scholarly journals AMP-activated protein kinase is involved in hormone-induced mouse oocyte meiotic maturation in vitro

2008 ◽  
Vol 313 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Jing Chen ◽  
Stephen M. Downs
Keyword(s):  
Protein Kinase ◽  
Mouse Oocyte ◽  
Meiotic Maturation ◽  
Maturation In Vitro ◽  
Amp Activated Protein Kinase ◽  
Oocyte Meiotic Maturation

Diethylstilbestrol exposure disrupts mouse oocyte meiotic maturation in vitro through affecting spindle assembly and chromosome alignment

Chemosphere ◽  
2020 ◽  
Vol 249 ◽  
pp. 126182 ◽  
Author(s):  
Zhi-Ming Ding ◽  
Li-Ping Hua ◽  
Muhammad Jamil Ahmad ◽  
Muhammad Safdar ◽  
Fan Chen ◽  
...  
Keyword(s):  
Spindle Assembly ◽  
Mouse Oocyte ◽  
Meiotic Maturation ◽  
Maturation In Vitro ◽  
Chromosome Alignment ◽  
Oocyte Meiotic Maturation

Progestins inhibit murine oocyte meiotic maturation in vitro

1993 ◽  
Vol 265 (3) ◽  
pp. 231-239 ◽  
Author(s):  
C. Brent Barrett ◽  
R. Douglas Powers
Keyword(s):  
Meiotic Maturation ◽  
Maturation In Vitro ◽  
Oocyte Meiotic Maturation

Maternal diabetes adversely affects AMP-activated protein kinase activity and cellular metabolism in murine oocytes

2007 ◽  
Vol 293 (5) ◽  
pp. E1198-E1206 ◽  
Author(s):  
Ann M. Ratchford ◽  
Aimee S. Chang ◽  
Maggie M.-Y. Chi ◽  
Rachael Sheridan ◽  
Kelle H. Moley
Keyword(s):  
Protein Kinase ◽  
Cellular Metabolism ◽  
Maternal Diabetes ◽  
Meiotic Maturation ◽  
Protein Kinase Activity ◽  
Diabetic Mice ◽  
Increased Risk ◽  
Ampk Activity ◽  
Amp Activated Protein Kinase

Maternal diabetes is associated with an increased risk of miscarriages and congenital anomalies. Preovulatory oocytes in murine models also experience maturational delay and greater granulosa cell apoptosis. The objective of this study was to examine whether maternal diabetes influences preovulatory oocyte metabolism and impacts meiotic maturation. Streptozotocin-induced diabetic B6SJLF1 mice were superovulated, and oocytes were collected at 0, 2, and 6 h after human chorionic gonadotropin (hCG) injection. Individual oocyte concentrations of ATP, 5′-AMP, glycogen, and fructose-1,6-phosphate (FBP) and enzyme activities of glucose-6-phosphate dehydrogenase (G6PDH), adenylate kinase, hydroxyacyl-CoA dehydrogenase (Hadh2), and glutamic pyruvate transaminase (Gpt2) were measured. Protein levels of phosphorylated AMP-activated protein kinase (AMPK) and acetyl-CoA carboxylase (ACC) were also measured. ATP levels were significantly lower in oocytes from diabetic mice, and the percent change in the AMP-to-ATP ratio was significantly higher in these oocytes. In contrast, activities of Hadh2 and Gpt2, two enzymes activated by AMPK, were significantly less in these oocytes. Additionally, glycogen and FBP levels, both endogenous inhibitors of AMPK, were elevated. Phosphorylated ACC, a downstream target of AMPK, and phosphorylated AMPK were both decreased in diabetic oocytes, thus confirming decreased AMPK activity. Finally, addition of the activator AICAR to the in vitro maturation assay restored AMPK activity and corrected the maturation defect experienced by the oocytes from diabetic mice. In conclusion, maternal diabetes adversely alters cellular metabolism leading to abnormal AMPK activity in murine oocytes. Increasing AMPK activity in these oocytes during the preovulatory phase reverses the metabolic changes and corrects delays in meiotic maturation.

scholarly journals Bisphenol B Exposure Disrupts Mouse Oocyte Meiotic Maturation in vitro Through Affecting Spindle Assembly and Chromosome Alignment

2020 ◽  
Vol 8 ◽  
Author(s):  
Shou-Xin Zhang ◽  
Zhi-Ming Ding ◽  
Muhammad Jamil Ahmad ◽  
Yong-Sheng Wang ◽  
Ze-Qun Duan ◽  
...  
Keyword(s):  
Dna Damage ◽  
Spindle Assembly ◽  
Epigenetic Modifications ◽  
Mouse Oocyte ◽  
Meiotic Maturation ◽  
Meiotic Arrest ◽  
First Polar Body ◽  
Chromosome Alignment ◽  
Oocyte Meiotic Maturation

Bisphenol B (BPB), a substitute of bisphenol A (BPA), is widely used in the polycarbonate plastic and resins production. However, BPB proved to be not a safe alternative to BPA, and as an endocrine disruptor, it can harm the health of humans and animals. In the present study, we explored the effects of BPB on mouse oocyte meiotic maturation in vitro. We found that 150 μM of BPB significantly compromised the first polar body extrusion (PBE) and disrupted the cell cycle progression with meiotic arrest. The spindle assembly and chromosome alignment were disordered after BPB exposure, which was further demonstrated by the aberrant localization of p-MAPK. Also, BPB exposure increased the acetylation levels of α-tubulin. As a result, the spindle assemble checkpoint (SAC) was continuously provoked, contributing to meiotic arrest. We further demonstrated that BPB severely induced DNA damage, but the ROS and ATP production were not altered. Furthermore, the epigenetic modifications were changed after BPB exposure, as indicated by increased K3K9me3 and H3K27me3 levels. Besides, the pattern of estrogen receptor α (ERα) dynamics was disrupted with a mass gathering on the spindle in BPB-exposed oocytes. Our collective results indicated that exposure to BPB compromised meiotic maturation and damaged oocyte quality by affecting spindle assembly and chromosome alignment, acetylation of α-tubulin, DNA damage, epigenetic modifications, and ERα dynamics in mouse oocytes.

Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK

2001 ◽  
Vol 355 (2) ◽  
pp. 297-305 ◽  
Author(s):  
Diana L. LEFEBVRE ◽  
Yahong BAI ◽  
Nazanin SHAHMOLKY ◽  
Monika SHARMA ◽  
Raymond POON ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cellular Response ◽  
Catalytic Domain ◽  
Metabolic Stress ◽  
Glucose Deprivation ◽  
Protein Band ◽  
Northern Blotting ◽  
Significant Similarity ◽  
Amp Activated Protein Kinase

Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.

scholarly journals Interleukin-6 Increases Insulin-Stimulated Glucose Disposal in Humans and Glucose Uptake and Fatty Acid Oxidation In Vitro via AMP-Activated Protein Kinase

Diabetes ◽  
2006 ◽  
Vol 55 (10) ◽  
pp. 2688-2697 ◽  
Author(s):  
A. L. Carey ◽  
G. R. Steinberg ◽  
S. L. Macaulay ◽  
W. G. Thomas ◽  
A. G. Holmes ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Protein Kinase ◽  
Glucose Uptake ◽  
Fatty Acid Oxidation ◽  
Interleukin 6 ◽  
Glucose Disposal ◽  
Acid Oxidation ◽  
Amp Activated Protein Kinase

AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle

2001 ◽  
Vol 280 (5) ◽  
pp. E677-E684 ◽  
Author(s):  
Nicolas Musi ◽  
Tatsuya Hayashi ◽  
Nobuharu Fujii ◽  
Michael F. Hirshman ◽  
Lee A. Witters ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Glucose Uptake ◽  
Muscle Contractions ◽  
Treadmill Running ◽  
Dependent Manner ◽  
Rat Skeletal Muscle ◽  
Amp Activated Protein Kinase ◽  
Dose Dependent

The AMP-activated protein kinase (AMPK) has been hypothesized to mediate contraction and 5-aminoimidazole-4-carboxamide 1-β-d-ribonucleoside (AICAR)-induced increases in glucose uptake in skeletal muscle. The purpose of the current study was to determine whether treadmill exercise and isolated muscle contractions in rat skeletal muscle increase the activity of the AMPKα1 and AMPKα2 catalytic subunits in a dose-dependent manner and to evaluate the effects of the putative AMPK inhibitors adenine 9-β-d-arabinofuranoside (ara-A), 8-bromo-AMP, and iodotubercidin on AMPK activity and 3- O-methyl-d-glucose (3-MG) uptake. There were dose-dependent increases in AMPKα2 activity and 3-MG uptake in rat epitrochlearis muscles with treadmill running exercise but no effect of exercise on AMPKα1 activity. Tetanic contractions of isolated epitrochlearis muscles in vitro significantly increased the activity of both AMPK isoforms in a dose-dependent manner and at a similar rate compared with increases in 3-MG uptake. In isolated muscles, the putative AMPK inhibitors ara-A, 8-bromo-AMP, and iodotubercidin fully inhibited AICAR-stimulated AMPKα2 activity and 3-MG uptake but had little effect on AMPKα1 activity. In contrast, these compounds had absent or minimal effects on contraction-stimulated AMPKα1 and -α2 activity and 3-MG uptake. Although the AMPKα1 and -α2 isoforms are activated during tetanic muscle contractions in vitro, in fast-glycolytic fibers, the activation of AMPKα2-containing complexes may be more important in regulating exercise-mediated skeletal muscle metabolism in vivo. Development of new compounds will be required to study contraction regulation of AMPK by pharmacological inhibition.

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