Abstract：
:AMP-activated protein kinase (AMPK), a cellular metabolic sensor, is essential in energy regulation and metabolism. Hepatocyte polarization during liver development and regeneration parallels increased metabolism. The current study investigates the effects of AMPK and its upstream activator LKB1 on polarity and bile canalicular network formation and maintenance in collagen sandwich cultures of rat hepatocytes. Immunostaining for the apical protein ABCB1 and the tight junction marker occludin demonstrated that canalicular network formation is sequential and is associated with activation of AMPK and LKB1. AMPK and LKB1 activators accelerated canalicular network formation. Inhibition of AMPK or LKB1 by dominant-negative AMPK or kinase-dead LKB1 constructs blocked canalicular network formation. AICAR and 2-deoxyglucose, which activate AMPK, circumvented the inhibitory effect of kinase-dead LKB1 on canalicular formation, indicating that AMPK directly affects canalicular network formation. After the canalicular network was formed, inhibition of AMPK and LKB1 by dominant-negative AMPK or kinase-dead LKB1 constructs resulted in loss of canalicular network, indicating that AMPK and LKB1 also participate in network maintenance. In addition, activation of AMPK and LKB1 prevented low-Ca(2+)-mediated disruption of the canalicular network and tight junctions. These studies reveal that AMPK and its upstream kinase, LKB1, regulate canalicular network formation and maintenance.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Fu D,Wakabayashi Y,Ido Y,Lippincott-Schwartz J,Arias IMdoi
10.1242/jcs.068098subject
Has Abstractpub_date
2010-10-01 00:00:00pages
3294-302issue
Pt 19eissn
0021-9533issn
1477-9137pii
jcs.068098journal_volume
123pub_type
杂志文章abstract：:RINGO/Speedy proteins are direct activators of Cdk1 and Cdk2 that have no sequence homology to cyclins. We have characterized the role in cell-cycle progression of a new human member of this protein family referred to as RINGO C. We show that siRNA-mediated knockdown of RINGO C results in premature mitotic exit with m...
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journal_title：Journal of cell science
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更新日期：1991-11-01 00:00:00
abstract：:Non-muscle myosin II (MyoII) contractility is central to the regulation of numerous cellular processes, including migration. Rho is a well-characterized modulator of actomyosin contractility, but the function of other GTPases, such as Rac, in regulating contractility is currently not well understood. Here, we show tha...
journal_title：Journal of cell science
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journal_title：Journal of cell science
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journal_title：Journal of cell science
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更新日期：2000-11-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1989-02-01 00:00:00
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journal_title：Journal of cell science
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doi：
更新日期：1985-06-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章,评审
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更新日期：2002-03-15 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1995-08-01 00:00:00
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更新日期：2013-01-01 00:00:00
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更新日期：2014-07-01 00:00:00
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pub_type： 杂志文章
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pub_type： 杂志文章
doi：10.1242/jcs.130500
更新日期：2013-10-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1993-04-01 00:00:00
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doi：
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journal_title：Journal of cell science
pub_type： 杂志文章,评审
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更新日期：2000-08-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1995-02-01 00:00:00
