scholarly journals Oxytocin receptor elicits different EGFR/MAPK activation patterns depending on its localization in caveolin-1 enriched domains

Oncogene ◽  
2003 ◽  
Vol 22 (38) ◽  
pp. 6054-6060 ◽  
Author(s):  
Valeria Rimoldi ◽  
Alessandra Reversi ◽  
Elena Taverna ◽  
Patrizia Rosa ◽  
Maura Francolini ◽  
...  
2005 ◽  
Vol 173 (4S) ◽  
pp. 385-386
Author(s):  
Gregor Bötticher ◽  
Zsófia Herbert ◽  
Erdogan Sendemir ◽  
Andreas Aschoff ◽  
Gustav Friedrich Jirikowski ◽  
...  

2006 ◽  
Vol 291 (2) ◽  
pp. H658-H667 ◽  
Author(s):  
Cherry Ballard-Croft ◽  
Adam C. Locklar ◽  
Gentian Kristo ◽  
Robert D. Lasley

Ischemia-reperfusion activates ERK and p38 MAPK in cardiac membranes, but the role of caveolae in MAPK signaling during this stress has not been studied. The purpose of this study was to determine the effect of in vivo myocardial ischemia-reperfusion on the level and distribution of caveolin-1 and -3 and cholesterol as well as MAPK activation in caveolin-enriched fractions. Adult male rats were subjected to in vivo regional myocardial ischemia induced by 25 min of coronary artery occlusion and 10 min ( n = 5) or 2 h ( n = 4) of reperfusion. Another group of rats served as appropriate nonischemic time controls ( n = 4). A discontinuous sucrose density gradient was used to isolate caveolae/lipid rafts from ischemic and nonischemic heart tissue. Caveolin-1 and -3, as well as cholesterol, were enriched in the light fractions. A redistribution of caveolin-3 and a reduction in caveolin-1 and cholesterol levels in the light fractions occurred after 10 min of reperfusion. The ERKs were activated in ischemic zone light and heavy fractions by 10 min of reperfusion. p44 ERK was activated after 2 h of reperfusion only in the light fractions, whereas p42 ERK phosphorylation was increased in the light and heavy fractions. Although no p38 MAPK activation occurred after 10 min of reperfusion, 2 h of reperfusion caused significant activation of p38 MAPK in nonischemic zone light and heavy fractions. These results show the importance of caveolar membrane/lipid rafts in MAPK signaling and suggest that subcellular compartmentation of p44/p42 ERKs and p38 MAPK may play distinct roles in the response to myocardial ischemia-reperfusion.


Oncogene ◽  
2002 ◽  
Vol 21 (11) ◽  
pp. 1658-1667 ◽  
Author(s):  
Francesca Guzzi ◽  
Deborah Zanchetta ◽  
Paola Cassoni ◽  
Valeria Guzzi ◽  
Maura Francolini ◽  
...  

2017 ◽  
Vol 23 (1) ◽  
pp. 6-12 ◽  
Author(s):  
Theodora K Kallak ◽  
Kerstin Uvnäs-Moberg

Objective During and after menopause, the symptoms of vaginal atrophy cause great discomfort and necessitate effective treatment options. Currently, vaginally applied oxytocin is being investigated as a treatment for the symptoms of vaginal atrophy in postmenopausal women. To clarify the mechanisms behind oxytocins effects on vaginal atrophy, the present study investigated the effects of oxytocin on cell proliferation in the cells of the Vk2E6E7 line, a non-tumour vaginal cell line. The study also compared the effects of oxytocin with those of estradiol (E2). Study design The effects of both oxytocin and E2 on the proliferation of Vk2E6E7 cells were investigated using Cell Proliferation ELISA BrdU Colorimetric Assay. The expression of both oxytocin and oxytocin receptor was studied in Vk2E6E7 cells using quantitative real-time polymerase chain reaction and immunofluorescent staining. Main outcome measures Cell proliferation and gene expression. Results Oxytocin increased cell proliferation both time dependently and dose dependently. This differed from the effect pattern observed in cells treated with E2. In addition, in oxytocin-treated cells, the oxytocin receptor was found to be co-localized with caveolin-1, indicating pro-proliferative signalling within the cell. Conclusions Oxytocin stimulates cell proliferation and the co-localization of oxytocin receptor with caveolin-1 in oxytocin-treated cells, supporting the role of oxytocin signalling in cell proliferation. In addition, these findings suggest that increased cell proliferation is one mechanism by which local vaginal oxytocin treatment increases vaginal thickness and relieves vaginal symptoms in postmenopausal women with vaginal atrophy.


2008 ◽  
Vol 24 (2) ◽  
pp. 105-112 ◽  
Author(s):  
Aynur Sendemir ◽  
Erdogan Sendemir ◽  
Hartmuth Kosmehl ◽  
Gustav F. Jirikowski

2007 ◽  
Vol 36 (5) ◽  
pp. 361-365 ◽  
Author(s):  
Z. Herbert ◽  
G. Bötticher ◽  
A. Aschoff ◽  
E. Sendemir ◽  
D.-H. Zermann ◽  
...  

2003 ◽  
Vol 285 (3) ◽  
pp. H1113-H1122 ◽  
Author(s):  
Nolan L. Boyd ◽  
Heonyong Park ◽  
Hong Yi ◽  
Yong Chool Boo ◽  
George P. Sorescu ◽  
...  

Caveolae are plasmalemmal domains enriched with cholesterol, caveolins, and signaling molecules. Endothelial cells in vivo are continuously exposed to shear conditions, and their caveolae density and location may be different from that of static cultured cells. Here, we show that chronic shear exposure regulates formation and localization of caveolae and caveolin-1 in bovine aortic endothelial cells (BAEC). Chronic exposure (1 or 3 days) of BAEC to laminar shear increased the total number of caveolae by 45–48% above static control. This increase was due to a rise in the luminal caveolae density without changing abluminal caveolae numbers or increasing caveolin-1 mRNA and protein levels. Whereas some caveolin-1 was found in the plasma membrane in static-cultured cells, it was predominantly localized in the Golgi. In contrast, chronic shear-exposed cells showed intense caveolin-1 staining in the luminal plasma membrane with minimum Golgi association. The preferential luminal localization of caveolae may play an important role in endothelial mechanosensing. Indeed, we found that chronic shear exposure (preconditioning) altered activation patterns of two well-known shear-sensitive signaling molecules (ERK and Akt) in response to a step increase in shear stress. ERK activation was blunted in shear preconditioned cells, whereas the Akt response was accelerated. These results suggest that chronic shear stimulates caveolae formation by translocating caveolin-1 from the Golgi to the luminal plasma membrane and alters cell signaling responses.


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