The effect of 2,3-butanedione 2-monoxime (BDM) on ventricular trabeculae from the avian heart

Brotto, Marco; Fogaça, R. T. H.; Creazzo, Tony L.; Godt, R. E.; Nosek, Thomas M.

doi:10.1007/bf00125305

Cited by 19 publications

(20 citation statements)

References 44 publications

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“…Ca release [12] and has also been shown to release Ca from the s.r. of avian ventricular trabeculae [4]. This interpretation is consistent with work on permeabilized canine myocytes, which found that a decrease of s.r.…”

Section: Introductionsupporting

confidence: 75%

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2,3-Butanedione monoxime (BDM) decreases sarcoplasmic reticulum Ca content by stimulating Ca release in isolated rat ventricular myocytes

Adams¹,

Trafford²,

Eisner³

1998

Pfl�gers Archiv European Journal of Physiology

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The effects of 2,3-butanedione monoxime (BDM) were examined using rat ventricular myocytes loaded with Indo-1 to measure the intracellular Ca concentration ([Ca2+]i). BDM (10 mM) produced a transient increase of the systolic Ca transient with no steady-state effect on its magnitude. This transient increase was more marked when BDM was applied after having decreased the external Ca concentration from 1 to 0.1 mM. There was a transient increase of resting [Ca2+]i in both quiescent and electrically stimulated cells. Prior application of BDM decreased the rise of [Ca2+]i produced by caffeine. In voltage-clamped cells the rise of [Ca2+]i produced by BDM was accompanied by a transient inward current attributed to the electrogenic Na-Ca exchange. The amount of Ca lost from the cell upon application of 10 mM BDM could be estimated either from the integral of the BDM-evoked current or from the reduction of the integral of a caffeine-evoked current and corresponded to about 50% of the sarcoplasmic reticulum (s.r.) Ca content. The decrease of s.r. Ca content and the transient potentiation of the systolic Ca transient suggest that BDM acts by stimulating Ca-induced Ca release. These effects must be allowed for when using BDM.

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Section: Introductionsupporting

confidence: 75%

“…One mechanism by which this may occur is a depression of the sarcolemmal L-type Ca current [1,4,6]. It has also been suggested that BDM may interfere with sarcoplasmic reticulum (s.r.)…”

Section: Introductionmentioning

confidence: 97%

2,3-Butanedione monoxime (BDM) decreases sarcoplasmic reticulum Ca content by stimulating Ca release in isolated rat ventricular myocytes

Adams¹,

Trafford²,

Eisner³

1998

Pfl�gers Archiv European Journal of Physiology

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“…The contractile properties of single Triton-skinned muscle fibers dissected from the four groups of muscle strips described above were determined as described by Brotto and Nosek [19,20]. The muscle fibers to be skinned were taken from the three muscle strips that had not been exposed to caffeine.…”

Section: Triton-skinned Muscle Fibersmentioning

confidence: 99%

Hypoxia and fatigue-induced modification of function and proteins in intact and skinned murine diaphragm muscle

Brotto

Leyen

Nosek

et al. 2000

Pflugers Arch - Eur J Physiol

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Fatigue studies of isolated, intact muscles typically utilize solutions saturated with O2. However, under in vivo fatiguing conditions, less oxygen is delivered to the muscles and they actually experience hypoxia. No studies to date have correlated the effects of acute hypoxia on the isometric contractile properties of intact muscles, skinned fibers isolated from the same muscles, and the cellular content of specific muscle proteins. Therefore, we have studied the effects of in vitro acute hypoxia on the fatigability of intact diaphragm muscle strips and on the isometric contractile properties of single Triton-skinned fibers isolated from control and hypoxic diaphragm muscles. We found that hypoxia and fatiguing stimulation per se affect the tetanic force of intact muscle strips without exhibiting any significant deleterious effects on the calcium-activated force of skinned muscle fibers dissected from the intact muscles. In contrast, fatiguing stimulation under hypoxic conditions decreased both the tetanic force of muscle strips and the calcium-activated force of skinned muscle fibers. Gel electrophoresis of muscles subjected to hypoxia and hypoxic-fatigue revealed that there is a significant reduction in three protein bands when compared to control muscles. Protein modification may be the underlying mechanism of muscle fatigue under physiologic conditions.

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“…At this concentration, BDM is known to suppress active myosin-actin interactions (e.g., Brotto et al, 1995). By applying this drug to the solution, we could therefore investigate whether such interactions contribute to passive tension.…”

Section: Strain Limit Of Cardiac Myofibrilsmentioning

confidence: 99%

Limits of titin extension in single cardiac myofibrils

Linke

Bartoo

Ivemeyer

et al. 1996

J Muscle Res Cell Motil

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Passive force and dynamic stiffness were measured in relaxed, single myofibrils from rabbit ventricle over a wide range of sarcomere lengths, from approximately 2-5 microns. Myofibril stretch up to sarcomere lengths of approximately 3 microns resulted in a steady increase in both force and stiffness. The shape of the length-force and the length-stiffness curves remained fully reproducible for repeated extensions to a sarcomere length of approximately 2.7 microns. Above this length, myofibrillar viscoelastic properties were apparently changed irreversibly, likely due to structural alterations within the titin (connectin) filaments. Stretch beyond approximately 3 microns sarcomere length resulted in a markedly reduced slope of the passive force curve, while the stiffness curve became flat. Thus, cardiac sarcomeres apparently reach a strain limit near a length of 3 microns. Above the strain limit, both curve types frequently showed a series of inflections, which we assumed to result from the disruption of titin-thick filament bonds and consequent addition of previously bound A-band titin segments to the elastic I-band titin portion. Indeed, we confirmed in immunofluorescence microscopic studies, using a monoclonal antibody against titin near the A/I junction, that upon sarcomere stretch beyond the strain limit length, the previously stationary antibody epitopes suddenly moved into the I-band, indicating A-band titin release. Altogether, the passive force/stiffness-length relation of cardiac myofibrils was qualitatively similar to, but quantitatively different from, that reported for skeletal myofibrils. From these results, we inferred that cardiac myofibrils have an approximately two times greater relative I-band titin extensibility than skeletal myofibrils. This could hint at differences in the maximum passive force-bearing capacity of titin filaments in the two muscle types.

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The effect of 2,3-butanedione 2-monoxime (BDM) on ventricular trabeculae from the avian heart

Cited by 19 publications

References 44 publications

2,3-Butanedione monoxime (BDM) decreases sarcoplasmic reticulum Ca content by stimulating Ca release in isolated rat ventricular myocytes

2,3-Butanedione monoxime (BDM) decreases sarcoplasmic reticulum Ca content by stimulating Ca release in isolated rat ventricular myocytes

Hypoxia and fatigue-induced modification of function and proteins in intact and skinned murine diaphragm muscle

Limits of titin extension in single cardiac myofibrils

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