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Regulation of protein expression and function of octn2 in forskolin-induced syncytialization in BeWo Cells.
Placenta. 2009 Feb; 30(2):187-94.P

Abstract

Placental OCTN2 is a high-affinity carnitine transporter that can interact with a number of therapeutic agents. The process of syncytialization is associated with the expression of a variety of genes. However, the association between syncytialization and OCTN2 expression is not yet clear. Given that forskolin induces BeWo cells to undergo biochemical and morphological differentiation, the purpose of the present study was to investigate whether the function and expression of OCTN2 are influenced by forskolin treatment during syncytialization. The forskolin-induced differentiation of BeWo cells was validated by secretion of beta-human chorionic gonadotropin (beta-hCG) and syncytin expression. Cellular localization of OCTN2 was analyzed by confocal microscopy. Expression of OCTN2 and the modular proteins PDZK1, PDZK2, NHERF1 and NHERF2 was analyzed by Western blotting and carnitine uptake by BeWo cells was estimated and the kinetic properties of uptake measured. The results showed that forskolin treatment increased beta-hCG secretion and syncytin expression, suggesting induction of syncytialization. Confocal images of BeWo cells showed the localization of OCTN2 in the brush-border membrane. OCTN2 protein expression was upregulated in isolated brush-border membranes by long-term forskolin treatment, but the V(m) for carnitine uptake was unchanged, although the K(m) increased. PDZK1, NHERF1 and NHERF2 protein expression in the brush-border membrane was downregulated by forskolin treatment, whereas PDZK2 levels remained unchanged. In conclusion, protein expression and function of OCTN2 in BeWo cells can be regulated by forskolin treatment. While the presence of forskolin results in an increase in OCTN2 protein expression, the increase in uptake capacity may be compensated by the decreased expression of PDZK1, NHERF1 or NHERF2.

Authors+Show Affiliations

School of Pharmacy, College of Medicine, National Taiwan University, 12F, 1 Jen-Ai Road, Section 1, Taipei 100, Taiwan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19091402

Citation

Huang, F-D, et al. "Regulation of Protein Expression and Function of Octn2 in Forskolin-induced Syncytialization in BeWo Cells." Placenta, vol. 30, no. 2, 2009, pp. 187-94.
Huang FD, Kung FL, Tseng YC, et al. Regulation of protein expression and function of octn2 in forskolin-induced syncytialization in BeWo Cells. Placenta. 2009;30(2):187-94.
Huang, F. D., Kung, F. L., Tseng, Y. C., Chen, M. R., Chan, H. S., & Lin, C. J. (2009). Regulation of protein expression and function of octn2 in forskolin-induced syncytialization in BeWo Cells. Placenta, 30(2), 187-94. https://doi.org/10.1016/j.placenta.2008.11.016
Huang FD, et al. Regulation of Protein Expression and Function of Octn2 in Forskolin-induced Syncytialization in BeWo Cells. Placenta. 2009;30(2):187-94. PubMed PMID: 19091402.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of protein expression and function of octn2 in forskolin-induced syncytialization in BeWo Cells. AU - Huang,F-D, AU - Kung,F-L, AU - Tseng,Y-C, AU - Chen,M-R, AU - Chan,H-S, AU - Lin,C-J, Y1 - 2008/12/16/ PY - 2008/07/22/received PY - 2008/11/14/revised PY - 2008/11/18/accepted PY - 2008/12/19/entrez PY - 2008/12/19/pubmed PY - 2009/3/25/medline SP - 187 EP - 94 JF - Placenta JO - Placenta VL - 30 IS - 2 N2 - Placental OCTN2 is a high-affinity carnitine transporter that can interact with a number of therapeutic agents. The process of syncytialization is associated with the expression of a variety of genes. However, the association between syncytialization and OCTN2 expression is not yet clear. Given that forskolin induces BeWo cells to undergo biochemical and morphological differentiation, the purpose of the present study was to investigate whether the function and expression of OCTN2 are influenced by forskolin treatment during syncytialization. The forskolin-induced differentiation of BeWo cells was validated by secretion of beta-human chorionic gonadotropin (beta-hCG) and syncytin expression. Cellular localization of OCTN2 was analyzed by confocal microscopy. Expression of OCTN2 and the modular proteins PDZK1, PDZK2, NHERF1 and NHERF2 was analyzed by Western blotting and carnitine uptake by BeWo cells was estimated and the kinetic properties of uptake measured. The results showed that forskolin treatment increased beta-hCG secretion and syncytin expression, suggesting induction of syncytialization. Confocal images of BeWo cells showed the localization of OCTN2 in the brush-border membrane. OCTN2 protein expression was upregulated in isolated brush-border membranes by long-term forskolin treatment, but the V(m) for carnitine uptake was unchanged, although the K(m) increased. PDZK1, NHERF1 and NHERF2 protein expression in the brush-border membrane was downregulated by forskolin treatment, whereas PDZK2 levels remained unchanged. In conclusion, protein expression and function of OCTN2 in BeWo cells can be regulated by forskolin treatment. While the presence of forskolin results in an increase in OCTN2 protein expression, the increase in uptake capacity may be compensated by the decreased expression of PDZK1, NHERF1 or NHERF2. SN - 0143-4004 UR - https://www.unboundmedicine.com/medline/citation/19091402/Regulation_of_protein_expression_and_function_of_octn2_in_forskolin_induced_syncytialization_in_BeWo_Cells_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0143-4004(08)00389-5 DB - PRIME DP - Unbound Medicine ER -