Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer.

Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer. Research Abstract Details 

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Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer. Abstract Text:

All tumors examined to date contain mutations in mitochondrial DNA (mtDNA). In addition, depletion of mtDNA is reported in a variety of tumors. Mitochondrial dysfunction resulting from changes in mtDNA invokes mitochondria-to-nucleus retrograde response in human cells. To identify proteins involved in retrograde response and their potential role in tumorigenesis, we carried out a comparative proteomic analysis using a cell line in which the mitochondrial genome was completely depleted (rho(0) cells lacking all mtDNA-encoded protein subunits), a cybrid cell line in which mtDNA was restored, and the parental cell line. Our comparative proteomic approach revealed marked changes in the cellular proteome and led us to identify quantitative changes in expression of several proteins. We found that subunits of complex I and complex III, molecular chaperones, and a protein involved in cell cycle control were downregulated and Inosine 5'-monophosphate dehydrogenase type 2 (IMPDH2) involved in nucleotide biosynthesis was upregulated in rho(0) cells. Our findings demonstrate that the expression of proteins is restored to wild type level by transfer of wild type mitochondria to rho(0) cells, suggesting that these proteins play key roles in retrograde response. To determine a potential role for identified retrograde responsive proteins in tumorigenesis, we analyzed the expression of UQCRC1 gene (encoding ubiquinol cytochrome-c reductase core protein I) in breast and ovarian tumors. We found that (1) UQCRC1 was highly expressed in breast (74%) and ovarian tumors (34%) and (2) the expression positively correlated with cytochrome c-oxidase (COXII) encoded by mtDNA. Our study opens an avenue for identification of retrograde proteins as potential tumor suppressors or oncogenes involved in carcinogenesis.

Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer. Publishing Authors By Initials

For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins research

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MEDLINE DATE:

Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Cancer biology & therapy

VOLUME: 5

Page Numbers: 967-75

Journal Abbreviation: Cancer Biol. Ther.

ISSN: 1538-4047

DAY: 2

MONTH: 08

YEAR: 2006

Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101137842

Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer. Keywords Mesh Terms:

KEYWORDS: rho GTP-Binding Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer. Information

Substance Name: rho GTP-Binding Proteins

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for Proteomic analysis of mitochondria-to-nucleus retrograde response in human cancer.

AFFILIATION: Department of Cancer Genetics, Roswell Park Cancer Institute, Buffalo, New York, USA.

Country: United States

AGENCY: United States NCI

GRANT: R01 CA113655

ACRONYM: CA

MEDLINETA: Cancer Biol Ther

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