Journal article

Caveolin-3 and eNOS colocalize and interact in ciliated airway epithelial cells in the rat


Authors listKrasteva, Gabriela; Pfeil, Uwe; Filip, Ana-Maria; Lips, Katrin S.; Kummer, Wolfgang; Koenig, Peter

Publication year2007

Pages615-625

JournalThe International Journal of Biochemistry and Cell Biology

Volume number39

Issue number3

ISSN1357-2725

DOI Linkhttps://doi.org/10.1016/j.biocel.2006.10.019

PublisherElsevier


Abstract
in ciliated airway epithelial cells endothelial nitric oxide synthase as well as several other membrane bound proteins are located in the apical cell pole. To date, mechanisms that serve to target and to keep these proteins in this region are unknown. Endothelial nitric oxide synthase is known to target to caveolae by interaction with caveolin-1 or caveolin-3. Since caveolin-1 is found only in a subpopulation of ciliated cells at the basolateral cell membrane, we examined if caveolin-3 could be responsible for the apical localization of endothelial nitric oxide synthase in ciliated cells. We used real-time RT-PCR, laser-assisted microdissection, Western blotting and double-labeling immunohistochemistry to examine the presence of caveolin-3 in the airway epithelium of the rat. Indeed, we found caveolin-3-mRNA as well as protein in ciliated cells throughout the trachea and the bronchial tree. Caveolin-3-immunoreactivity was confined to the apical region and was colocalized with endothelial nitric oxide synthase and the high affinity choline transporter in a compartment distinct from the plasma membrane at the light microscopic level. No caveolae were found in the apical plasma membrane of ciliated cells but a tubulovesicular network was present in the apical region that reached up to the basal bodies of the cilia and was in close contact with mitochondria. Co-immunoprecipitation of caveolin-3 with endothelial nitric oxide synthase verified that both proteins interact in airway ciliated cells. These findings indicate that caveolin-3 is responsible to keep endothelial nitric oxide synthase in a membrane compartment in the apical region of ciliated cells. (c) 2006 Elsevier Ltd. All rights reserved.



Citation Styles

Harvard Citation styleKrasteva, G., Pfeil, U., Filip, A., Lips, K., Kummer, W. and Koenig, P. (2007) Caveolin-3 and eNOS colocalize and interact in ciliated airway epithelial cells in the rat, The International Journal of Biochemistry and Cell Biology, 39(3), pp. 615-625. https://doi.org/10.1016/j.biocel.2006.10.019

APA Citation styleKrasteva, G., Pfeil, U., Filip, A., Lips, K., Kummer, W., & Koenig, P. (2007). Caveolin-3 and eNOS colocalize and interact in ciliated airway epithelial cells in the rat. The International Journal of Biochemistry and Cell Biology. 39(3), 615-625. https://doi.org/10.1016/j.biocel.2006.10.019



Keywords


AFFINITY CHOLINE TRANSPORTERBEAT FREQUENCYcaveolin-3ciliated cellshigh affinity choline transporterINOSITOL 1,4,5-TRISPHOSPHATE RECEPTORSMICRODOMAINSsmooth endoplasmic reticulum

Last updated on 2025-18-06 at 13:48