• English
    • Norsk
  • English 
    • English
    • Norsk
  • Administration
View Item 
  •   Home
  • Øvrige samlinger
  • Høstingsarkiver
  • CRIStin høstingsarkiv
  • View Item
  •   Home
  • Øvrige samlinger
  • Høstingsarkiver
  • CRIStin høstingsarkiv
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes

Ruud Larsen, Ann K.; Møller, Michael T. N; Blankson, Henrietta; Samari, Hamid R.; Holden, Lise; Seglen, Per O.
Journal article; PublishedVersion; Peer reviewed
View/Open
Naringin-sensit ... ctin%2C+a+Cytoskeletal.pdf (432.0Kb)
Year
2002
Permanent link
http://urn.nb.no/URN:NBN:no-61987

CRIStin
404235

Metadata
Show metadata
Appears in the following Collection
  • Det medisinske fakultet [180]
  • CRIStin høstingsarkiv [8384]
Original version
Journal of Biological Chemistry. 2002, 277, 34826-34835, DOI: http://dx.doi.org/10.1074/jbc.M205028200
Abstract
To identify phosphoproteins that might play a role in naringin-sensitive hepatocellular cytoskeletal disruption and apoptosis induced by algal toxins, hepatocyte extracts were separated by gel electrophoresis and immunostained with a phosphothreonine-directed antibody. Use of dilute (5%) polyacrylamide gels containing 6 m urea allowed the resolution of one very large (approximately 500-kDa) okadaic acid- and naringin-sensitive phosphoprotein, identified by tryptic fingerprinting, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, and immunostaining as the cytolinker protein, plectin. The naringin-sensitive phosphorylation induced by okadaic acid and microcystin-LR probably reflected inhibition of a type 2A protein phosphatase, whereas the naringin-resistant phosphorylation induced by calyculin A, tautomycin, and cantharidin probably involved a type 1 phosphatase. Okadaic acid caused a collapse of the plectin-immunostaining bile canalicular sheaths and the general cytoskeletal plectin network into numerous medium-sized plectin aggregates. Inhibitors of protein kinase C, cAMP-dependent protein kinase, or Ca(2+)/calmodulin-dependent kinase II had moderate or no protective effects on plectin network disruption, whereas naringin offered 86% protection. Okadaic acid induced a naringin-sensitive phosphorylation of AMP-activated protein kinase (AMPK), the stress-activated protein kinases SEK1 and JNK, and S6 kinase. The AMPK-activating kinase (AMPKK) is likely to be the target of inhibition by naringin, the other kinases serving as downstream components of an AMPKK-initiated signaling pathway.

This article was originally published in the Journal of Biological Chemistry. © 2002 American Society of Biochemistry and Molecular Biology
 
Responsible for this website 
University of Oslo Library


Contact Us 
duo-hjelp@ub.uio.no


Privacy policy
 

 

For students / employeesSubmit master thesisAccess to restricted material

Browse

All of DUOCommunities & CollectionsBy Issue DateAuthorsTitlesThis CollectionBy Issue DateAuthorsTitles

For library staff

Login

Statistics

View Usage Statistics
RSS Feeds
 
Responsible for this website 
University of Oslo Library


Contact Us 
duo-hjelp@ub.uio.no


Privacy policy