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Nutrients. 2019 Aug 3;11(8). pii: E1795. doi: 10.3390/nu11081795.

Identification of the Secreted Proteins Originated from Primary Human Hepatocytes and HepG2 Cells.

Author information

1
Department for Diagnostic Laboratory Medicine, Institute for Clinical Chemistry and Pathobiochemistry, University Hospital Tübingen, 72076 Tübingen, Germany. andras.franko@med.uni-tuebingen.de.
2
Institute for Diabetes Research and Metabolic Diseases of the Helmholtz Centre Munich, University of Tübingen, 72076 Tübingen, Germany. andras.franko@med.uni-tuebingen.de.
3
German Center for Diabetes Research (DZD e.V.), 85764 Neuherberg, Germany. andras.franko@med.uni-tuebingen.de.
4
German Center for Diabetes Research (DZD e.V.), 85764 Neuherberg, Germany.
5
Institute for Clinical Biochemistry and Pathobiochemistry of DDZ, University of Düsseldorf, 40225 Düsseldorf, Germany.
6
Department of Traumatology, BG Trauma Clinic, Siegfried Weller Institute for Trauma Research, Eberhard Karls Universität Tübingen, 72076 Tübingen, Germany.
7
Department of General, Visceral and Transplant Surgery, University Hospital Tübingen, 72076 Tübingen, Germany.
8
Institute for Diabetes Research and Metabolic Diseases of the Helmholtz Centre Munich, University of Tübingen, 72076 Tübingen, Germany.
9
Department of Internal Medicine IV, Division of Endocrinology, Diabetology, Nephrology, University Hospital Tübingen, 72076 Tübingen, Germany.
10
Department for Diagnostic Laboratory Medicine, Institute for Clinical Chemistry and Pathobiochemistry, University Hospital Tübingen, 72076 Tübingen, Germany.

Abstract

The liver plays a pivotal role in whole-body carbohydrate, lipid, and protein metabolism. One of the key regulators of glucose and lipid metabolism are hepatokines, which are found among the liver secreted proteins, defined as liver secretome. To elucidate the composition of the human liver secretome and identify hepatokines in primary human hepatocytes (PHH), we conducted comprehensive protein profiling on conditioned medium (CM) of PHH. Secretome profiling using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-MS/MS) identified 691 potential hepatokines in PHH. Subsequently, pathway analysis assigned these proteins to acute phase response, coagulation, and complement system pathways. The secretome of PHH was compared to the secreted proteins of the liver hepatoma cell line HepG2. Although the secretome of PHH and HepG2 cells show a high overlap, the HepG2 secretome rather mirrors the fetal liver with some cancer characteristics. Collectively, our study represents one of the most comprehensive secretome profiling approaches for PHH, allowing new insights into the composition of the secretome derived from primary human material, and points out strength and weakness of using HepG2 cell secretome as a model for the analysis of the human liver secretome.

KEYWORDS:

HepG2 cells; hepatokines; mass spectrometry; primary human hepatocytes; proteomics

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