Enhanced Ca2+-induced calcium release by isolated sarcoplasmic reticulum vesicles from malignant hyperthermia susceptible pig muscle

Mickelson, James R.; Ross, Julie A.; Reed, B K; Louis, Charles F.

doi:10.1016/0005-2736(86)90234-8

Cited by 93 publications

(37 citation statements)

References 52 publications

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“…The protein profile observed in Fig. 1A (lane a) was similar to that reported by others for porcine skeletal muscle SR preparations [17,24]. SDS-PAGE separations of SR fractions presented by these authors showed fewer bands, especially in the 30-60 kDa range.…”

supporting

confidence: 71%

Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins

Schulz

Palmer

Steckelberg

et al. 2006

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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supporting

confidence: 71%

Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins

Schulz

Palmer

Steckelberg

et al. 2006

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…The effect of breed can clearly be attributed to specific genetic mutations in the case of some highly selected lean pig lines. The first is a well-known mutation RYR1 T , causing a substitution of amino acids (Arg615Cys) in the ryanodine receptor (Fuji et al, 1991), the protein that is responsible for the release of Ca 21 from the sarcoplasmic reticulum (Mickelson et al, 1986). This mutation causes uncontrolled release of Ca…”

Section: Factors Affecting Raw Materials Propertiesmentioning

confidence: 99%

Factors in pig production that impact the quality of dry-cured ham: a review

Čandek-Potokar

Škrlep

2012

Animal

101

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This study reviews the factors of pig production that impact the quality of dry-cured ham. When processing is standardized, the quality of the final dry-cured product is primarily determined by the quality of the meat before curing (green ham). This has been defined as the aptitude for seasoning and is determined by the green ham weight, adipose tissue quantity and quality, meat physico-chemical properties and the absence of visual defects. Various ante-mortem factors including pig age and weight, genetic type, diet, feeding strategy and slaughter conditions determine green ham properties such as the dynamics of water loss, salt intake and, as a consequence, proteolysis and lipolysis. Muscle conditions (pH, salt concentration, water content and availability, temperature) influence enzymatic activity and development of characteristic texture and flavor. Generally, hams of older and heavier pigs present better seasoning aptitude because of higher adiposity. Adiposity is also positively correlated with fat saturation, which is desired to avoid rancidity and oiliness. The fatty acid profile of tissue lipids can be manipulated by diet composition. Feeding strategy affects tissue accretion and protein turnover, thus directly impacting proteolysis. With respect to the impact of pig genotype on dry-cured ham quality, local breeds are generally considered more suitable for producing quality dry hams; however, the majority of dry-cured hams on the market today are from modern pig breeds raised in conventional systems, providing lean hams. The importance of all these factors of pig production is discussed and synthesized, with an emphasis on the main difficulties encountered in dry-cured ham production.Keywords: dry-cured ham, pig production factors ImplicationsThe industry of dry-cured hams faces the challenge of how to create a product with desirable taste and nutritional properties. Consumers demand lean products, but lean hams have higher seasoning losses, higher salt intake, lower oxidative stability and lower eating quality. Meeting consumer demands for lower fat and salt content (two factors of nutritional quality) can increase problems related to sensory quality and consumer acceptance of dry ham. An understanding and control over pig production factors can help optimize the product without compromising its quality.

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“…This is consistent with the view that there is no time-dependent aspect to the blocking action of halothane during the rising phase of the HVA current and that blockade by halothane is at equilibrium at the time of the first measurable current flow. Halothane is known to enhance release of Ca*+ from the sarcoplasmic reticulum in skeletal muscle (Beeler and Gable, 1985;Mickelson et al, 1986), and it has been suggested that inhibition of Ca*+ current by halothane may reflect a halothane-induced elevation in intracellular Ca *+, thereby mediating Ca2+-dependent inactivation (Kmjevic, 1974;Krnjevic and Puil, 1988). Because LVA Ca2+ current is not thought to be subject to Ca*+-dependent inactivation, it seems unlikely that elevation of [Caz+], can account for the reduction in LVA.…”

Section: Effects Of Halothane On High-threshold Ca2+ Currentmentioning

confidence: 99%

“…It is unlikely that the release of Ca*+ from intracellular stores could appreciably elevate submembrane Ca2+ under such conditions. Third, a caffeine-releasable pool of intracellular Ca2+, a potential target of halothane action (Beeler and Gable, 1985;Mickelson et al, 1986), does not appear to be present in GH, cells. The present results also provide some information concerning the idea that halothane reduces HVA current either by mimicking the action of a G-protein or by activating a somatostatin-sensitive G-protein that inhibits the Ca*+ current .…”

Section: Mechanism Of Action Of Halothanementioning

confidence: 99%

Halothane inhibits two components of calcium current in clonal (GH3) pituitary cells

et al. 1991

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The effect of halothane on isolated calcium (Ca2+) current of clonal (GH3) pituitary cells was investigated using standard whole-cell clamp techniques at room temperature. Halothane (0.1–5.0 mM) reversibly reduced both the low-threshold, transient [low-voltage-activated (LVA)] component and the high-threshold [high-voltage-activated (HVA)] component of Ca2+ current. Halothane had little effect on the voltage dependence of activation or inactivation of either component of Ca2+ current. Inhibition of the peak high-threshold Ca2+ current was half- maximal at about 0.8 mM halothane, with maximal inhibition (100%) occurring with 5 mM halothane. When measured at the end of a 190-msec command step, half-maximal reduction of high-threshold current occurred at less than 0.5 mM halothane. The low-threshold transient current was less sensitive to halothane, with half-maximal inhibition of peak transient current activated at -30 mV occurring at approximately 1.3 mM. The effect of halothane on the HVA current was apparently not mediated by changes in intracellular Ca2+ concentration. The ability of halothane to inhibit Ca2+ current was unaffected by either the inclusion of the rapid Ca2+ buffer 1,2-bis(2-aminophenoxy)ethane N,N,N′,N′-tetraacetic acid (BAPTA) in the recording pipette or exposure of the cell to 10 mM caffeine. To assess the selectivity of the effect of halothane, the actions of halothane on two components of voltage- activated potassium (K+) current observed in the absence of extracellular Ca2+ and on voltage-dependent sodium (Na+) current were also examined. Halothane had no effect on the voltage-dependent, inactivating K+ current of GH3 cells at concentrations up to 1.2 mM. In contrast, the non-inactivating K+ current, though less sensitive to halothane than either Ca2+ current, was reduced by about 40% by 1.2 mM halothane at +20 mV. Peak Na+ current was also blocked by halothane, but 50% block required around 2.6 mM halothane with little effect at 1.6 mM. Reduction of Na+ current was associated with a substantial negative shift in the steady-state inactivation curve. Although the results indicate that a number of voltage-dependent ionic currents are sensitive to halothane, both components of Ca2+ current exhibit a greater sensitivity to halothane than any of three other voltage- dependent currents in GH3 cells. These results show that GH3 cell Ca2+ currents are selectively inhibited by clinically appropriate concentrations of halothane and that the reduction of Ca2+ current can account for the inhibition by halothane of TRH- or KCl-induced prolactin secretion in GH3 cells.

show abstract

Enhanced Ca2+-induced calcium release by isolated sarcoplasmic reticulum vesicles from malignant hyperthermia susceptible pig muscle

Cited by 93 publications

References 52 publications

Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins

Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins

Factors in pig production that impact the quality of dry-cured ham: a review

Halothane inhibits two components of calcium current in clonal (GH3) pituitary cells

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