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71.
Clemens Benjamin J. Weitkamp Laurie Siwicke Kevin Wade Joy Harris Julianne Hess Jon Porter Laurie Parker Keith Sutton Trent Orlov Alexei M. 《Reviews in Fish Biology and Fisheries》2019,29(4):767-788
Reviews in Fish Biology and Fisheries - Pacific lamprey Entosphenus tridentatus has an anadromous life cycle that begins with larvae that filter-feed in freshwater, followed by transformation into... 相似文献
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Baricault L Ségui B Guégand L Olichon A Valette A Larminat F Lenaers G 《Experimental cell research》2007,313(17):3800-3808
OPA1, an intra-mitochondrial dynamin GTPase, is a key actor of outer and inner mitochondrial membrane dynamic. OPA1 amino-terminal cleavage by PARL and m-AAA proteases was recently proposed to participate to the mitochondrial network dynamic in a DeltaPsi(m)-dependent way, and to apoptosis. Here, by an in vitro approach combining the use of purified mitochondrial fractions and mitochondrial targeting drugs, we intended to identify the central stimulus responsible for OPA1 cleavage. We confirm that apoptosis induction and PTPore opening, as well as DeltaPsi(m) dissipation induce OPA1 cleavage. Nevertheless, our experiments evidenced that decreased mitochondrial ATP levels, either generated by apoptosis induction, DeltaPsi(m) dissipation or inhibition of ATP synthase, is the common and crucial stimulus that controls OPA1 processing. In addition, we report that ectopic iron addition activates OPA1 cleavage, whereas zinc inhibits this process. These results suggest that the ATP-dependent OPA1 processing plays a central role in correlating the energetic metabolism to mitochondrial dynamic and might be involved in the pathophysiology of diseases associated to excess of iron or depletion of zinc and ATP. 相似文献
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Laurie A. Earley Steven M. Sammons Mary T. Mendona Carol J. Johnston 《Zeitschrift fur angewandte Ichthyologie》2019,35(4):917-923
There are numerous studies on the effects of dams on aquatic biota, yet relatively little is known about whether hydropeaking activities cause physiological change in fish. Using Alabama bass (Micropterus henshalli) as a model, we evaluated whether hydropeaking in a regulated river altered glucocorticoid stress responsiveness relative to fish from an unregulated tributary. Blood samples were collected at the time of capture (baseline) and then collected again after a 1‐hr period of confinement (response). Leukocyte profiles (blood smears) were created and plasma was extracted to assess plasma cortisol levels and neutrophils and lymphocyte (N:L) ratios, between sites and times to evaluate differences between sites and the two sampling periods. Baseline cortisol levels were higher in fish collected from the regulated river compared to those from unregulated site, but response levels of cortisol were similar between sites. Baseline and response level N:L ratios did not differ between sites. High baseline levels of cortisol suggested that fish exposed to regulated flows expressed an altered stress response and were likely in an allostatic state, i.e., attempting to acclimate. Further research is needed to understand how altered stress responses due to hydropeaking flows may be affecting fish. 相似文献
76.
Xiang-Lan Sun Sarah J. Lessard Ding An Ho-Jin Koh Hiroyasu Esumi Michael F. Hirshman Laurie J. Goodyear 《Journal of cellular biochemistry》2019,120(1):685-696
The signaling mechanisms mediating myocardial glucose transport are not fully understood. Sucrose nonfermenting AMP-activated protein kinase (AMPK)-related kinase (SNARK) is an AMPK-related protein kinase that is expressed in the heart and has been implicated in contraction-stimulated glucose transport in mouse skeletal muscle. We first determined if SNARK is phosphorylated on Thr208, a site critical for SNARK activity. Mice were treated with exercise, ischemia, submaximal insulin, or maximal insulin. Treadmill exercise slightly, but significantly increased SNARK Thr208 phosphorylation. Ischemia also increased SNARK Thr208 phosphorylation, but there was no effect of submaximal or maximal insulin. HL1 cardiomyocytes were used to overexpress wild-type (WT) SNARK and to knockdown endogenous SNARK. Overexpression of WT SNARK had no effect on ischemia-stimulated glucose transport; however, SNARK knockdown significantly decreased ischemia-stimulated glucose transport. SNARK overexpression or knockdown did not alter insulin-stimulated glucose transport or glycogen concentrations. To study SNARK function in vivo, SNARK heterozygous knockout mice (SNARK+/−) and WT littermates performed treadmill exercise. Exercise-stimulated glucose transport was decreased by ~50% in hearts from SNARK+/− mice. In summary, exercise and ischemia increase SNARK Thr208 phosphorylation in the heart and SNARK regulates exercise-stimulated and ischemia-stimulated glucose transport. SNARK is a novel mediator of insulin-independent glucose transport in the heart. 相似文献
77.
Biber K Laurie DJ Berthele A Sommer B Tölle TR Gebicke-Härter PJ van Calker D Boddeke HW 《Journal of neurochemistry》1999,72(4):1671-1680
Stimulation of astrocytes with the excitatory neurotransmitter glutamate leads to the formation of inositol 1,4,5-trisphosphate and the subsequent increase of intracellular calcium content. Astrocytes express both ionotropic receptors and metabotropic glutamate (mGlu) receptors, of which mGlu5 receptors are probably involved in glutamate-induced calcium signaling. The mGlu5 receptor occurs as two splice variants, mGlu5a and mGlu5b, but it was hitherto unknown which splice variant is responsible for the glutamate-induced effects in astrocytes. We report here that both mRNAs encoding mGlu5 receptor splice variants are expressed by cultured astrocytes. The expression of mGlu5a receptor mRNA is much stronger than that of mGlu5b receptor mRNA in these cells. In situ hybridization experiments reveal neuronal expression of mGlu5b receptor mRNA in adult rat forebrain but a strong neuronal expression of mGlu5a mRNA only in olfactory bulb. Signals for mGlu5a receptor mRNA in the rest of the brain were diffuse and weak but consistently above background. Activation of mGlu5 receptors in astrocytes yields increases in inositol phosphate production and transient calcium responses. It is surprising that the rank order of agonist potency [quisqualate > (2S,1 'S,2'S)-2-(carboxycyclopropyl)glycine = trans-(1S,3R)-1-amino-1,3-cyclopentanedicarboxylic acid (1S,3R-ACPD) > glutamate] differs from that reported for recombinantly expressed mGlu5a receptors. The expression of mGlu5a receptor mRNA and the occurrence of 1S,3R-ACPD-induced calcium signaling were found also in cultured microglia, indicating for the first time expression of mGlu5a receptors in these macrophage-like cells. 相似文献
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Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity 总被引:2,自引:0,他引:2
Fujii N Boppart MD Dufresne SD Crowley PF Jozsi AC Sakamoto K Yu H Aschenbach WG Kim S Miyazaki H Rui L White MF Hirshman MF Goodyear LJ 《American journal of physiology. Cell physiology》2004,287(1):C200-C208
c-Jun NH2-terminal kinase (JNK) is highly expressed in skeletal muscle and is robustly activated in response to muscle contraction. Little is known about the biological functions of JNK signaling in terminally differentiated muscle cells, although this protein has been proposed to regulate insulin-stimulated glycogen synthase activity in mouse skeletal muscle. To determine whether JNK signaling regulates contraction-stimulated glycogen synthase activation, we applied an electroporation technique to induce JNK overexpression (O/E) in mouse skeletal muscle. Ten days after electroporation, in situ muscle contraction increased JNK activity 2.6-fold in control muscles and 15-fold in the JNK O/E muscles. Despite the enormous activation of JNK activity in JNK O/E muscles, contraction resulted in similar increases in glycogen synthase activity in control and JNK O/E muscles. Consistent with these findings, basal and contraction-induced glycogen synthase activity was normal in muscles of both JNK1- and JNK2-deficient mice. JNK overexpression in muscle resulted in significant alterations in the basal phosphorylation state of several signaling proteins, such as extracellular signal-regulated kinase 1/2, p90 S6 kinase, glycogen synthase kinase 3, protein kinase B/Akt, and p70 S6 kinase, in the absence of changes in the expression of these proteins. These data suggest that JNK signaling regulates the phosphorylation state of several kinases in skeletal muscle. JNK activation is unlikely to be the major mechanism by which contractile activity increases glycogen synthase activity in skeletal muscle. electroporation; gene delivery; muscle contraction; exercise 相似文献