Clearance kinetics and matrix binding partners of the receptor for advanced glycation end products

Autor: N.S. Mason, Judson M. Englert, Pavle S. Milutinovic, Tim D. Oury, Louis J. Sparvero, Lauren T. Crum, Lasse Ramsgaard, Jan J. Enghild, Michael T. Lotze
Jazyk: angličtina
Rok vydání: 2014
Předmět:
Proteomics
Male
Receptor for Advanced Glycation End Products
lcsh:Medicine
Plasma protein binding
Pharmacology
Biochemistry
RAGE (receptor)
Extracellular matrix
Mice
0302 clinical medicine
Laminin
Glycation
Molecular Cell Biology
Tissue Distribution
Biomacromolecule-Ligand Interactions
Receptors
Immunologic
Receptor
lcsh:Science
Lung
0303 health sciences
Extracellular Matrix Proteins
Multidisciplinary
biology
Chemistry
3. Good health
Extracellular Matrix
medicine.anatomical_structure
030220 oncology & carcinogenesis
Injections
Intravenous
Cytochemistry
Cellular Structures and Organelles
Injections
Intraperitoneal
Research Article
Protein Binding
Collagen Type IV
Serum albumin
Biological Availability
Collagen Type I
03 medical and health sciences
Administration
Inhalation
medicine
Animals
Humans
Protein Interactions
030304 developmental biology
Basement membrane
lcsh:R
Biology and Life Sciences
Proteins
Biological Transport
Cell Biology
Fibronectins
Mice
Inbred C57BL
Kinetics
Metabolism
Solubility
Immunology
biology.protein
lcsh:Q
Zdroj: PLoS ONE, Vol 9, Iss 3, p e88259 (2014)
PLoS ONE
Milutinovic, P S, Englert, J M, Crum, L T, Mason, N S, Ramsgaard, L, Enghild, J J, Sparvero, L J, Lotze, M T & Oury, T D 2014, ' Clearance kinetics and matrix binding partners of the receptor for advanced glycation end products ', PLOS ONE, vol. 9, no. 3, pp. e88259 . https://doi.org/10.1371/journal.pone.0088259
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0088259
Popis: Elucidating the sites and mechanisms of sRAGE action in the healthy state is vital to better understand the biological importance of the receptor for advanced glycation end products (RAGE). Previous studies in animal models of disease have demonstrated that exogenous sRAGE has an anti-inflammatory effect, which has been reasoned to arise from sequestration of pro-inflammatory ligands away from membrane-bound RAGE isoforms. We show here that sRAGE exhibits in vitro binding with high affinity and reversibly to extracellular matrix components collagen I, collagen IV, and laminin. Soluble RAGE administered intratracheally, intravenously, or intraperitoneally, does not distribute in a specific fashion to any healthy mouse tissue, suggesting against the existence of accessible sRAGE sinks and receptors in the healthy mouse. Intratracheal administration is the only effective means of delivering exogenous sRAGE to the lung, the organ in which RAGE is most highly expressed; clearance of sRAGE from lung does not differ appreciably from that of albumin.
Databáze: OpenAIRE
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