February 1, 1997Journal of Biological ChemistryOpen Access

Ca2+ Binding to Troponin C in Skinned Skeletal Muscle Fibers Assessed with Caged Ca2+ and a Ca2+ Fluorophore

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Population

Small bundles of fibers from rabbit skinned psoas muscles

Comparison

Flash photolysis of caged Ca2+ at short and long… vs Fibers after extracting troponin C

Design

Preclinical

Authors

JPJitandrakumar R. PatelNorthwestern University KMKerry S. McDonaldUniversity of Missouri MWMatthew R. WolffUniversity of Wisconsin–Madison

Discussion

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Implication

Challenges troponin C Ca2+ affinity hypothesis in skeletal muscle; leaves open mechanisms and cardiac translation for further study.

Structured PICO

Population

Small bundles of fibers from rabbit skinned psoas muscles

Intervention

Flash photolysis of caged Ca2+ (dimethoxynitrophenamine or o-nitrophenyl-EGTA) at short (approximately 1.97 microm) and long (approximately 2.51 microm) sarcomere lengths

Comparator

Fibers after extracting troponin C

Outcome

Ca2+ binding to troponin C (measured by difference in [Ca2+]free)surrogate

Length-dependent changes in Ca2+ sensitivity of tension in skeletal muscle are not related to length-dependent changes in Ca2+ binding affinity of troponin C.

Cite This Study

Patel et al. (1997) studied this question.

synapsesocial.com/papers/6a727147febe604dd70a9ae5 https://doi.org/10.1074/jbc.272.9.6018

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Ca2+ Binding to Troponin C in Skinned Skeletal Muscle Fibers Assessed with Caged Ca2+ and a Ca2+ Fluorophore

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Ca2+ Binding to Troponin C in Skinned Skeletal Muscle Fibers Assessed with Caged Ca2+ and a Ca2+ Fluorophore

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider