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J. Biol. Chem., Vol. 277, Issue 38, 34826-34835, September 20, 2002
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From the Proteomics and Mammalian Cell Biology Section, Department
of Cell Biology, Institute for Cancer Research, The Norwegian Radium
Hospital, Montebello, 0310 Oslo, Norway
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 (~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 Ca2+/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.
Naringin-sensitive Phosphorylation of Plectin, a Cytoskeletal
Cross-linking Protein, in Isolated Rat Hepatocytes*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Cell Biology,
Institute for Cancer Research, The Norwegian Radium Hospital, N-0310
Oslo, Norway. Tel.: 47-22935947; Fax: 47-22934580; E-mail: per.seglen@labmed.uio.no.
§
These two authors contributed equally to the present work.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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