Abstract
Skinned tail and leg muscle fibers of the limulus were used to study the mechanism of Ca2+ regulation of contraction. Although a Ca2+-sensitive 31,000 dalton protein phosphorylation could be observed in the presence of [γ-32P] ATP no such phosphorylation occurred in the presence of [γ-32P] ITP. Ca2+-activated tension occurred equally as well in ATP and ITP. For this reason we eliminated the possibility that a Ca2+-sensitive myosin light chain kinase/phosphatase system is the mechanism responsible for the Ca2+-activated tension. Other agents known to affect a myosin light chain kinase/phosphatase system showed negative results (ATPγS, trifluoperazine, catalytic subunit of the cyclic adenosine 3′,5′-monophosphate dependent protein kinase and calmodulin). Troponin I reversibly inhibits Ca2+-activated tension. These results are consistent with thin filament regulation being responsible for Ca2+-activated tension in skinned fibers.
| Original language | English |
|---|---|
| Pages (from-to) | 121-124 |
| Number of pages | 4 |
| Journal | Pflügers Archiv European Journal of Physiology |
| Volume | 392 |
| Issue number | 2 |
| DOIs | |
| State | Published - Dec 1 1981 |
| Externally published | Yes |
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Keywords
- Ca
- ITP
- Limulus
- Myosin light chain
- Phosphorylation
- Skinned fibers
ASJC Scopus subject areas
- Physiology
Cite this
Regulation of Ca2+-activated tension in limulus striated muscle. / Kerrick, W. Glenn; Bolles, L. L.
In: Pflügers Archiv European Journal of Physiology, Vol. 392, No. 2, 01.12.1981, p. 121-124.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Regulation of Ca2+-activated tension in limulus striated muscle
AU - Kerrick, W. Glenn
AU - Bolles, L. L.
PY - 1981/12/1
Y1 - 1981/12/1
N2 - Skinned tail and leg muscle fibers of the limulus were used to study the mechanism of Ca2+ regulation of contraction. Although a Ca2+-sensitive 31,000 dalton protein phosphorylation could be observed in the presence of [γ-32P] ATP no such phosphorylation occurred in the presence of [γ-32P] ITP. Ca2+-activated tension occurred equally as well in ATP and ITP. For this reason we eliminated the possibility that a Ca2+-sensitive myosin light chain kinase/phosphatase system is the mechanism responsible for the Ca2+-activated tension. Other agents known to affect a myosin light chain kinase/phosphatase system showed negative results (ATPγS, trifluoperazine, catalytic subunit of the cyclic adenosine 3′,5′-monophosphate dependent protein kinase and calmodulin). Troponin I reversibly inhibits Ca2+-activated tension. These results are consistent with thin filament regulation being responsible for Ca2+-activated tension in skinned fibers.
AB - Skinned tail and leg muscle fibers of the limulus were used to study the mechanism of Ca2+ regulation of contraction. Although a Ca2+-sensitive 31,000 dalton protein phosphorylation could be observed in the presence of [γ-32P] ATP no such phosphorylation occurred in the presence of [γ-32P] ITP. Ca2+-activated tension occurred equally as well in ATP and ITP. For this reason we eliminated the possibility that a Ca2+-sensitive myosin light chain kinase/phosphatase system is the mechanism responsible for the Ca2+-activated tension. Other agents known to affect a myosin light chain kinase/phosphatase system showed negative results (ATPγS, trifluoperazine, catalytic subunit of the cyclic adenosine 3′,5′-monophosphate dependent protein kinase and calmodulin). Troponin I reversibly inhibits Ca2+-activated tension. These results are consistent with thin filament regulation being responsible for Ca2+-activated tension in skinned fibers.
KW - Ca
KW - ITP
KW - Limulus
KW - Myosin light chain
KW - Phosphorylation
KW - Skinned fibers
UR - http://www.scopus.com/inward/record.url?scp=0019810123&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019810123&partnerID=8YFLogxK
U2 - 10.1007/BF00581259
DO - 10.1007/BF00581259
M3 - Article
C2 - 7322841
AN - SCOPUS:0019810123
VL - 392
SP - 121
EP - 124
JO - Pflugers Archiv European Journal of Physiology
JF - Pflugers Archiv European Journal of Physiology
SN - 0031-6768
IS - 2
ER -