16 weeks) and body weight (87-477 g) of (healthy) donor rats. In contrast, the amount of full-length GPI-APs in rat serum, as determined by chip-based sensing, turned out to decline with age/body weight. These correlations suggest that age-/weight-induced alterations (in certain biophysical/biochemical characteristics) of plasma membranes are responsible for the release of full-length GPI-APs which becomes counteracted by elevated GPI-PLD activity in serum. Thus, sensitive and specific measurement of these GPI-AP-relevant parameters may be useful for monitoring of age-related cell surface changes, in general, and diseases, in particular.

Authors+Show Affiliations

Institute for Diabetes and Obesity, Helmholtz Diabetes Center (HDC) at Helmholtz Zentrum München, German Research Center for Environmental Health (GmbH), Oberschleissheim, Germany; German Center for Diabetes Research (DZD), Oberschleissheim, Germany; Department Biology I, Genetics, Ludwig-Maximilians-Universität München, Planegg, Martinsried, Germany. Electronic address: guenter.mueller@helmholtz-muenchen.de.Institute for Diabetes and Obesity, Helmholtz Diabetes Center (HDC) at Helmholtz Zentrum München, German Research Center for Environmental Health (GmbH), Oberschleissheim, Germany; German Center for Diabetes Research (DZD), Oberschleissheim, Germany; Division of Metabolic Diseases, Department of Medicine, Technische Universität München, München, Germany.German Center for Diabetes Research (DZD), Oberschleissheim, Germany; Division of Metabolic Diseases, Department of Medicine, Technische Universität München, München, Germany; Helmholtz Zentrum München, German Research Center for Environmental Health (GmbH), Oberschleissheim, Germany.Institute for Diabetes and Obesity, Helmholtz Diabetes Center (HDC) at Helmholtz Zentrum München, German Research Center for Environmental Health (GmbH), Oberschleissheim, Germany; German Center for Diabetes Research (DZD), Oberschleissheim, Germany; Department of Pharmacology and Experimental Therapy, Institute of Experimental and Clinical Pharmacology and Toxicology, Eberhard Karls University Hospitals and Clinics, Tübingen, Germany.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32628941

Citation

Müller, Günter A., et al. "Age-dependent Membrane Release and Degradation of Full-length Glycosylphosphatidylinositol-anchored Proteins in Rats." Mechanisms of Ageing and Development, vol. 190, 2020, p. 111307.
Müller GA, Ussar S, Tschöp MH, et al. Age-dependent membrane release and degradation of full-length glycosylphosphatidylinositol-anchored proteins in rats. Mech Ageing Dev. 2020;190:111307.
Müller, G. A., Ussar, S., Tschöp, M. H., & Müller, T. D. (2020). Age-dependent membrane release and degradation of full-length glycosylphosphatidylinositol-anchored proteins in rats. Mechanisms of Ageing and Development, 190, 111307. https://doi.org/10.1016/j.mad.2020.111307
Müller GA, et al. Age-dependent Membrane Release and Degradation of Full-length Glycosylphosphatidylinositol-anchored Proteins in Rats. Mech Ageing Dev. 2020 Jul 3;190:111307. PubMed PMID: 32628941.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Age-dependent membrane release and degradation of full-length glycosylphosphatidylinositol-anchored proteins in rats. AU - Müller,Günter A, AU - Ussar,Siegfried, AU - Tschöp,Matthias H, AU - Müller,Timo D, Y1 - 2020/07/03/ PY - 2020/03/18/received PY - 2020/06/18/revised PY - 2020/06/29/accepted PY - 2020/7/7/pubmed PY - 2020/7/7/medline PY - 2020/7/7/entrez KW - Glycosylphosphatidylinositol-anchored proteins KW - Lipid rafts KW - Lipolytic cleavage KW - Phospholipase D KW - Plasma membrane fluidity KW - Rat adipocytes KW - Rat serum SP - 111307 EP - 111307 JF - Mechanisms of ageing and development JO - Mech. Ageing Dev. VL - 190 N2 - Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) are associated with the surface of eucaryotic cells only through a covalently coupled carboxy-terminal GPI glycolipid structure which is anchored at the outer leaflet of plasma membranes. This mode of membrane association may be responsible for the recent observations that full-length GPI-APs harbouring the complete GPI anchor are (i) released from isolated rat adipocytes in vitro and (ii) expressed in rat and human serum. The upregulation of the adipocyte release in response to increased cell size and blood glucose/insulin levels of the donor rats and downregulation of the expression in serum of insulin resistant and diabetic rats have been reconciled with enhanced degradation of the full-length GPI-APs released into micelle-like complexes together with (lyso) phospholipids and cholesterol by serum GPI-specific phospholipase D (GPI-PLD). Here by using a sensitive and reliable sensing method for full-length GPI-APs, which relies on surface acoustic waves propagating over microfluidic chips, the upregulation of (i) the release of the full-length GPI-APs CD73, alkaline phosphatase and CD55 from isolated adipocyte plasma membranes monitored in a "lab-on-the-chip" configuration, (ii) their release from isolated rat adipocytes into the incubation medium and (iii) the lipolytic cleavage of their GPI anchors in serum was demonstrated to increase with age (3-16 weeks) and body weight (87-477 g) of (healthy) donor rats. In contrast, the amount of full-length GPI-APs in rat serum, as determined by chip-based sensing, turned out to decline with age/body weight. These correlations suggest that age-/weight-induced alterations (in certain biophysical/biochemical characteristics) of plasma membranes are responsible for the release of full-length GPI-APs which becomes counteracted by elevated GPI-PLD activity in serum. Thus, sensitive and specific measurement of these GPI-AP-relevant parameters may be useful for monitoring of age-related cell surface changes, in general, and diseases, in particular. SN - 1872-6216 UR - https://www.unboundmedicine.com/medline/citation/32628941/Age-dependent_membrane_release_and_degradation_of_full-length_glycosylphosphatidylinositol-anchored_proteins_in_rats L2 - https://linkinghub.elsevier.com/retrieve/pii/S0047-6374(20)30103-2 DB - PRIME DP - Unbound Medicine ER -
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