Progressive decrease of phosphocreatine, creatine and creatine kinase in skeletal muscle upon transformation to sarcoma
Autor: | Patra, Subrata, Bera, Soumen, SinhaRoy, Soumya, Ghoshal, Sarani, Ray, Subhankar, Basu, Abhimanyu, Schlattner, Uwe, Wallimann, Theo, Ray, Manju |
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Přispěvatelé: | Department of Biological Chemistry, Kolkata University, Department of Surgery, SSKM Hospital, Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Biology, Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)-Institute of Cell Biology, Hamant, Sarah |
Jazyk: | angličtina |
Rok vydání: | 2008 |
Předmět: |
Phosphocreatine
Immunoblotting Creatine Kinase Mitochondrial Form Adenocarcinoma MESH: Neoplasms Muscle Tissue MESH: Phosphocreatine MESH: Sarcoma Experimental Mice Neoplasms Muscle Tissue Stomach Neoplasms Creatine Kinase BB Form [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Animals Humans MESH: Animals MESH: Creatine Kinase Mitochondrial Form [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology RNA Messenger Muscle Skeletal Creatine Kinase MESH: Mice MESH: RNA Messenger MESH: Muscle Skeletal MESH: Humans MESH: Creatine Kinase MESH: Immunoblotting MESH: Creatine MESH: Adenocarcinoma Creatine Kinase MM Form Sarcoma MESH: Stomach Neoplasms MESH: Creatine Kinase BB Form Creatine Cell Transformation Neoplastic MESH: Cell Transformation Neoplastic MESH: Creatine Kinase MM Form MESH: Sarcoma Disease Progression MESH: Disease Progression Sarcoma Experimental Colorectal Neoplasms MESH: Colorectal Neoplasms |
Zdroj: | FEBS Journal FEBS Journal, Wiley, 2008, 275 (12), pp.3236-47. ⟨10.1111/j.1742-4658.2008.06475.x⟩ |
ISSN: | 1742-464X 1742-4658 |
DOI: | 10.1111/j.1742-4658.2008.06475.x⟩ |
Popis: | International audience; In vertebrates, phosphocreatine and ATP are continuously interconverted by the reversible reaction of creatine kinase in accordance with cellular energy needs. Sarcoma tissue and its normal counterpart, creatine-rich skeletal muscle, are good source materials to study the status of creatine and creatine kinase with the progression of malignancy. We experimentally induced sarcoma in mouse leg muscle by injecting either 3-methylcholanthrene or live sarcoma 180 cells into one hind leg. Creatine, phosphocreatine and creatine kinase isoform levels decreased as malignancy progressed and reached very low levels in the final stage of sarcoma development; all these parameters remained unaltered in the unaffected contralateral leg muscle of the same animal. Creatine and creatine kinase levels were also reduced significantly in frank malignant portions of human sarcoma and gastric and colonic adenocarcinoma compared with the distal nonmalignant portions of the same samples. In mice, immunoblotting with antibodies against cytosolic muscle-type creatine kinase and sarcomeric mitochondrial creatine kinase showed that both of these isoforms decreased as malignancy progressed. Expressions of mRNA of muscle-type creatine kinase and sarcomeric mitochondrial creatine kinase were also severely downregulated. In human sarcoma these two isoforms were undetectable also. In human gastric and colonic adenocarcinoma, brain-type creatine kinase was found to be downregulated, whereas ubiquitous mitochondrial creatine kinase was upregulated. These significantly decreased levels of creatine and creatine kinase isoforms in sarcoma suggest that: (a) the genuine muscle phenotype is lost during sarcoma progression, and (b) these parameters may be used as diagnostic marker and prognostic indicator of malignancy in this tissue. |
Databáze: | OpenAIRE |
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