Source:http://linkedlifedata.com/resource/pubmed/id/21126059
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
51
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pubmed:dateCreated |
2010-12-21
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pubmed:abstractText |
Neuropeptides of the adipokinetic hormone (AKH) family are among the best studied hormone peptides. They play important roles in insect hemolymph sugar homeostasis, larval lipolysis, and storage-fat mobilization. Mechanistic investigations have shown that, upon AKH stimulation, adipokinetic hormone receptor (AKHR) couples to a Gs protein and enhances adenylate cyclase activity, leading to intracellular cAMP accumulation. However, the underlying molecular mechanism by which this signaling pathway connects to extracellular signal-regulated kinase 1/2 (ERK1/2) remains to be elucidated. Using HEK293 cells stably or transiently expressing AKHR, we demonstrated that activation of AKHR elicited transient phosphorylation of ERK1/2. Our investigation indicated that AKHR-mediated activation of ERK1/2 was significantly inhibited by H-89 (protein kinase A inhibitor), Go6983, and GF109203X (protein kinase C inhibitors) but not by U73122 (PLC inhibitor) or FIPI (PLD inhibitor). Moreover, AKHR-induced ERK1/2 phosphorylation was blocked by the calcium chelators EGTA and BAPTA-AM. Furthermore, ERK1/2 activation in both transiently and stably AKHR-expressing HEK293 cells was found to be sensitive to pretreatment of pertussis toxin, whereas AKHR-mediated ERK1/2 activation was insensitive to siRNA-induced knockdown of ?-arrestins and to pretreatment of inhibitors of EGFR, Src, and PI3K. On the basis of our data, we propose that activated AKHR signals to ERK1/2 primarily via PKA- and calcium-involved PKC-dependent pathways. Our current study provides the first in-depth study defining the mechanisms of AKH-mediated ERK activation through the Bombyx AKHR.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arrestins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glucagon,
http://linkedlifedata.com/resource/pubmed/chemical/beta-arrestin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1520-4995
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
28
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10862-72
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pubmed:meshHeading |
pubmed-meshheading:21126059-Animals,
pubmed-meshheading:21126059-Arrestins,
pubmed-meshheading:21126059-Bombyx,
pubmed-meshheading:21126059-Cell Line,
pubmed-meshheading:21126059-Cyclic AMP,
pubmed-meshheading:21126059-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:21126059-Enzyme Activation,
pubmed-meshheading:21126059-GTP-Binding Proteins,
pubmed-meshheading:21126059-Gene Expression,
pubmed-meshheading:21126059-Humans,
pubmed-meshheading:21126059-Insect Proteins,
pubmed-meshheading:21126059-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:21126059-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:21126059-Protein Kinase C,
pubmed-meshheading:21126059-Receptors, Glucagon,
pubmed-meshheading:21126059-Signal Transduction
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pubmed:year |
2010
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pubmed:articleTitle |
Bombyx adipokinetic hormone receptor activates extracellular signal-regulated kinase 1 and 2 via G protein-dependent PKA and PKC but ?-arrestin-independent pathways.
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pubmed:affiliation |
Institute of Biochemistry, College of Life Sciences, Zijingang Campus, Zhejiang University, Hangzhou, Zhejiang 310058, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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