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Mortalin, apoptosis, and neurodegeneration.
Londono, Carolina; Osorio, Cristina; Gama, Vivian; Alzate, Oscar.
Affiliation
  • Londono C; Systems Proteomics Center Laboratory, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, Escuela de Medicina, Universidad Pontificia Bolivariana, Medellín, Colombia. londonop@email.unc.edu.
  • Osorio C; Systems Proteomics Center Laboratory and Program in Molecular Biology and Biotechnology, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA. osorioc@email.unc.edu.
  • Gama V; Neuroscience Center, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA. vivian_gama@med.unc.edu.
  • Alzate O; Systems Proteomics Center Laboratory, Department of Cell and Developmental Biology, Program in Molecular Biology and Biotechnology and Department of Neurology, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, Escuela de Medicina, Universidad Pontificia Bolivariana, Medellin,
Biomolecules ; 2(1): 143-64, 2012 Mar 01.
Article in En | MEDLINE | ID: mdl-24970131
Mortalin is a highly conserved heat-shock chaperone usually found in multiple subcellular locations. It has several binding partners and has been implicated in various functions ranging from stress response, control of cell proliferation, and inhibition/prevention of apoptosis. The activity of this protein involves different structural and functional mechanisms, and minor alterations in its expression level may lead to serious biological consequences, including neurodegeneration. In this article we review the most current data associated with mortalin's binding partners and how these protein-protein interactions may be implicated in apoptosis and neurodegeneration. A complete understanding of the molecular pathways in which mortalin is involved is important for the development of therapeutic strategies for cancer and neurodegenerative diseases.

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Biomolecules Year: 2012 Type: Article Affiliation country: Colombia

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Biomolecules Year: 2012 Type: Article Affiliation country: Colombia