title: Proteomic definitions of basement membrane composition in health and disease.
abstract: Basement membranes are formed from condensed networks of extracellular matrix (ECM) proteins. These structures underlie all epithelial, mesothelial and endothelial sheets and provide an essential structural scaffold. Candidate-based investigations have established that predominant components of basement membranes are laminins, collagen type IV, nidogens and heparan sulphate proteoglycans. More recently, global proteomic approaches have been applied to investigate ECM and these analyses confirm tissue-specific ECM proteomes with a high degree of complexity. The proteomes consist of structural as well as regulatory ECM proteins such as proteases and growth factors. This review is focused on the proteomic analysis of basement membranes and illustrates how this approach can be used to build our understanding of ECM regulation in health and disease.
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, UK; Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, Manchester, UK.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Randles
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, UK.
authors.forename: Martin J
authors.initials: MJ
authors.lastname: Humphries
authors.affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, UK; Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, Manchester, UK; Department of Paediatric Nephrology, Central Manchester University Hospitals NHS Foundation Trust (CMFT), Manchester Academic Health Science Centre (MAHSC), Manchester, UK. Electronic address: Rachel.Lennon@manchester.ac.uk.
authors.forename: Rachel
authors.initials: R
authors.lastname: Lennon
mesh_terms: D018171:Agrin / Q000235:genetics / Q000378:metabolism; D000818:Animals; D017544:Aortic Aneurysm, Abdominal / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D001485:Basement Membrane / Q000737:chemistry / Q000378:metabolism* / Q000473:pathology; D024141:Collagen Type IV / Q000235:genetics / Q000378:metabolism; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism / Q000473:pathology; D005786:Gene Expression Regulation; D019812:Heparan Sulfate Proteoglycans / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007797:Laminin / Q000235:genetics / Q000378:metabolism; D008181:Lupus Nephritis / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D009369:Neoplasms / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D040901:Proteomics; D015398:Signal Transduction
chemical_list: D018171:Agrin; D024141:Collagen Type IV; D019812:Heparan Sulfate Proteoglycans; D007797:Laminin; D008562:Membrane Glycoproteins; D020033:Protein Isoforms; C029967:nidogen
keywords: Bioinformatics; Degradomics; Enrichment; Extracellular matrix; Fractionation; Glycoproteomics; Mass spectrometry; Proteomics; Quantification; Systems biology