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Physiologic Function
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Muscle Contraction
Muscle Contraction
Muscle Contraction is a fundamental physiological process whereby muscle fibers shorten, generating force and movement.
This complex mechanism involves the coordinated interaction of actin and myosin proteins, driven by the hydrolysis of ATP.
Muscle contraction is essential for a wide range of bodily functions, from locomotion and posture to circulation and respiration.
Researchers studying muscle contraction utilize a variety of experimental protocols to investigate the underlying molecular pathways, biophysical properties, and regulatory mechanisms.
Optimizing these protocols is crucial for accelerating advancements in areas such as skeletal muscle physiology, neuromuscular disorders, and exercise science.
PubCompare.ai's AI-driven platform can help researchers easily locate, compare, and select the most effective muscle contraction research protocols from the literature, preprints, and patents, empowering them to make informed decisions and drive their research forward more efficiently.
This complex mechanism involves the coordinated interaction of actin and myosin proteins, driven by the hydrolysis of ATP.
Muscle contraction is essential for a wide range of bodily functions, from locomotion and posture to circulation and respiration.
Researchers studying muscle contraction utilize a variety of experimental protocols to investigate the underlying molecular pathways, biophysical properties, and regulatory mechanisms.
Optimizing these protocols is crucial for accelerating advancements in areas such as skeletal muscle physiology, neuromuscular disorders, and exercise science.
PubCompare.ai's AI-driven platform can help researchers easily locate, compare, and select the most effective muscle contraction research protocols from the literature, preprints, and patents, empowering them to make informed decisions and drive their research forward more efficiently.
Most cited protocols related to «Muscle Contraction»
Adult
Contracture
Digestion
Enzymes
isolation
Muscle Cells
Muscle Contraction
Myocytes, Cardiac
Physical Examination
Primary Cell Culture
Sarcoplasmic Reticulum
Stimulations, Electric
Therapies, Investigational
Trypan Blue
Arm, Upper
Buttocks
Condyle
Ethics Committees, Research
factor A
Femur
Generic Drugs
Gracilis Muscle
Healthy Volunteers
Hip Joint
Homo sapiens
Joints
Joints, Ankle
Knee Joint
Lata, Fascia
Lower Extremity
Muscle, Gastrocnemius
Muscle Contraction
Muscle Tissue
Nervousness
Plant Roots
Rectus Femoris
Semimembranosus
Soleus Muscle
Surface Electromyography
Tendons
Vastus Lateralis
Vastus Medialis
Buffers
Cells
Microscopy
Muscle Cells
Muscle Contraction
Myocytes, Cardiac
Cell tractions were computed using constrained Fourier transform traction microscopy (FTTM).[14] (link) Briefly, the displacement field was computed by comparing fluorescent microbead images obtained during the experiment with a reference image obtained at the end of the experiment subsequent to detaching the cell from its underlying substrate. The projected cell area was calculated based on a manual trace of the cell contour determined from a phase contrast image obtained at the start of the experiment. Both cell shape and cell area were found to vary only marginally during the experiment. From the displacement field we calculated the traction field, and from the traction field we computed a scalar measure of contractility called the contractile moment, T.[14] (link) The contractile moment corresponds to the strength of an equivalent force dipole and provides thereby a scalar measure of the cell's contractile strength.
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Cells
Cell Shape
Microscopy
Microscopy, Phase-Contrast
Microspheres
Muscle Contraction
Traction
Bath
Microscopy
Muscle Cells
Muscle Contraction
Transients
Most recents protocols related to «Muscle Contraction»
Example 6
The organ bath system represents an ex vivo system lacking central nervous system (CNS) connections. Gastrointestinal motility is investigated using mice as an animal model. Experiments are performed to measure colonic contractility in conscious germ free (GF) and colonized mice with infusion of tryptamine by enema as well as following colonization of GF with tryptamine producing E. coli. The effect of tryptamine on epithelial biology also is determined.
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Animal Model
Bath
Central Nervous System
Colon
Consciousness
Enema
Escherichia coli
Gastrointestinal Motility
Mus
Muscle Contraction
Tryptamines
Example 3
Preparations of full-thickness colonic segments (˜1.5 cm) were allowed to equilibrate in 37° C. Kreb's-jacketed organ baths with their distal ends opening to a pressure transducer and maintained under basal pressure of 5-cm column of vehicle (RL). The proximal end was closed during pressure recordings but opened to allow luminal infusion of vehicle or tryptamine in solution (100 μM, 1 mM and 3 mM; 10 minutes per treatment; n=5-7 mice).
Contractile frequency was not significantly different comparing tryptamine treatments with vehicle controls; however, there was a trend toward increased frequency in segments treated with luminal 1 mM tryptamine compared to controls (5.9±0.8 vs 4.1±0.6; P=0.15). Mean contractile amplitude and contractile magnitude, as measured by area under the curve, were also not significantly different between control (vehicle alone) and any of the tryptamine concentrations examined. Contractile duration, measured at half amplitude, was not significantly different between vehicle controls and any of the luminal tryptamine treatments.
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Bath
Colon
Mus
Muscle Contraction
Phenobarbital
Pressure
Transducers, Pressure
Tryptamines
Example 7
Intestinal microbiota having at least one tryptophan decarboxylase enzyme (e.g., C. sporogenes and R. gnavus) is given orally (in the form of a probiotic, prebiotic, or symbiotic) to a subject. The subject is evaluated for the presence of the provided bacteria (e.g., probiotic bacteria) in the intestine, production of tryptamine in the intestine, and improved gastrointestinal epithelial function (e.g., colonic contractility). Subjects include GF, HM, 5HTR4 KO, and WT mice. Subjects also include animals (e.g., humans) having a gastrointestinal disorder.
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Animals
Aromatic-L-Amino-Acid Decarboxylases
Bacteria
Colon
Defecation
Enzymes
Gastrointestinal Diseases
Gastrointestinal Microbiome
Homo sapiens
Intestines
Mus
Muscle Contraction
Prebiotics
Probiotics
Symbiosis
Tryptamines
All participants were scheduled to have CMR-LGE examination just before each CPET. CMR-LGE examination involved a 3.0-Tesla Skyra scanner (Siemens Medical Systems, Erlangen, Germany) operating on the VD13 platform with a 32-channel phased-array receiver body coil. Short-axis (contiguous 8-mm-thick slices) and standard long-axis view (2-, 3- and 4-chamber views) cine images were obtained by steady-state free precession (SSFP) cine imaging with the following parameters: repetition time, 45 ms; echo time, 1.4 ms; matrix, 256 × 256; and field of view, 34 to 40 cm. LV geometry as well as functions, including LV end-diastolic volume (LVEDV), LV end-systolic volume (LVESV), resting CO (COrest), LVEF, LV mass, and left ventricle wall motion (LVWMS) were determined using SSFP cine imaging. The lower the LVWMS is, the better the LV contractility [28 (link)].
Quantitative parametric images of myocardial extracellular volume (ECV) fractions were acquired from longitudinal relaxation time (T1) mapping in short-axis slices before (pre) and after (post) contrast medium enhancement. The ECV was estimated by the following equation:
The CMR-LGE system determines the T1 in each myocardial segment. Myocardial fibrosis was estimated with a modified Look-Locker inversion-recovery (MOLLI) sequence [15 (link)] acquired during the end-expiratory phase in the basal, middle and apical LV myocardial segments at short-axes before (T1myo pre) and approximately 15 to 20 min after (T1myo post) a 0.1 mmol/kg intravenous dose of gadolinium-DOTA (gadoterate meglumine, Dotarem, Guerbet S.A., France). The ECV value was further normalized by the blood T1 mapping image before (T1blood pre) and after (T1blood post) enhancement in the corresponding short-axis slices. The basal slice (Base), mid-cavity slice (Middle), and apical slice (Apex) of LV myocardial segments [29 (link)] were drawn along the epicardial and endocardial surfaces on matched pre- and post-contrast MOLLI images to identify the myocardium for ECV analysis.
Quantitative parametric images of myocardial extracellular volume (ECV) fractions were acquired from longitudinal relaxation time (T1) mapping in short-axis slices before (pre) and after (post) contrast medium enhancement. The ECV was estimated by the following equation:
The CMR-LGE system determines the T1 in each myocardial segment. Myocardial fibrosis was estimated with a modified Look-Locker inversion-recovery (MOLLI) sequence [15 (link)] acquired during the end-expiratory phase in the basal, middle and apical LV myocardial segments at short-axes before (T1myo pre) and approximately 15 to 20 min after (T1myo post) a 0.1 mmol/kg intravenous dose of gadolinium-DOTA (gadoterate meglumine, Dotarem, Guerbet S.A., France). The ECV value was further normalized by the blood T1 mapping image before (T1blood pre) and after (T1blood post) enhancement in the corresponding short-axis slices. The basal slice (Base), mid-cavity slice (Middle), and apical slice (Apex) of LV myocardial segments [29 (link)] were drawn along the epicardial and endocardial surfaces on matched pre- and post-contrast MOLLI images to identify the myocardium for ECV analysis.
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BLOOD
Cardiovascular System
Clostridium perfringens epsilon-toxin
Dental Caries
Diastole
Dotarem
ECHO protocol
Endocardium
Epistropheus
Exhaling
Fibrosis
Gadolinium
gadolinium 1,4,7,10-tetraazacyclododecane-N,N',N'',N'''-tetraacetate
gadoterate meglumine
Human Body
Inversion, Chromosome
Left Ventricles
Muscle Contraction
Myocardium
Sequence Inversion
Systole
Volumes, Packed Erythrocyte
Myosin II was purified from
rabbit skeletal muscle and fluorescently labeled with DyeLight 488
(Invitrogen, Carlsbad, CA, USA) according to Alvarado and Koenderink.66 (link) Labeled
and unlabeled myosin II were stored separately in myosin storage buffer
(300 mM KCl, 25 mM KH2PO4, 0.5 mM DTT, 50% (v/v)
glycerol, pH 6.5), where the high ionic strength prevents myosin self-assembly
into bipolar filaments. For experiments, myosin II was dialyzed overnight
in glycerol-free myosin buffer (300 mM KCl, 20 mM imidazol, 4 mM MgCl2, 1 mM DTT, pH 7.4) and controlled self-assembly into bipolar
filaments was induced by adjusting a KCl concentration of 50 mM via
mixing with myosin polymerization buffer (20 mM imidazol, 1.6 mM MgCl2, 1 mM DTT, 1.2 mM Trolox, pH 7.4). After an incubation time
of 10 min at 20 °C, the bipolar myosin II filaments were immediately
used for contractile experiments. For the contraction experiments,
the F-actin networks were transferred into an actomyosin buffer by
a 10-fold buffer exchange (50 mM KCl, 20 mM imidazol, 2 mM MgCl2, 1 mM DTT, 1 mM Trolox, pH 7.4). The reorganization of the
networks was performed at a final ATP concentration of 0.1 mM combined
with an ATP-regeneration system of creatine phosphate (10 mM)/creatine
kinase (0.1 mg/mL)66 (link) and a myosin II concentration
of 0.4 μM.
rabbit skeletal muscle and fluorescently labeled with DyeLight 488
(Invitrogen, Carlsbad, CA, USA) according to Alvarado and Koenderink.66 (link) Labeled
and unlabeled myosin II were stored separately in myosin storage buffer
(300 mM KCl, 25 mM KH2PO4, 0.5 mM DTT, 50% (v/v)
glycerol, pH 6.5), where the high ionic strength prevents myosin self-assembly
into bipolar filaments. For experiments, myosin II was dialyzed overnight
in glycerol-free myosin buffer (300 mM KCl, 20 mM imidazol, 4 mM MgCl2, 1 mM DTT, pH 7.4) and controlled self-assembly into bipolar
filaments was induced by adjusting a KCl concentration of 50 mM via
mixing with myosin polymerization buffer (20 mM imidazol, 1.6 mM MgCl2, 1 mM DTT, 1.2 mM Trolox, pH 7.4). After an incubation time
of 10 min at 20 °C, the bipolar myosin II filaments were immediately
used for contractile experiments. For the contraction experiments,
the F-actin networks were transferred into an actomyosin buffer by
a 10-fold buffer exchange (50 mM KCl, 20 mM imidazol, 2 mM MgCl2, 1 mM DTT, 1 mM Trolox, pH 7.4). The reorganization of the
networks was performed at a final ATP concentration of 0.1 mM combined
with an ATP-regeneration system of creatine phosphate (10 mM)/creatine
kinase (0.1 mg/mL)66 (link) and a myosin II concentration
of 0.4 μM.
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Actomyosin
Buffers
Cytoskeletal Filaments
F-Actin
Glycerin
imidazole
Magnesium Chloride
Muscle Contraction
Myosin ATPase
Myosin Type II
Phosphocreatine
Polymerization
Regeneration
Skeletal Muscles
Trolox C
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Fura-2 AM is a fluorescent calcium indicator used for measuring intracellular calcium levels. It is a cell-permeable derivative of the parent compound Fura-2. Fura-2 AM can be loaded into cells, where intracellular esterases cleave off the acetoxymethyl (AM) ester group, trapping the Fura-2 indicator inside the cell.
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Blebbistatin is a small molecule that selectively inhibits non-muscle myosin II ATPase activity. It is commonly used as a research tool in cell biology and biochemistry studies.
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The MyoPacer is a laboratory instrument designed to stimulate muscle tissue samples. It provides electrical stimulation to elicit and measure the contractile responses of muscle samples under controlled conditions.
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Prism 9 is a powerful data analysis and graphing software developed by GraphPad. It provides a suite of tools for organizing, analyzing, and visualizing scientific data. Prism 9 offers a range of analysis methods, including curve fitting, statistical tests, and data transformation, to help researchers and scientists interpret their data effectively.