Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors

We have compared the microsomal protein composition of eight malignant and six benign adrenocortical tumors with proteomic methods. IGF2 had increased level in the malignant tumors, confirming previous microarray studies on the same material. Aldolase A, a glycolytic enzyme, also showed increased le...

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Main Authors:	Kjellin, Hanna, Johansson, Henrik, Höög, Anders, Lehtiö, Janne, Jakobsson, Per-Johan, Kjellman, Magnus
Format:	Online
Language:	English
Published:	Public Library of Science 2014
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3912167/

id	pubmed-3912167
recordtype	oai_dc
spelling	pubmed-39121672014-02-04 Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors Kjellin, Hanna Johansson, Henrik Höög, Anders Lehtiö, Janne Jakobsson, Per-Johan Kjellman, Magnus Research Article We have compared the microsomal protein composition of eight malignant and six benign adrenocortical tumors with proteomic methods. IGF2 had increased level in the malignant tumors, confirming previous microarray studies on the same material. Aldolase A, a glycolytic enzyme, also showed increased levels in the malignant tissue compared to the benign. Additionally, several proteins belonging to complex I in the mitochondrial respiration chain showed decreased levels in the malignant tissue. Taken together, this may indicate a shift in energy metabolism where glycolysis may be favored over tight coupling of glycolysis and mitochondrial respiration, a phenomenon known as the Warburg effect. One of the complex I proteins that showed decreased levels in the malignant tissue was GRIM-19. This protein has been suggested as a tumor suppressive protein by being a negative regulator of STAT3. In summary, an analysis of the microsomal proteome in adrenocortical tumors identifies groups of proteins as well as specific proteins differentially expressed in the benign and malignant forms. These proteins shed light on the biology behind malignancy and could delineate future drug targets. Public Library of Science 2014-02-03 /pmc/articles/PMC3912167/ /pubmed/24498411 http://dx.doi.org/10.1371/journal.pone.0087951 Text en © 2014 Kjellin et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Kjellin, Hanna Johansson, Henrik Höög, Anders Lehtiö, Janne Jakobsson, Per-Johan Kjellman, Magnus
spellingShingle	Kjellin, Hanna Johansson, Henrik Höög, Anders Lehtiö, Janne Jakobsson, Per-Johan Kjellman, Magnus Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors
author_facet	Kjellin, Hanna Johansson, Henrik Höög, Anders Lehtiö, Janne Jakobsson, Per-Johan Kjellman, Magnus
author_sort	Kjellin, Hanna
title	Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors
title_short	Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors
title_full	Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors
title_fullStr	Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors
title_full_unstemmed	Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors
title_sort	differentially expressed proteins in malignant and benign adrenocortical tumors
description	We have compared the microsomal protein composition of eight malignant and six benign adrenocortical tumors with proteomic methods. IGF2 had increased level in the malignant tumors, confirming previous microarray studies on the same material. Aldolase A, a glycolytic enzyme, also showed increased levels in the malignant tissue compared to the benign. Additionally, several proteins belonging to complex I in the mitochondrial respiration chain showed decreased levels in the malignant tissue. Taken together, this may indicate a shift in energy metabolism where glycolysis may be favored over tight coupling of glycolysis and mitochondrial respiration, a phenomenon known as the Warburg effect. One of the complex I proteins that showed decreased levels in the malignant tissue was GRIM-19. This protein has been suggested as a tumor suppressive protein by being a negative regulator of STAT3. In summary, an analysis of the microsomal proteome in adrenocortical tumors identifies groups of proteins as well as specific proteins differentially expressed in the benign and malignant forms. These proteins shed light on the biology behind malignancy and could delineate future drug targets.
publisher	Public Library of Science
publishDate	2014
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3912167/
_version_	1612054199769497600

Differentially Expressed Proteins in Malignant and Benign Adrenocortical Tumors

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