Stay tuned: Active processes tune tree cricket ears to maintain a match to temperature-dependent song frequency

2018 ◽  
Vol 143 (3) ◽  
pp. 1858-1858
Author(s):  
Natasha Mhatre ◽  
Gerald Pollack ◽  
Andrew Mason
Keyword(s):  
Temperature Dependent ◽  
Tree Cricket ◽  
Song Frequency ◽  
Active Processes

scholarly journals Stay tuned: active amplification tunes tree cricket ears to track temperature-dependent song frequency

2016 ◽  
Vol 12 (4) ◽  
pp. 20160016 ◽  
Author(s):  
Natasha Mhatre ◽  
Gerald Pollack ◽  
Andrew Mason
Keyword(s):  
Selective Advantage ◽  
Temperature Dependent ◽  
Adaptive Function ◽  
Mate Finding ◽  
Signal Characteristics ◽  
Tree Cricket ◽  
Song Frequency ◽  
Cricket Song ◽  
Active Processes ◽  
Auditory Processes

Tree cricket males produce tonal songs, used for mate attraction and male–male interactions. Active mechanics tunes hearing to conspecific song frequency. However, tree cricket song frequency increases with temperature, presenting a problem for tuned listeners. We show that the actively amplified frequency increases with temperature, thus shifting mechanical and neuronal auditory tuning to maintain a match with conspecific song frequency. Active auditory processes are known from several taxa, but their adaptive function has rarely been demonstrated. We show that tree crickets harness active processes to ensure that auditory tuning remains matched to conspecific song frequency, despite changing environmental conditions and signal characteristics. Adaptive tuning allows tree crickets to selectively detect potential mates or rivals over large distances and is likely to bestow a strong selective advantage by reducing mate-finding effort and facilitating intermale interactions.

scholarly journals Stay tuned: active amplification tunes tree-cricket ears to track temperature-dependent song frequency

2016 ◽  
Author(s):  
Natasha Mhatre ◽  
Gerald Pollack ◽  
Andrew Mason
Keyword(s):  
Selective Advantage ◽  
Temperature Dependent ◽  
Adaptive Function ◽  
Mate Finding ◽  
Signal Characteristics ◽  
Tree Cricket ◽  
Song Frequency ◽  
Cricket Song ◽  
Active Processes ◽  
Auditory Processes

AbstractTree cricket males produce tonal songs, used for mate-attraction and male-male interactions. Active mechanics tunes hearing to conspecific song frequency. However, tree cricket song frequency increases with temperature, presenting a problem for tuned listeners. We show that the actively amplified frequency increases with temperature, thus shifting mechanical and neuronal auditory tuning to maintain a match with conspecific song frequency. Active auditory processes are known from several taxa, but their adaptive function has rarely been demonstrated. We show that tree crickets harness active processes to ensure that auditory tuning remains matched to conspecific song frequency, despite changing environmental conditions and signal characteristics. Adaptive tuning allows tree crickets to selectively detect potential mates or rivals over large distances and is likely to bestow a strong selective advantage by reducing mate-finding effort and facilitating intermale interactions.

Temperature Dependent Investigation on Optically Active Processes of Higher-Order Bands in Irradiated Silicon

1996 ◽  
Vol 154 (2) ◽  
pp. 789-796
Author(s):  
Yi Shi ◽  
Fengmei Wu ◽  
Youdou Zheng ◽  
M. Suezawa ◽  
M. Imai ◽  
...  
Keyword(s):  
Higher Order ◽  
Optically Active ◽  
Temperature Dependent ◽  
Active Processes

scholarly journals Temperature-dependent shift of pHi in fish white muscle: contributions of passive and active processes

1997 ◽  
Vol 272 (1) ◽  
pp. R84-R89
Author(s):  
P. L. Van Dijk ◽  
I. Hardewig ◽  
H. O. Portner
Keyword(s):  
White Muscle ◽  
Passive Component ◽  
Muscle Proteins ◽  
Cell Water ◽  
Temperature Dependent ◽  
Zoarces Viviparus ◽  
Intracellular Proteins ◽  
Good Accordance ◽  
Buffer Value ◽  
Active Processes

This study was designed to determine the mechanisms causing temperature-induced pH shifts in the white muscle of the marine teleost Zoarces viviparus. The white musculature undergoes an intracellular acidification with increasing body temperature at a slope of the pH-temperature relationship equal to -0.016 +/- 0.003 U/degree C. This is in good accordance with the overall relationship between the change in pK and the change in temperature of the intracellular proteins, which was determined to be -0.013 +/- 0.001 U/degree C. Thus the dissociation state of muscle proteins is kept fairly constant in white muscle of Zoarces viviparus. The passive component of the observed pH shift, which is due to the physicochemical response of the intracellular buffers to temperature change, accounts for only 35% of the pH transition. Ventilatory adjustment of intracellular PCO2 does not contribute to the temperature-induced shift of intracellular pH (pHi) in Zoarces viviparus. Therefore, the remaining 65% of pH adjustment must be ascribed to ion exchange mechanisms. The nonbicarbonate buffer value amounted to 34.4 +/- 2.3 meq.pH-1 kg cell water-1 at 12 degrees C and decreased slightly but not significantly with temperature. On the basis of our data we calculated that a removal of 0.52 mmol base equivalents.kg cell water-1.degree C-1 was necessary to shift pHi to its new steady state.

(111) Monocrystalline Nickel Films

1972 ◽  
Vol 30 ◽  
pp. 512-513
Author(s):  
T.E. Pratt ◽  
R.W. Vook
Keyword(s):  
Film Thickness ◽  
Deposition Rate ◽  
Room Temperature ◽  
Narrow Range ◽  
High Vacuum ◽  
Residual Pressure ◽  
Temperature Dependent ◽  
Deposition Parameters ◽  
Transmission Electron ◽  
Substrate Temperatures

(111) oriented thin monocrystalline Ni films have been prepared by vacuum evaporation and examined by transmission electron microscopy and electron diffraction. In high vacuum, at room temperature, a layer of NaCl was first evaporated onto a freshly air-cleaved muscovite substrate clamped to a copper block with attached heater and thermocouple. Then, at various substrate temperatures, with other parameters held within a narrow range, Ni was evaporated from a tungsten filament. It had been shown previously that similar procedures would yield monocrystalline films of CU, Ag, and Au.For the films examined with respect to temperature dependent effects, typical deposition parameters were: Ni film thickness, 500-800 A; Ni deposition rate, 10 A/sec.; residual pressure, 10-6 torr; NaCl film thickness, 250 A; and NaCl deposition rate, 10 A/sec. Some additional evaporations involved higher deposition rates and lower film thicknesses.Monocrystalline films were obtained with substrate temperatures above 500° C. Below 450° C, the films were polycrystalline with a strong (111) preferred orientation.

In Vitro Effects of Urokinase — Prevention by Different Inhibitors

1990 ◽  
Vol 64 (03) ◽  
pp. 402-406 ◽  
Author(s):  
M D Oethinger ◽  
E Seifried
Keyword(s):  
In Vitro Study ◽  
Thrombin Time ◽  
Plasma Samples ◽  
Temperature Dependent ◽  
Chloromethyl Ketone ◽  
Control Value ◽  
Dose Time ◽  
In Vitro Effects ◽  
Full Protection

SummaryThe present in vitro study investigated dose-, time- and temperature-dependent effects of two-chain urokinase plasminogen activato(u-PA, urokinase) on normal citrated plasma. When 10 μg/ml u-PA wereadded to pooled normal plasma and incubated for 30 min at an ambient temperature (25° C), α2-antiplas-min decreased to 8% of the control value. Incubation on ice yielded a decrease to 45% of control,whereas α2-antiplasmin was fully consumed at 37° C. Fibrinogen and plasminogen fell to 46% and 39%, respectively, after a 30 min incubation at 25° C. Thrombin time prolonged to 190% of control.Various inhibitors were studied with respect to their suitability and efficacy to prevent these in vitro effects. Aprotinin exhibited a good protective effect on fibrinogen at concentrations exceeding 500 KlU/ml plasma. Its use, however, was limited due to interferences with some haemostatic assays. We could demonstrate that L-Glutamyl-L-Glycyl-L-Arginyl chloromethyl ketone (GGACK) and a specific polyclonal anti-u-PA-antibody (anti-u-PA-IgG) effectively inhibited urokinase-induced plasmin generation without interfering with haemostatic assays. The anti-u-PA-antibody afforded full protection ofα2-antiplasmin at therapeutic levels of u-PA.It is concluded that u-PA in plasma samples from patients during thrombolytic therapy may induce in vitro effects which should be prevented by the use of a suitable inhibitor such as GGACK or specific anti-u-PA-antibody.

Sign in / Sign up

Export Citation Format

Share Document