Chemically skinned mammalian skeletal muscle I. The structure of skinned rabbit psoas

Eastwood, Abraham B.; Wood, Donald S.; Bock, K.L.; Sorenson, Martha M.

doi:10.1016/0040-8166(79)90062-4

Cited by 147 publications

(76 citation statements)

References 17 publications

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“…Tension Measurements-Chemically skinned fibers were prepared from rabbit psoas muscle and stored in the presence of glycerol at Ϫ20°C (44,45). Segments of single fibers were dissected and mounted for isometric tension measurements as described by Metzger et al (46) in chambers of 0.5-1.0 ml equipped with temperature control and rapid stirring.…”

Section: E77amentioning

confidence: 99%

Biological Function and Site II Ca2+-induced Opening of the Regulatory Domain of Skeletal Troponin C Are Impaired by Invariant Site I or II Glu Mutations

Pearlstone¹,

Chandra²,

Sorenson³

et al. 2000

Journal of Biological Chemistry

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Section: E77amentioning

confidence: 99%

Biological Function and Site II Ca2+-induced Opening of the Regulatory Domain of Skeletal Troponin C Are Impaired by Invariant Site I or II Glu Mutations

Pearlstone¹,

Chandra²,

Sorenson³

et al. 2000

Journal of Biological Chemistry

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“…Ca2+ transport was initiated by the addition of 0 2 mM-MgATP and monitored for several minutes; that is, until the ATP-dependent C(a2+ uptake process was completed and slow passive efflux of Ca2' began. Eastwood, Wood, Bock & Sorenson (1979). Small bundles of several hundred psoas fibres were removed from the muscle, tied to Teflon sticks at 110-120% of resting length and skinned' in a solution of the following composition (in mM): 170 potassium gluconate, 2 5 magnesium gluconate.…”

Section: Measurement Of Ca2+ Transport By Sr Vesiclesmentioning

confidence: 99%

Sulphydryl reagents trigger Ca2+ release from the sarcoplasmic reticulum of skinned rabbit psoas fibres.

Salama

Abramson

Pike

1992

The Journal of Physiology

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SUMMARY1. By analogy with studies on sarcoplasmic reticulum (SR) vesicles, Ca2+ release induced by heavy metals and mercaptans (e.g. cysteine) was investigated in rabbit skinned psoas fibres through measurements of isometric tension.2. Heavy metals (at 2-5 /tM) elicited phasic contractions by triggering Ca2+ release from the SR and had the following order of potency: Hg2+ > Cu2+ > Cd2+ > Ag+ > Ni2+. Higher concentrations produced tonic contractions due to maintained high Ca2+ permeability of SR membranes.3. Contractions induced by heavy metals required a functional and Ca2+-loaded SR, were dependent on [Ca2+]free, blocked by Ruthenium Red (RR), inhibited by free Mg2+ and reduced glutathione (GSH) but not by oxidized glutathione (GSSG). Such contractions were not elicited through direct interactions) of heavy metals with the myofilaments.4. In the presence of catalytic concentrations of Hg2+ or Cu2+ (2-5 /UM), additions of cysteine (25-100 /LM) elicited rapid twitches, producing 70 % of maximal force with a time to half-peak of 2 s. Contractions induced by cysteine plus a catalyst required a functional SR network, were dependent on free [Mg2+] and were blocked by RR or GSH but not by GSSG.5. In the presence of Hg2+ (2-5 ,uM), low concentrations of cysteine (10 /uM) elicited tonic contractures, but subsequent or higher additions of cysteine (50-100 uM) caused further SR Ca2+ release and tension, followed by rapid and full relaxation.6. High cysteine (200-250 /tM, without Cu2+ or Hg2+) blocked contractions elicited by Cl-induced depolarization of sealed T-tubules. High cysteine probably acted as a sulphydryl reducing agent which promoted rapid relaxation of the fibres through the closure of Ca2+-release channels and ATP-dependent re-uptake of Ca2+ by the SR. 7. In some batches of skinned fibres (-10%), cysteine (5-50 /tM) alone (without Hg2+ or Cu2+ catalyst) produced rapid twitches. This implied that the catalysts) necessary to promote the sulphydryl oxidation reaction with exogenously added cysteine may be present in intact fibres but is usually lost by the skinning procedure.

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“…: Cooperativity in thin filaments bundle. For a detailed report on the preparation and ultra-structure see EASTWOOD et al (12).…”

Section: Skinned Muscle Preparationmentioning

confidence: 99%

Molecular basis of cooperativity in vertebrate muscle thin filaments

Brandt

Diamond

Glück

et al. 1984

Carlsberg Res. Commun.

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Extraction of as little as one troponin C per regulatory strand on a thin filament reduces the slope of the pCa/tension relation thus the regulatory units along a thin filament of rabbit psoas fibers are linked cooperatively so that a thin filament activates as a unit. This explains why the pCa/tension relation in skinned fibers has a slope much higher than can be expected by binding of Ca 2 § to one regulatory unit (BRANDT et al. 1980;BRANDT et al. 1982). These results also show that troponin C is the only myfibrillar component responsible for calcium sensitivity in psoas muscle.

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Chemically skinned mammalian skeletal muscle I. The structure of skinned rabbit psoas

Cited by 147 publications

References 17 publications

Biological Function and Site II Ca2+-induced Opening of the Regulatory Domain of Skeletal Troponin C Are Impaired by Invariant Site I or II Glu Mutations

Biological Function and Site II Ca2+-induced Opening of the Regulatory Domain of Skeletal Troponin C Are Impaired by Invariant Site I or II Glu Mutations

Sulphydryl reagents trigger Ca2+ release from the sarcoplasmic reticulum of skinned rabbit psoas fibres.

Molecular basis of cooperativity in vertebrate muscle thin filaments

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