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November 1, 1989The Journal of Cell BiologyOpen Access

Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle.

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Population

Skinned rabbit psoas fibers

Comparison

Activation and stretching of sarcomeres vs Relaxed fibers

Design

Preclinical

Authors

RHRobert HorowitsNational Institutes of HealthKMKosçak MaruyamaChiba UniversityRPRichard J. PodolskyNational Institutes of Health

Discussion

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Implication

Titin elasticity remains activation-independent in animal skeletal muscle; extends basic models but leaves cardiac translation open.

Key Points

  • This study aims to understand the behavior of connectin during thick filament movement in skeletal muscle under relaxed and activated conditions.
  • Utilized immunoelectron microscopy to visualize connectin behavior in skinned rabbit psoas fibers.
  • Observed relaxed and activated sarcomere mechanics based on connectin labeling.
  • Analyzed thick filament movement and spacing variations in both active and relaxed states.
  • In relaxed fibers, striations are symmetrically arranged around the M-line, confirming connectin's elastic behavior.
  • Activated fibers show thick filaments translocating within shortened sarcomeres, altering spacings between Z-disc and antibody.
  • Connectin's binding to thick filaments remains unchanged under different conditions of calcium ions and activity.

Structured PICO

P
Population
Skinned rabbit psoas fibers
I
Intervention
Activation and stretching of sarcomeres
C
Comparator
Relaxed fibers
O
Outcome
Behavior and movement of connectin (titin) filaments measured by immunoelectron microscopysurrogate

This basic science study demonstrates that the elastic properties of connectin (titin) in skeletal muscle are not altered by calcium ions or cross-bridge activity during muscle activation.

Cite This Study

Horowits et al. (1989) studied this question.

synapsesocial.com/papers/6a109a98d478ddac0ffd4204https://doi.org/10.1083/jcb.109.5.2169
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1FILAMENT LENGTHS IN STRIATED MUSCLE1963 · 336 citations
  2. 2Control of sarcomere length in skinned muscle fibres of Rana temporaria during mechanical transients.1984 · 152 citations
  3. 3The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments.1987 · 309 citations
  4. 4Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy.1985 · 141 citations
  5. 5The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line.1988 · 626 citations