Abstract：
:We demonstrated previously an inhibitory effect of luminal leptin on glucose absorption in differentiated Caco-2 cells. Since this process is dependent on the Na(+) gradient established by the Na(+)/K(+)ATPase this work was undertaken to investigate if the ATPase is one of the hormone's targets. Fully differentiated Caco-2 cells were incubated with 10nM luminal leptin and the activity of the Na(+)/K(+) ATPase was assayed by measuring the amount of inorganic phosphate liberated. To elucidate the signaling pathway involved, the suspected mediators, namely PKC, p38MAPK, ERK and PI3K, were inhibited with specific pharmacological inhibitors and their implication was confirmed by determining changes in the protein expression of their active phosphorylated forms by Western blot analysis. Leptin reduced significantly the activity of the Na(+)/K(+) ATPase, by activating p38MAPK via inhibition of PKC, an upstream inhibitor of the kinase. ERK and PI3K are modulators of the pump and are not along the pathway activated by leptin but cross talk with it at the level of p38MAPK.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
El-Zein O,Usta J,El Moussawi L,Kreydiyyeh SIdoi
10.1016/j.cellsig.2014.12.004subject
Has Abstractpub_date
2015-03-01 00:00:00pages
416-23issue
3eissn
0898-6568issn
1873-3913pii
S0898-6568(14)00402-1journal_volume
27pub_type
杂志文章abstract：:We investigated the effects of retinoic acid (RA) on the signalling pathways by prostaglandin E2 (PGE2) in osteoblast-like MC3T3-E1 cells. The pretreatment with RA significantly inhibited the formation of inositol phosphates induced by 10 microM PGE2 in a dose-dependent manner in the range between 0.1 nM and 0.1 micro...
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journal_title：Cellular signalling
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