Atypical Cristae Morphology of Human Syncytiotrophoblast Mitochondria ROLE FOR COMPLEX V

作者：De Los Rios Castillo Daniela; Zarco Zavala Mariel; Olvera Sanchez Sofia; Pablo Pardo Juan; Juarez Oscar; Martinez Federico; Mendoza Hernandez Guillermo; Garcia Trejo Jose J; Flores Herrera Oscar^*

来源：Journal of Biological Chemistry, 2011, 286(27): 23911-23919.

DOI：10.1074/jbc.M111.252056

Mitochondrial complexes I, III(2), and IV from human cytotrophoblast and syncytiotrophoblast associate to form supercomplexes or respirasomes, with the following stoichiometries: I(1):(III(2))(1) and I(1):(III(2))(1-2):IV(1-4). The content of respirasomes was similar in both cell types after isolating mitochondria. However, syncytiotrophoblast mitochondria possess low levels of dimeric complex V and do not have orthodox cristae morphology. In contrast, cytotrophoblast mitochondria show normal cristae morphology and a higher content of ATP synthase dimer. Consistent with the dimerizing role of the ATPase inhibitory protein (IF(1)) (Garcia, J.J., Morales-Rios, E., Cortes-Hernandez, P., and Rodriguez-Zavala, J. S. (2006) Biochemistry 45, 12695-12703), higher relative amounts of IF(1) were observed in cytotrophoblast when compared with syncytiotrophoblast mitochondria. Therefore, there is a correlation between dimerization of complex V, IF(1) expression, and the morphology of mitochondrial cristae in human placental mitochondria. The possible relationship between cristae architecture and the physiological function of the syncytiotrophoblast mitochondria is discussed.

• 出版日期2011-7-8