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Analysis of podocyte adhesome proteomes

ABSTRACT: To elucidate potential mechanisms how EPB41L5 modulates integrin adhesion complex maturation, we performed quantitative SILAC-based integrin adhesome proteomics. For MS analysis of the podocyte adhesome, EPB41L5 or Luciferase (as negative control) was transient expressed in SILAC labeled podocytes by nucleofection (Amaxa Nucleofector, Lonza, Switzerland). Podocytes were seeded on cell culture dishes for 24 hours. Isolation of integrin adhesion complexes from podocytes was performed prior LC-MSMS analysis.In a second set of experiments adhesion complexes of collagen IV and fibronectin coated dishes were purified and analysed by LC-MSMS.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Podocyte (sensu Diptera)

SUBMITTER: Joern Dengjel

LAB HEAD: Joern Dengjel

PROVIDER: PXD023821 | Pride | 2021-08-05

REPOSITORIES: Pride

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EPB41L5 controls podocyte extracellular matrix assembly by adhesome-dependent force transmission.

Maier Jasmin I JI Rogg Manuel M Helmstädter Martin M Sammarco Alena A Schilling Oliver O Sabass Benedikt B Miner Jeffrey H JH Dengjel Jörn J Walz Gerd G Werner Martin M Huber Tobias B TB Schell Christoph C

Cell reports 20210301 12

The integrity of the kidney filtration barrier essentially relies on the balanced interplay of podocytes and the glomerular basement membrane (GBM). Here, we show by analysis of in vitro and in vivo models that a loss of the podocyte-specific FERM-domain protein EPB41L5 results in impaired extracellular matrix (ECM) assembly. By using quantitative proteomics analysis of the secretome and matrisome, we demonstrate a shift in ECM composition characterized by diminished deposition of core GBM compo ...[more]

PMID: 33761352

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