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Comparative proteomic analysis associated with term placental insufficiency in cloned pig
Author(s) -
Lee SoYoung,
Park JongYi,
Choi YunJung,
Cho SeongKeun,
Ahn Jong Deok,
Kwon DeugNam,
Hwang KyuChan,
Kang SungJo,
Paik SeungSam,
Seo Han Geuk,
Lee Hoon Taek,
Kim JinHoi
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200601045
Subject(s) - somatic cell nuclear transfer , biology , cytotrophoblast , microbiology and biotechnology , placental insufficiency , cloning (programming) , proteomics , western blot , annexin a2 , apoptosis , annexin , andrology , placenta , genetics , embryo , gene , fetus , embryogenesis , blastocyst , pregnancy , medicine , computer science , programming language
Somatic cell‐derived nuclear transfer (scNT) is a method of animal cloning in which the oocyte reprograms a somatic cell nucleus to divide and execute developmental programs. Despite many successes in this field, cloning by scNT remains very inefficient. Unlike other cloned animals, pigs derived by scNT have placentas with severe villous hypoplasia. To obtain a better understanding of the protein networks involved in this phenomenon, we assessed global protein expression profiles in term placentas from scNT‐derived and control animals. Proteomic analysis of term placentas from scNT‐derived animals identified 43 proteins that were differentially expressed compared to control animals. Among them, 14‐3‐3 proteins and Annexin V, which are closely involved in the apoptotic signaling pathway, were significantly down‐ and up‐regulated, respectively. Western blot analysis and immunohistochemistry indicated that down‐regulation of 14‐3‐3 proteins in scNT‐derived placentas induced apoptosis of cytotrophoblast cells via mitochondria‐mediated apoptosis. Taken together, our results suggest that placental insufficiency in scNT‐derived placentas may be due to apoptosis, induced in part by the down‐regulation of 14‐3‐3 proteins and up‐regulation of Annexin V. They also indicate that proteomic maps represent an important tool for future studies of placental insufficiency and pathology.