Universität zu Köln

Rinschen, Markus M., Schroeter, Christina B., Koehler, Sybille, Ising, Christina ORCID: 0000-0002-7267-3488, Schermer, Bernhard ORCID: 0000-0002-5194-9000, Kann, Martin, Benzing, Thomas and Brinkkoetter, Paul T. (2016). Quantitative deep mapping of the cultured podocyte proteome uncovers shifts in proteostatic mechanisms during differentiation. Am. J. Physiol.-Cell Physiol., 311 (3). S. C404 - 14. BETHESDA: AMER PHYSIOLOGICAL SOC. ISSN 1522-1563

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Abstract

The renal filtration barrier is maintained by the renal podocyte, an epithelial postmitotic cell. Immortalized mouse podocyte cell lines-both in the differentiated and undifferentiated state-are widely utilized tools to estimate podocyte injury and cytoskeletal rearrangement processes in vitro. Here, we mapped the cultured podocyte proteome at a depth of more than 8,800 proteins and quantified 7,240 proteins. Copy numbers of proteins mutated in forms of hereditary nephrotic syndrome or focal segmental glomerulosclerosis (FSGS) were assessed. We found that cultured podocytes express abundant copy numbers of endogenous receptors, such as tyrosine kinase membrane receptors, the G protein-coupled receptor (GPCR), NPR3 (ANP receptor), and several poorly characterized GPCRs. The data set was correlated with deep mapping mRNA sequencing (mR-NAseq) data from the native mouse podocyte, the native mouse podocyte proteome and staining intensities from the human protein atlas. The generated data set was similar to these previously published resources, but several native and high-abundant podocyte-specific proteins were not identified in the data set. Notably, this data set detected general perturbations in proteostatic mechanisms as a dominant alteration during podocyte differentiation, with high proteasome activity in the undifferentiated state and markedly increased expression of lysosomal proteins in the differentiated state. Phosphoproteomics analysis of mouse podocytes at a resolution of more than 3,000 sites suggested a preference of phosphorylation of actin filament-associated proteins in the differentiated state. The data set obtained here provides a resource and provides the means for deep mapping of the native podocyte proteome and phosphoproteome in a similar manner.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Rinschen, Markus M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Schroeter, Christina B. UNSPECIFIED UNSPECIFIED UNSPECIFIED Koehler, Sybille UNSPECIFIED UNSPECIFIED UNSPECIFIED Ising, Christina UNSPECIFIED orcid.org/0000-0002-7267-3488 UNSPECIFIED Schermer, Bernhard UNSPECIFIED orcid.org/0000-0002-5194-9000 UNSPECIFIED Kann, Martin UNSPECIFIED UNSPECIFIED UNSPECIFIED Benzing, Thomas UNSPECIFIED UNSPECIFIED UNSPECIFIED Brinkkoetter, Paul T. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-263941
DOI:	10.1152/ajpcell.00121.2016
Journal or Publication Title:	Am. J. Physiol.-Cell Physiol.
Volume:	311
Number:	3
Page Range:	S. C404 - 14
Date:	2016
Publisher:	AMER PHYSIOLOGICAL SOC
Place of Publication:	BETHESDA
ISSN:	1522-1563
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language PHOSPHOPROTEOMIC ANALYSIS; GLOMERULAR PROTEIN; COUPLED RECEPTOR; GENE-EXPRESSION; CELL CONTACTS; REVEALS; KIDNEY; MOUSE; PHOSPHORYLATION; LOCALIZATION Multiple languages Cell Biology; Physiology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/26394