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PLoS One. 2014 Feb 3;9(2):e87951. doi: 10.1371/journal.pone.0087951. eCollection 2014.

Differentially expressed proteins in malignant and benign adrenocortical tumors.

Author information

1
Rheumatology Unit, Department of Medicine, Karolinska Institutet, Stockholm, Sweden ; Department of Molecular Medicine and Surgery, Karolinska Institutet, Stockholm, Sweden ; Science for Life Laboratory, Cancer Proteomics Mass Spectrometry, Karolinska Institutet, Solna, Sweden.
2
Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden ; Science for Life Laboratory, Cancer Proteomics Mass Spectrometry, Karolinska Institutet, Solna, Sweden.
3
Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
4
Rheumatology Unit, Department of Medicine, Karolinska Institutet, Stockholm, Sweden.
5
Department of Breast- and Endocrine Surgery, Section of Endocrine and Sarcoma Surgery, Karolinska University Hospital, Stockholm, Sweden.

Abstract

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.

PMID:
24498411
PMCID:
PMC3912167
DOI:
10.1371/journal.pone.0087951
[Indexed for MEDLINE]
Free PMC Article

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