AMP-activated protein kinase in the grass carp Ctenopharyngodon idellus: Molecular characterization, tissue distribution and mRNA expression in response to overwinter starvation stress

2020 ◽  
Vol 246-247 ◽  
pp. 110457
Author(s):  
Wenyi Wu ◽  
Jian Sun ◽  
Hong Ji ◽  
Haibo Yu ◽  
Jishu Zhou
Keyword(s):  
Protein Kinase ◽  
Tissue Distribution ◽  
Mrna Expression ◽  
Molecular Characterization ◽  
Grass Carp ◽  
Ctenopharyngodon Idellus ◽  
Starvation Stress ◽  
Amp Activated Protein Kinase

AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells

2007 ◽  
Vol 292 (6) ◽  
pp. E1555-E1567 ◽  
Author(s):  
Brian J. Krawiec ◽  
Gerald J. Nystrom ◽  
Robert A. Frost ◽  
Leonard S. Jefferson ◽  
Charles H. Lang
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Muscle Atrophy ◽  
Ubiquitin Ligases ◽  
C2c12 Cells ◽  
Skeletal Muscle Atrophy ◽  
Compound C ◽  
Mrna Content ◽  
Amp Activated Protein Kinase

The hypothesis of the present study was that exposure of differentiated muscle cells to agonists of the AMP-activated protein kinase (AMPK) would increase the mRNA content of the muscle-specific ubiquitin ligases muscle atrophy F-box (MAFbx) and muscle RING finger 1 (MuRF1). C2C12 cells were incubated with incremental doses of 5-aminoimidazol-4-carboximide ribonucleoside (AICAR) or metformin for 24 h. Both MAFbx and MuRF1 mRNA increased dose dependently in response to these AMPK activators. AICAR, metformin, and 2-deoxy-d-glucose produced time-dependent alterations in ubiquitin ligase expression, typified by a biphasic pattern of expression marked by an acute repression followed by a sustained induction. AMPK-activating treatments in conjunction with dexamethasone produced a pronounced synergistic effect on ligase mRNA expression at later time points. This cooperative response occurred in the absence of a dexamethasone-dependent increase in AMPK expression or activity, as determined by immunoblotting for phosphorylation and expression of AMPKα and its downstream target acetyl-CoA carboxylase (ACC). These responses elicited by AMPK activation singly or in combination with dexamethasone did not extend to the mRNA expression of the UBR box family E3s UBR1/E3αI and UBR2/E3αII. Treatment with the AMPK inhibitor compound C prevented increases in MAFbx and MuRF1 mRNA in response to serum deprivation, as well as AICAR and dexamethasone treatment individually or jointly. Stimulation of AMPK activity in vivo via AICAR injection increased both MAFbx and MuRF1 mRNA in murine skeletal muscle. These data suggest that activation of AMPK in skeletal muscle results in a specific upregulation of MAFbx and MuRF1, responses that are reminiscent of the proposed atrophic transcriptional program executed under various conditions of skeletal muscle wasting. Therefore, AMPK may be a critical component of the intercalated network of signaling pathways governing skeletal muscle atrophy, where its input acts to modify anti- and proatrophic signals to influence gene expression in reaction to catabolic perturbations.

Molecular characterization of the AMP-activated protein kinase and its role in cellular metabolism

1997 ◽  
Vol 25 (4) ◽  
pp. 1224-1228 ◽  
Author(s):  
D. Carling ◽  
A. Woods ◽  
C. Thornton ◽  
P. C. F. Cheung ◽  
F. C. Smith ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Molecular Characterization ◽  
Cellular Metabolism ◽  
Amp Activated Protein Kinase

scholarly journals TAC1 Gene Products Regulate Pituitary Hormone Secretion and Gene Expression in Prepubertal Grass Carp Pituitary Cells

Endocrinology ◽  
2017 ◽  
Vol 158 (6) ◽  
pp. 1776-1797 ◽  
Author(s):  
Guangfu Hu ◽  
Mulan He ◽  
Wendy K. W. Ko ◽  
Anderson O. L. Wong
Keyword(s):  
Protein Kinase ◽  
Mrna Expression ◽  
Grass Carp ◽  
Messenger Rna ◽  
Hormone Secretion ◽  
Adenosine Monophosphate ◽  
Pituitary Hormone ◽  
Neurokinin A ◽  
Pituitary Cells ◽  
Gene Products

Abstract Tachykinin-1 (TAC1) is known to have diverse functions in mammals, but similar information is scarce in fish species. Using grass carp as a model, the pituitary actions, receptor specificity and postreceptor signaling of TAC1 gene products, namely substance P (SP) and neurokinin A (NKA), were examined. TAC1 encoding SP and NKA as well as tachykinin receptors NK1R and NK2R were cloned in the carp pituitary. The newly cloned receptors were shown to be functional with properties similar to mammalian counterparts. In carp pituitary cells, SP and NKA could trigger luteinizing hormone (LH), prolactin (PRL), and somatolactin α (SLα) secretion, with parallel rises in PRL and SLα transcripts. Short-term SP treatment (3 hours) induced LH release, whereas prolonged induction (24 hours) could attenuate LHβ messenger RNA (mRNA) expression. At pituitary cell level, LH, PRL, and SLα regulation by TAC1 gene products were mediated by NK1R, NK2R, and NK3R, respectively. Apparently, SP- and NKA-induced LH and SLα secretion and transcript expression were mediated by adenylyl cyclase/cyclic adenosine monophosphate (cAMP)/protein kinase A (PKA), phospholiphase C (PLC)/inositol 1,4,5-triphosphate/protein kinase C (PKC), and Ca2+/calmodulin (CaM)/CaM-dependent protein kinase-II pathways. The signal transduction for PRL responses was similar, except for the absence of a PKC component. Regarding SP inhibition of LHβ mRNA expression, the cAMP/PKA- and PLC/PKC-dependent (but not Ca2+/CaM-dependent) cascades were involved. These results, as a whole, suggest that TAC1 gene products play a role in LH, PRL, and SLα regulation via overlapping postreceptor signaling coupled to different subtypes of tachykinin receptor expressed in the carp pituitary.

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