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Journal articles on the topic 'Cardiac Myosin ATPase Inhibition'

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Published: 7 June 2025

Last updated: 2 August 2025

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1

Tang, Wanjian, William C. Unrath, Rohini Desetty, and Christopher M. Yengo. "Dilated cardiomyopathy mutation in the converter domain of human cardiac myosin alters motor activity and response to omecamtiv mecarbil." Journal of Biological Chemistry 294, no. 46 (2019): 17314–25. http://dx.doi.org/10.1074/jbc.ra119.010217.

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We investigated a dilated cardiomyopathy (DCM) mutation (F764L) in human β-cardiac myosin by determining its motor properties in the presence and absence of the heart failure drug omecamtive mecarbil (OM). The mutation is located in the converter domain, a key region of communication between the catalytic motor and lever arm in myosins, and is nearby but not directly in the OM-binding site. We expressed and purified human β-cardiac myosin subfragment 1 (M2β-S1) containing the F764L mutation, and compared it to WT with in vitro motility as well as steady-state and transient kinetics measurement

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2

Hartmund, T., and H. Gesser. "Cardiac force and high-energy phosphates under metabolic inhibition in four ectothermic vertebrates." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 271, no. 4 (1996): R946—R954. http://dx.doi.org/10.1152/ajpregu.1996.271.4.r946.

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Isometric twitch tension of ventricular preparations stimulated at 0.2 Hz fell over 30 min of anoxia by a fraction decreasing in the order rainbow trout, cod, eel, and freshwater turtle. Drops in the estimated cytoplasmic energy state were related to larger tension losses for trout than for the other species, possibly due to larger changes in free phosphate. Anoxic energy degradation was slower for turtle than for the other species. Anoxia combined with glycolytic inhibition (1 mmol/l iodoacetate) enhanced the decrease in twitch tension for a drop in energy state and enlarged the increase in A

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3

Vander Roest, Alison Schroer, Chao Liu, Makenna M. Morck та ін. "Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super relaxed state". Proceedings of the National Academy of Sciences 118, № 24 (2021): e2025030118. http://dx.doi.org/10.1073/pnas.2025030118.

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Hypertrophic cardiomyopathy (HCM) is the most common inherited form of heart disease, associated with over 1,000 mutations, many in β-cardiac myosin (MYH7). Molecular studies of myosin with different HCM mutations have revealed a diversity of effects on ATPase and load-sensitive rate of detachment from actin. It has been difficult to predict how such diverse molecular effects combine to influence forces at the cellular level and further influence cellular phenotypes. This study focused on the P710R mutation that dramatically decreased in vitro motility velocity and actin-activated ATPase, in c

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4

Lim, Megan S., and Michael P. Walsh. "Phosphorylation of skeletal and cardiac muscle C-proteins by the catalytic subunit of cAMP-dependent protein kinase." Biochemistry and Cell Biology 64, no. 7 (1986): 622–30. http://dx.doi.org/10.1139/o86-086.

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Catecholamines are known to influence the contractility of cardiac and skeletal muscles, presumably via cAMP-dependent phosphorylation of specific proteins. We have investigated the in vitro phosphorylation of myofibrillar proteins by the catalytic subunit of cAMP-dependent protein kinase of fast- and slow-twitch skeletal muscles and cardiac muscle with a view to gaining a better understanding of the biochemical basis of catecholamine effects on striated muscles. Incubation of canine red skeletal myofibrils with the isolated catalytic subunit of cAMP-dependent protein kinase and Mg-[γ-32P]ATP

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5

Toepfer, Christopher N., Hiroko Wakimoto, Amanda C. Garfinkel, et al. "Hypertrophic cardiomyopathy mutations in MYBPC3 dysregulate myosin." Science Translational Medicine 11, no. 476 (2019): eaat1199. http://dx.doi.org/10.1126/scitranslmed.aat1199.

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The mechanisms by which truncating mutations in MYBPC3 (encoding cardiac myosin-binding protein C; cMyBPC) or myosin missense mutations cause hypercontractility and poor relaxation in hypertrophic cardiomyopathy (HCM) are incompletely understood. Using genetic and biochemical approaches, we explored how depletion of cMyBPC altered sarcomere function. We demonstrated that stepwise loss of cMyBPC resulted in reciprocal augmentation of myosin contractility. Direct attenuation of myosin function, via a damaging missense variant (F764L) that causes dilated cardiomyopathy (DCM), normalized the incre

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6

SMITH, Gerry A., Jamie I. VANDENBERG, Nicholas S. FREESTONE, and Henry B. F. DIXON. "The effect of Mg2+ on cardiac muscle function: is CaATP the substrate for priming myofibril cross-bridge formation and Ca2+ reuptake by the sarcoplasmic reticulum?" Biochemical Journal 354, no. 3 (2001): 539–51. http://dx.doi.org/10.1042/bj3540539.

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Kinetics are established for the activation of the myofibril from the relaxed state [Smith, Dixon, Kirschenlohr, Grace, Metcalfe and Vandenberg (2000) Biochem. J. 346, 393–402]. These require two troponin Ca2+-binding sites, one for each myosin head, to act as a single unit in initial cross-bridge formation. This defines the first, or activating, ATPase reaction, as distinct from the further activity of the enzyme that continues when a cross-bridge to actin is already established. The pairing of myosin heads to act as one unit suggests a possible alternating mechanism for muscle action. A larg

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7

Yutisha, Deshmukh* Tejashri Kadu Sachin Dighade. "Recent Therapy and Clinical Approaches for Hypertrophic Cardiomyopathy." International Journal of Pharmaceutical Sciences 3, no. 3 (2025): 728–38. https://doi.org/10.5281/zenodo.14998473.

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Hypertrophic cardiomyopathy (HCM) is a genetic cardiac condition characterized by abnormal thickening of the myocardium, often due to mutations in sarcomere protein genes. This leads to complications like arrhythmias, left ventricular outflow tract obstruction (LVOT), and sudden cardiac death (SCD). Recent advancements have highlighted the importance of early diagnosis using echocardiography, genetic testing, and advanced imaging. Among the therapeutic innovations, Mavacamten, an allosteric cardiac myosin ATPase inhibitor, offers a novel approach by reducing myocardial hypercontractility and i

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8

Makhija, Mahima, Alka Bansal, Punam Jakhar, Lokendra Sharma, Susheel Kumar, and Dharmendra Gupta. "Mavacamten: a novel avenue towards hypertrophic obstructive cardiomyopathy." International Journal of Basic & Clinical Pharmacology 13, no. 4 (2024): 568–72. http://dx.doi.org/10.18203/2319-2003.ijbcp20241661.

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Hypertrophic obstructive cardiomyopathy (HCM) is the most common heterogeneous genetic cardiovascular disorder. Its pathophysiology involves left ventricular hypertrophy, increased fibrosis, hypercontractility, and reduced compliance. The symptomatic obstructive HCM presents as dyspnoea, syncope, chest pain, palpitations, arrhythmias, or sudden death, usually after provocative manoeuvres like exercise. Until April 2022, treatment options were disease non-specific like Beta blockers, Cardio-selective Calcium Channel Blockers, Dipyridamole, and Ranolazine. Mavacamten is a first-in-class, FDA-app

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9

Tahiliani, Arun G., and John H. McNeill. "Prevention of diabetes-induced myocardial dysfunction in rats by methyl palmoxirate and triiodothyronine treatment." Canadian Journal of Physiology and Pharmacology 63, no. 8 (1985): 925–31. http://dx.doi.org/10.1139/y85-153.

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Diabetes results in myocardial functional alterations which are accompanied by a depression of biochemical parameters such as myosin ATPase and calcium uptake in the sarcoplasmic reticulum. Methyl palmoxirate, a fatty acid analog, is reported to decrease circulating glucose levels by inhibiting fatty acid metabolism, thus forcing carbohydrate utilization. In the present study, we attempted to prevent streptozotocin diabetes-induced myocardial alterations in the rat. Using the isolated working heart preparation, we observed a depression of myocardial function in rats 6 weeks after the induction

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10

Wu, Li-Ling, Chaoshu Tang, and Maw-Shung Liu. "Altered phosphorylation and calcium sensitivity of cardiac myofibrillar proteins during sepsis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 281, no. 2 (2001): R408—R416. http://dx.doi.org/10.1152/ajpregu.2001.281.2.r408.

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Altered phosphorylation and Ca2+ sensitivity of cardiac myofibrillar proteins during different phases of sepsis were investigated. Sepsis was induced by cecal ligation and puncture (CLP). The results show that phosphorylation of troponin I (TnI) was increased by 268% during the early phase (9 h after CLP) but decreased by 46% during the late phase (18 h after CLP) of sepsis. Phosphorylation of C protein was increased by 76% during the early phase but decreased by 41% during the late phase of sepsis. Phosphorylation of myosin light chain-2 (MLC-2) remained unaltered during the early phase but w

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11

McClellan, G., A. Weisberg, and S. Winegrad. "cAMP can raise or lower cardiac actomyosin ATPase activity depending on alpha-adrenergic activity." American Journal of Physiology-Heart and Circulatory Physiology 267, no. 2 (1994): H431—H442. http://dx.doi.org/10.1152/ajpheart.1994.267.2.h431.

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Adenosine 3',5'-cyclic monophosphate (cAMP) or beta-adrenergic stimulation has been shown to increase actomyosin adenosinetriphosphatase (ATPase) activity in cardiac muscle. Because the major catecholamine transmitters have both alpha- and beta-adrenergic activity, the possibility of a role for alpha-adrenergic stimulation in the regulation of ATPase activity has been investigated. Histochemical measurement of actomyosin ATPase activity in quickly frozen rat hearts has been used as the assay of enzymatic function of the contractile proteins. The dose-response curve of ATPase activity to cAMP s

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12

Scellini, Beatrice, Nicoletta Piroddi, Marica Dente, et al. "Myosin Isoform-Dependent Effect of Omecamtiv Mecarbil on the Regulation of Force Generation in Human Cardiac Muscle." International Journal of Molecular Sciences 25, no. 18 (2024): 9784. http://dx.doi.org/10.3390/ijms25189784.

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Omecamtiv mecarbil (OM) is a small molecule that has been shown to improve the function of the slow human ventricular myosin (MyHC) motor through a complex perturbation of the thin/thick filament regulatory state of the sarcomere mediated by binding to myosin allosteric sites coupled to inorganic phosphate (Pi) release. Here, myofibrils from samples of human left ventricle (β-slow MyHC-7) and left atrium (α-fast MyHC-6) from healthy donors were used to study the differential effects of μmolar [OM] on isometric force in relaxing conditions (pCa 9.0) and at maximal (pCa 4.5) or half-maximal (pCa

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13

Chu, Miensheng, Yevgeniya Koshman, Rekha Iyengar, Taehoon Kim, Brenda Russell, and Allen M. Samarel. "Contractile Activity Regulates Inducible Nitric Oxide Synthase Expression and NOi Production in Cardiomyocytes via a FAK-Dependent Signaling Pathway." Journal of Signal Transduction 2012 (July 26, 2012): 1–11. http://dx.doi.org/10.1155/2012/473410.

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Intracellular nitric oxide (NOi) is a physiological regulator of excitation-contraction coupling, but is also involved in the development of cardiac dysfunction during hypertrophy and heart failure. To determine whether contractile activity regulates nitric oxide synthase (NOS) expression, spontaneously contracting, neonatal rat ventricular myocytes (NRVM) were treat with L-type calcium channel blockers (nifedipine and verapamil) or myosin II ATPase inhibitors (butanedione monoxime (BDM) and blebbistatin) to produce contractile arrest. Both types of inhibitors significantly reduced iNOS but no

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14

Rouslin, W., and C. W. Broge. "Isoform-independent heart rate-related variation in cardiac myofibrillar Ca(2+)-activated Mg(2+)-ATPase activity." American Journal of Physiology-Cell Physiology 270, no. 5 (1996): C1271—C1276. http://dx.doi.org/10.1152/ajpcell.1996.270.5.c1271.

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In the present study, we compared the activities of the cardiac myofibrillar Ca(2+)-activated Mg(2+)-ATPase and the content of cardiac muscle mitochondrial ATPase inhibitor protein (IF1) of several mammalian species covering broad ranges of body mass and heart rate, i.e., from beef cattle to mouse. The cardiac myofibrillar ATPase from each species was assayed over a range of pCa values at pH 7.4. While the cardiac myofibrillar ATPase from all species examined showed essentially identical Ca2+ concentration dependencies with the ATPase in each species activating steeply between pCa 6.5 and 5.5,

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15

Lim, M. S., and M. P. Walsh. "The effects of caldesmon on the ATPase activities of rabbit skeletal-muscle myosin." Biochemical Journal 238, no. 2 (1986): 523–30. http://dx.doi.org/10.1042/bj2380523.

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We studied the effects of caldesmon, a major actin- and calmodulin-binding protein found in a variety of muscle and non-muscle tissues, on the various ATPase activities of skeletal-muscle myosin. Caldesmon inhibited the actin-activated myosin Mg2+-ATPase, and this inhibition was enhanced by tropomyosin. In the presence of the troponin complex and tropomyosin, caldesmon inhibited the Ca2+-dependent actomyosin Mg2+-ATPase; this inhibition could be partly overcome by Ca2+/calmodulin. Caldesmon, phosphorylated to the extent of approximately 4 mol of Pi/mol of caldesmon, inhibited the actin-activat

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16

Afzal, N., G. N. Pierce, V. Elimban, R. E. Beamish, and N. S. Dhalla. "Influence of verapamil on some subcellular defects in diabetic cardiomyopathy." American Journal of Physiology-Endocrinology and Metabolism 256, no. 4 (1989): E453—E458. http://dx.doi.org/10.1152/ajpendo.1989.256.4.e453.

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The effects of verapamil on cardiac myofibrillar adenosinetriphosphatase (ATPase) activity, myosin ATPase, and myosin isoenzyme profile as well as sarcoplasmic reticular Ca2+ uptake and ATPase activities were examined in Sprague-Dawley rats made diabetic with a single injection of streptozotocin (65 mg/kg). Myofibrillar ATPase activity and myosin Ca2+ ATPase activity as well as Ca2+ uptake and Ca2+-stimulated ATPase activities of the sarcoplasmic reticulum were significantly decreased in diabetic hearts in comparison to the control values. The myosin isoenzyme component V3 was prominent in dia

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17

Pagh, K., and G. Gerisch. "Monoclonal antibodies binding to the tail of Dictyostelium discoideum myosin: their effects on antiparallel and parallel assembly and actin-activated ATPase activity." Journal of Cell Biology 103, no. 4 (1986): 1527–38. http://dx.doi.org/10.1083/jcb.103.4.1527.

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Eight monoclonal antibodies that bind to specific sites on the tail of Dictyostelium discoideum myosin were tested for their effects on polymerization and ATPase activity. Two antibodies that bind close to the myosin heads inhibited actin activation of the ATPase either partially or completely, without having an effect on polymerization. Two other antibodies bind to sites within the distal portion of the tail that has been shown, by cleavage mapping, to be important for polymerization. One of these antibodies binds close to the sites of heavy chain phosphorylation which is known to regulate bo

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18

Powers, F. M., and R. J. Solaro. "Caffeine alters cardiac myofilament activity and regulation independently of Ca2+ binding to troponin C." American Journal of Physiology-Cell Physiology 268, no. 6 (1995): C1348—C1353. http://dx.doi.org/10.1152/ajpcell.1995.268.6.c1348.

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We investigated the mechanism by which caffeine influences myofilament responsiveness to Ca2+ by measuring isometric force, Ca2+ binding, and ATPase activity of dog cardiac myofilament proteins. Caffeine (20 mM) increased submaximal and depressed maximal force in skinned fiber bundles. Although the Ca2+ sensitivity of myofilament activity was increased by caffeine, there was no effect on Ca2+ binding to troponin C (TnC) in skinned fiber bundles. To determine if caffeine altered actin-myosin interaction or affected myosin directly, myofibrillar, actomyosin, and myosin ATPase activities were mea

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19

Geenen, D. L., A. Malhotra, and J. Scheuer. "Regional variation in rat cardiac myosin isoenzymes and ATPase activity after infarction." American Journal of Physiology-Heart and Circulatory Physiology 256, no. 3 (1989): H745—H750. http://dx.doi.org/10.1152/ajpheart.1989.256.3.h745.

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Three and 11 wk after coronary artery ligation in rats, the right and left ventricular free wall, septum, and papillary muscles from infarcted and sham-operated hearts were analyzed to determine whether regional variability existed in cardiac actomyosin adenosine triphosphate (ATPase) activity and myosin isoenzymes. Infarction produced a 74% greater right ventricular mass and 19% greater septal mass compared with sham-operated hearts at 3 wk. There was no additional increase in cardiac mass associated with infarction from 3 to 11 wk above that expected for normal growth. Actomyosin ATPase acti

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20

Phan, Brigitte, and Emil Reisler. "Inhibition of myosin ATPase by beryllium fluoride." Biochemistry 31, no. 20 (1992): 4787–93. http://dx.doi.org/10.1021/bi00135a007.

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21

De La Cruz, Enrique M., H. Lee Sweeney, and E. Michael Ostap. "ADP Inhibition of Myosin V ATPase Activity." Biophysical Journal 79, no. 3 (2000): 1524–29. http://dx.doi.org/10.1016/s0006-3495(00)76403-4.

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22

Malhotra, A., J. P. Mordes, L. McDermott, and T. F. Schaible. "Abnormal cardiac biochemistry in spontaneously diabetic Bio-Breeding/Worcester rat." American Journal of Physiology-Heart and Circulatory Physiology 249, no. 5 (1985): H1051—H1055. http://dx.doi.org/10.1152/ajpheart.1985.249.5.h1051.

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Diabetes produced by injection of alloxan or streptozotocin results in cardiac dysfunction in rats that is associated with lower cardiac contractile protein ATPase activity. The purpose of this investigation was to examine cardiac myosin biochemistry in the Bio-Breeding Worcester (BB/W) rat, a strain in which diabetes occurs spontaneously and closely resembles insulin-dependent diabetes in humans. Hearts from diabetic BB/W rats were studied at 1, 4, and 7 mo after the onset of diabetes and were compared with age-matched BB/W rats that were bred for resistance to diabetes. Calcium-stimulated my

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23

Dillmann, W. H. "Methyl palmoxirate increases Ca2+-myosin ATPase activity and changes myosin isoenzyme distribution in the diabetic rat heart." American Journal of Physiology-Endocrinology and Metabolism 248, no. 5 (1985): E602—E606. http://dx.doi.org/10.1152/ajpendo.1985.248.5.e602.

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Previous studies have shown that in rats diabetes mellitus leads to a decrease in cardiac ventricle myosin V1 and an increase in myosin V3 levels. Insulin administration reverts myosin isoenzyme distribution to normal levels. It is currently unclear whether the effects of insulin on myosin isoenzyme distribution are a direct effect of the hormone or are mediated through insulin-induced alterations in cardiac metabolism. To gain further insight into this question diabetic rats received methyl palmoxirate, a potent inhibitor of long-chain fatty acid oxidation. Administration of 25 mg methyl palm

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24

Bogutska, K. I., O. V. Tsimbalyuk, and V. M. Danilova. "Peculiarities of cardiac muscle myosin ATPase functioning." Biopolymers and Cell 18, no. 4 (2002): 297–300. http://dx.doi.org/10.7124/bc.00060e.

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25

Morris, G. S., K. M. Baldwin, J. M. Lash, R. L. Hamlin, and W. M. Sherman. "Exercise alters cardiac myosin isozyme distribution in obese Zucker and Wistar rats." Journal of Applied Physiology 69, no. 1 (1990): 380–83. http://dx.doi.org/10.1152/jappl.1990.69.1.380.

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Recent evidence suggests that exercise training may significantly increase the expression of the cardiac myosin isozyme V1 in the diabetic heart, a change associated with improved cardiac functional capacity. To test this hypothesis, cardiac myofibrillar adenosinetriphosphatase (ATPase) activity and myosin isozyme profiles were determined in trained and sedentary male hyperinsulinemic obese Zucker (OZT, OZS) and obese Wistar (OWT, OWS) rats. Lean sedentary (LZS, LWS) animals served as age-matched controls. Myofibrillar ATPase activity and the relative quantity of the high-ATPase isozyme V1 was

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26

Winegrad, Saul, George McClellan, Andrea Weisberg, Lin Er Lin, Steven Weindling та Robert Horowits. "β-Adrenergic regulation of cardiac myosin". Canadian Journal of Physiology and Pharmacology 65, № 4 (1987): 606–9. http://dx.doi.org/10.1139/y87-102.

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Calcium-independent regulation of the contractile proteins of cardiac muscle has been studied using hyperpermeable cells from rat ventricles and sections of quickly frozen rat hearts. These preparations have been used to study maximum calcium-activated force, myosin ATPase activity, and the maximum velocity of unloaded shortening. β-adrenergic activity increases the amount of force and the ATPase activity in accordance with the concentration of the V1 isozyme of myosin. V3 activity is decreased at the same time. In tissues containing only V1, there is no change in maximum velocity in response

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27

Liu, Haidun, Mary Henein, Maria Anillo, and John F. Dawson. "Cardiac actin changes in the actomyosin interface have different effects on myosin duty ratio." Biochemistry and Cell Biology 96, no. 1 (2018): 26–31. http://dx.doi.org/10.1139/bcb-2017-0136.

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Hypertrophic cardiomyopathy (HCM) is an inherited cardiovascular disease (CD) that commonly causes an increased size of cardiomyocytes in the left ventricle. The proteins myosin and actin interact in the myocardium to produce contraction through the actomyosin ATPase cycle. The duty ratio (r) of myosin is the proportion of the actomyosin ATPase cycle that myosin is bound to actin and does work. A common hypothesis is that HCM mutations increase contraction in cardiac sarcomeres; however, the available data are not clear on this connection. Based on previous work with human α-cardiac actin (ACT

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Liou, Ying-Ming, Meei Jyh Jiang, and Ming-Che Wu. "Altered Expression of Cardiac Myosin Isozymes Associated with the Malignant Hyperthermia Genotype in Swine." Anesthesiology 93, no. 5 (2000): 1312–19. http://dx.doi.org/10.1097/00000542-200011000-00026.

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Background Anesthetic-induced malignant hyperthermia (MH) in humans and pigs is associated with dramatic alterations in cardiac function. However, it remains controversial as to whether MH-associated cardiac symptoms represent a primary difference of myocardium or a secondary alteration consequent to increases in the hyperthermic stress. Here the authors describe changes in myosin isoform expression in the hearts of MH-susceptible pigs with and without prior exposure to halothane. Methods One group of pigs was diagnosed as MH susceptible by halothane challenge and Hal-1843 nucleotide examinati

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Sharma, R. V., R. J. Tomanek, and R. C. Bhalla. "Effect of swimming training on cardiac function and myosin ATPase activity in SHR." Journal of Applied Physiology 59, no. 3 (1985): 758–65. http://dx.doi.org/10.1152/jappl.1985.59.3.758.

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Male spontaneously hypertensive rats (SHR) and Wistar-Kyoto normotensive rats (WKY) were subjected to swimming training 6 times/wk, commencing at 4 wk of age, to determine whether this type of endurance exercise might alter contractile proteins and cardiac function in young adult SHR. The total duration of exercise was 190 h. Myofibrillar adenosinetriphosphatase (ATPase) activity was assayed at various free [Ca2+] ranging from 10(-7) to 10(-5) M. Ca2+-stimulated ATPase activity of actomyosin and purified myosin was determined at various Ca2+ concentrations both in the low and high ionic streng

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Pollack, P. S., A. Malhotra, F. S. Fein, and J. Scheuer. "Effects of diabetes on cardiac contractile proteins in rabbits and reversal with insulin." American Journal of Physiology-Heart and Circulatory Physiology 251, no. 2 (1986): H448—H454. http://dx.doi.org/10.1152/ajpheart.1986.251.2.h448.

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In rats, chronic diabetes is associated with depressed cardiac myosin ATPase activity and a shift from the predominant V1 isoenzyme to V3, correlating with depressed contractility. Rabbit myocardium consists mostly of the V3 isoenzyme, and therefore a switch to even more V3 isoenzyme in diabetes might not be possible and therefore not explain the mechanical abnormalities observed. To explore this, rabbits were made diabetic with 140-150 mg/kg of alloxan, and their hearts were studied 3 days, 1 mo, 3 mo, and 6 mo later. Ca2+-myosin-ATPase activity was decreased in the diabetic rabbit at 1, 3, a

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Higashihara, M., K. Takahata, and K. Kurokawa. "Effect of phosphorylation of myosin light chain by myosin light chain kinase and protein kinase C on conformational change and ATPase activities of human platelet myosin." Blood 78, no. 12 (1991): 3224–31. http://dx.doi.org/10.1182/blood.v78.12.3224.3224.

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Abstract Human platelet myosin forms 10S and 6S conformations, and its Ca(2+)- and Mg(2+)-ATPase activities are parallel with the transition between 10S and 6S conformation, as judged by the gel filtration, intrinsic fluorescence, and viscosity methods. The 20,000-dalton myosin light chain (LC20) is phosphorylated by both myosin light chain kinase (MLC kinase) and Ca2+, phospholipid-dependent protein kinase (protein kinase C [PKC]). The phosphorylation (1 mol of phosphate/mol of LC20) by MLC kinase shifts the equilibrium toward the 6S conformation, but that by PKC does not. The prephosphorylat

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Higashihara, M., K. Takahata, and K. Kurokawa. "Effect of phosphorylation of myosin light chain by myosin light chain kinase and protein kinase C on conformational change and ATPase activities of human platelet myosin." Blood 78, no. 12 (1991): 3224–31. http://dx.doi.org/10.1182/blood.v78.12.3224.bloodjournal78123224.

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Human platelet myosin forms 10S and 6S conformations, and its Ca(2+)- and Mg(2+)-ATPase activities are parallel with the transition between 10S and 6S conformation, as judged by the gel filtration, intrinsic fluorescence, and viscosity methods. The 20,000-dalton myosin light chain (LC20) is phosphorylated by both myosin light chain kinase (MLC kinase) and Ca2+, phospholipid-dependent protein kinase (protein kinase C [PKC]). The phosphorylation (1 mol of phosphate/mol of LC20) by MLC kinase shifts the equilibrium toward the 6S conformation, but that by PKC does not. The prephosphorylation of my

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Schaible, T., A. Malhotra, G. Ciambrone, P. Buttrick, and J. Scheuer. "Combined effects of hypertension and chronic running program on rat heart." Journal of Applied Physiology 63, no. 1 (1987): 322–27. http://dx.doi.org/10.1152/jappl.1987.63.1.322.

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Previous studies in hearts of female rats have demonstrated that ventricular hypertrophy due to systolic overload, when combined with hypertrophy induced by a chronic swimming program, results in increased cardiac performance and enhanced contractile protein activity compared with the effects of hypertension alone. To explore how a chronic running program affects the function of hypertensive hearts, renal hypertension was created in female rats, and the animals were subjected to a program of chronic treadmill running. Running alone caused enhanced cardiac function, an increase in myosin adenos

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Yamashita, H., S. Sugiura, T. Serizawa, et al. "Sliding velocity of isolated rabbit cardiac myosin correlates with isozyme distribution." American Journal of Physiology-Heart and Circulatory Physiology 263, no. 2 (1992): H464—H472. http://dx.doi.org/10.1152/ajpheart.1992.263.2.h464.

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To investigate the relationship between the mechanical and biochemical properties of cardiac myosin, the sliding velocity of isolated cardiac myosin obtained from both euthyroid and hyperthyroid rabbits on actin cables was measured with an in vitro motility assay system. Ten rabbits (T) were treated with L-thyroxine to induce hyperthyroidism, and eight nontreated animals (N) were used as controls. Myosin was purified from the left ventricles of anesthetized animals. Myosin isozyme content was analyzed by the pyrophosphate gel electrophoresis method, and myosin adenosinetriphosphatase (ATPase)

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Alpert, Norman R., Christine Brosseau, Andrea Federico, Maike Krenz, Jeffrey Robbins, and David M. Warshaw. "Molecular mechanics of mouse cardiac myosin isoforms." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 4 (2002): H1446—H1454. http://dx.doi.org/10.1152/ajpheart.00274.2002.

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Two myosin isoforms are expressed in myocardium, αα-homodimers (V1) and ββ-homodimers (V3). V1exhibits higher velocities and myofibrillar ATPase activities compared with V3. We also observed this for cardiac myosin from normal (V1) and propylthiouracil-treated (V3) mice. Actin velocity in a motility assay ( V actin) over V1 myosin was twice that of V3 as was the myofibrillar ATPase. Myosin's average force (Favg) was similar for V1 and V3. Comparing V actin and Favg across species for both V1 and V3, our laboratory showed previously (VanBuren P, Harris DE, Alpert NR, and Warshaw DM. Circ Res 77

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Park, Sungjo, Katalin Ajtai, and Thomas P. Burghardt. "Inhibition of myosin ATPase by metal fluoride complexes." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1430, no. 1 (1999): 127–40. http://dx.doi.org/10.1016/s0167-4838(98)00262-3.

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Rasicci, David V., Jinghua Ge, Adrien P. Chen, et al. "Early-Stage Alcoholic Cardiomyopathy Highlighted by Metabolic Remodeling, Oxidative Stress, and Cardiac Myosin Dysfunction in Male Rats." International Journal of Molecular Sciences 26, no. 14 (2025): 6766. https://doi.org/10.3390/ijms26146766.

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Chronic ethanol use can lead to alcoholic cardiomyopathy (ACM), while the impact on the molecular and cellular aspects of the myocardium is unclear. Accordingly, male Sprague-Dawley rats were exposed to an ethanol-containing diet for 16 weeks and compared with a control group that was fed an isocaloric diet. Histological measurements from H&E slides revealed no significant differences in cell size. A proteomic approach revealed that alcohol exposure leads to enhanced mitochondrial lipid metabolism, and electron microscopy revealed impairments in mitochondrial morphology/density. Cardiac my

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Rupp, Heinz, and Bernhard Maisch. "Separation of large mammalian ventricular myosin differing in ATPase activityThis paper is one of a selection of papers published in this Special Issue, entitled The Cellular and Molecular Basis of Cardiovascular Dysfunction, Dhalla 70th Birthday Tribute." Canadian Journal of Physiology and Pharmacology 85, no. 3-4 (2007): 326–31. http://dx.doi.org/10.1139/y07-032.

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To investigate a possible heterogeneity of human ventricular myosin, papillary muscles of patients with valvular dysfunction were examined using a modified native gel electrophoresis. Myosin was separated into 2 components termed VA and VB, whereby the VA to VB proportion appeared to depend on the ventricular load. The proportion of the faster migrating band VA was correlated (P < 0.05) with end-diastolic pressure and the aortic pressure-cardiac index product. The regression based on these variables accounted for 67% of the variation in VA (R2 = 0.67). The VA proportion was, however, not si

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Rohde, John A., Osha Roopnarine, David D. Thomas, and Joseph M. Muretta. "Mavacamten stabilizes an autoinhibited state of two-headed cardiac myosin." Proceedings of the National Academy of Sciences 115, no. 32 (2018): E7486—E7494. http://dx.doi.org/10.1073/pnas.1720342115.

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We used transient biochemical and structural kinetics to elucidate the molecular mechanism of mavacamten, an allosteric cardiac myosin inhibitor and a prospective treatment for hypertrophic cardiomyopathy. We find that mavacamten stabilizes an autoinhibited state of two-headed cardiac myosin not found in the single-headed S1 myosin motor fragment. We determined this by measuring cardiac myosin actin-activated and actin-independent ATPase and single-ATP turnover kinetics. A two-headed myosin fragment exhibits distinct autoinhibited ATP turnover kinetics compared with a single-headed fragment. M

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Farrar, R. P., J. W. Starnes, G. D. Cartee, P. Y. Oh, and H. L. Sweeney. "Effects of exercise on cardiac myosin isozyme composition during the aging process." Journal of Applied Physiology 64, no. 2 (1988): 880–83. http://dx.doi.org/10.1152/jappl.1988.64.2.880.

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The effects of aging and exercise on isoforms of cardiac myosin and Ca2+-activated actomyosin adenosinetriphosphatase (ATPase) activity were examined in Fischer 344 rats. Rats were divided into running (R) and age-matched sedentary (S) groups. The groups initiated their exercise program at either 3, 4, or 18 mo of age. Rats were killed at 10, 12, 24, or 27 mo of age. ATPase activity decreased 25% in the S group and 28% in the R group from 12 to 27 mo of age. The myosin isozyme patterns shifted in both S and R groups from a predominantly V1 isozyme form (63.8%) at 10 mo of age to a more equal d

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Buttrick, P. M., A. Malhotra, and J. Scheuer. "Effects of systolic overload and swim training on cardiac mechanics and biochemistry in rats." Journal of Applied Physiology 64, no. 4 (1988): 1466–71. http://dx.doi.org/10.1152/jappl.1988.64.4.1466.

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We have previously shown that swim conditioning corrects the depressed mechanical function and myosin adenosinetriphosphatase (ATPase) activities associated with renovascular hypertension (HTN) in the rat. The present study was designed to assess the effects of swim conditioning on another form of systolic overload, subdiaphragmatic suprarenal aortic stenosis. Cardiac mechanics in an isolated working heart apparatus and myosin enzymology were studied in four groups of rats: controls (C), animals with chronic systolic overload secondary to aortic constriction (St), swim-conditioning animals (Sw

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Hornby, L., N. Hamilton, D. Marshall, T. A. Salerno, M. H. Laughlin, and C. D. Ianuzzo. "Role of cardiac work in regulating myocardial biochemical characteristics." American Journal of Physiology-Heart and Circulatory Physiology 258, no. 5 (1990): H1482—H1490. http://dx.doi.org/10.1152/ajpheart.1990.258.5.h1482.

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The purpose of this study was to determine the extent to which functional demand regulates the biochemical character and enzyme capacities of the rat myocardium. Hearts from donor rats were heterotopically transplanted onto the abdominal aorta and inferior vena cava of isogenic recipients. The procedure results in a perfused but nonpumping heart that has a reduced heart rate (HR) and performs essentially no stroke work (SW). After 30 days, metabolic enzyme activities (phosphorylase, 6-phosphofructokinase, citrate synthase, and 3-hydroxyacyl-CoA dehydrogenase) were significantly lower (40-60%)

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Tiago, Teresa, Sónia Simão, Manuel Aureliano, Francisco Javier Martín-Romero, and Carlos Gutiérrez-Merino. "Inhibition of Skeletal Muscle S1-Myosin ATPase by Peroxynitrite†." Biochemistry 45, no. 11 (2006): 3794–804. http://dx.doi.org/10.1021/bi0518500.

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Ngai, P. K., and M. P. Walsh. "The effects of phosphorylation of smooth-muscle caldesmon." Biochemical Journal 244, no. 2 (1987): 417–25. http://dx.doi.org/10.1042/bj2440417.

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Caldesmon is a major calmodulin- and actin-binding protein of smooth muscle which interacts with calmodulin in a Ca2+-dependent manner or with actin in a Ca2+-independent manner. Isolated caldesmon is capable of inhibiting the actin-activated Mg2+-ATPase of smooth-muscle myosin, suggesting a possible physiological role for caldesmon in regulating the contractile state of smooth-muscle. Caldesmon can be phosphorylated in vitro by a co-purifying Ca2+/calmodulin-dependent protein kinase and dephosphorylated by a protein phosphatase, both of which are present in smooth muscle. We investigated furt

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Winder, S. J., C. Sutherland, and M. P. Walsh. "A comparison of the effects of calponin on smooth and skeletal muscle actomyosin systems in the presence and absence of caldesmon." Biochemical Journal 288, no. 3 (1992): 733–39. http://dx.doi.org/10.1042/bj2880733.

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Thiosphosphorylated smooth muscle myosin and skeletal muscle myosin, both of which express Ca(2+)-independent actin-activated MgATPase activity, were used to examine the functional effects of calponin and caldesmon separately and together. Separately, calponin and caldesmon inhibited the actin-activated MgATPase activities of thiophosphorylated smooth muscle myosin and skeletal muscle myosin, calponin being significantly more potent in both systems. Calponin-mediated inhibition resulted from the interaction of calponin with actin since it could be reversed by increasing the actin concentration

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Hecht, Gail, and Athanasia Koutsouris. "Myosin regulation of NKCC1: effects on cAMP-mediated Cl− secretion in intestinal epithelia." American Journal of Physiology-Cell Physiology 277, no. 3 (1999): C441—C447. http://dx.doi.org/10.1152/ajpcell.1999.277.3.c441.

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The basally located actin cytoskeleton has been demonstrated previously to regulate Cl−secretion from intestinal epithelia via its effects on the Na+-K+-2Cl−cotransporter (NKCC1). In nontransporting epithelia, inhibition of myosin light chain kinase (MLCK) prevents cell-shrinkage-induced activation of NKCC1. The aim of this study was to investigate the role of myosin in the regulation of secretagogue-stimulated Cl− secretion in intestinal epithelia. The human intestinal epithelial cell line T84 was used for these studies. Prevention of myosin light chain phosphorylation with the MLCK inhibitor

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Tahiliani, Arun G., and John H. McNeill. "Effects of triiodothyronine and carnitine therapy on myocardial dysfunction in diabetic rats." Canadian Journal of Physiology and Pharmacology 64, no. 6 (1986): 669–72. http://dx.doi.org/10.1139/y86-110.

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Streptozotocin-diabetic rats were treated with a combination of triiodothyronine and carnitine for 6 weeks. These compounds were used as they are known to correct the diabetes-induced depression of cardiac myosin ATPase and sarcoplasmic reticular (SR) calcium uptake, respectively. Myocardial performance, which was assessed using the working heart preparation, revealed a depression of function in untreated diabetics when compared with controls at most left atrial filling pressures. Hearts from diabetic rats treated with the combination exhibited depression at only the higher filling pressures a

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Trujillo, Adriana S., Karen H. Hsu, Joy Puthawala, et al. "Myosin dilated cardiomyopathy mutation S532P disrupts actomyosin interactions, leading to altered muscle kinetics, reduced locomotion, and cardiac dilation in Drosophila." Molecular Biology of the Cell 32, no. 18 (2021): 1690–706. http://dx.doi.org/10.1091/mbc.e21-02-0088.

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We explored the mechanism of human myosin–induced dilated cardiomyopathy (DCM) using the Drosophila melanogaster model system. We discovered that the S532P myosin DCM mutation reduces the actin-dependent ATPase activity and the actin-binding rate and increases the actin-detachment rate, leading to reduced muscle function and cardiac dilation.

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Morris, G. S., P. V. Fiore, R. L. Hamlin, and W. M. Sherman. "Effects of long-term cocaine administration and exercise on cardiac metabolism and isomyosin expression." Canadian Journal of Physiology and Pharmacology 72, no. 1 (1994): 1–5. http://dx.doi.org/10.1139/y94-001.

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Although chronic cocaine use is cardiotoxic, its use remains problematic in athletics. Hence adaptive changes induced in the heart by superimposing chronic cocaine use on an exercise training are of interest but remain poorly understood. Therefore this study investigated the effects of cocaine treatment combined with exercise training on the metabolic and contractile properties of the heart. Male Sprague–Dawley rats were assigned to one of four groups: normal sedentary (NS, n = 6), cocaine sedentary (CS, n = 6), normal trained (NT, n = 6), and cocaine trained (CT, n = 6). Trained animals were

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Gerzen, Oksana P., Veronika O. Votinova, Iulia K. Potoskueva, Alyona E. Tzybina, and Larisa V. Nikitina. "Direct Effects of Toxic Divalent Cations on Contractile Proteins with Implications for the Heart: Unraveling Mechanisms of Dysfunction." International Journal of Molecular Sciences 24, no. 13 (2023): 10579. http://dx.doi.org/10.3390/ijms241310579.

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The binding of calcium and magnesium ions to proteins is crucial for regulating heart contraction. However, other divalent cations, including xenobiotics, can accumulate in the myocardium and enter cardiomyocytes, where they can bind to proteins. In this article, we summarized the impact of these cations on myosin ATPase activity and EF-hand proteins, with special attention given to toxic cations. Optimal binding to EF-hand proteins occurs at an ionic radius close to that of Mg2+ and Ca2+. In skeletal Troponin C, Cd2+, Sr2+, Pb2+, Mn2+, Co2+, Ni2+, Ba2+, Mg2+, Zn2+, and trivalent lanthanides c

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