What does this research mean for the field?

Titin molecules are polar structures that span half-sarcomere lengths, lacking repetitive epitopes over large regions, with one end anchored at the Z line and the other extending close to the M line. Novelty: ClaimNovelty.NOVEL_FINDING. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

This research aims to characterize the organization of titin filaments in sarcomeres using monoclonal antibodies.

May 1, 1988The Journal of Cell BiologyOpen Access

The 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.

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Population

Relaxed chicken breast muscle

Design

Preclinical

Authors

DFDieter O. FürstHeart Failure & Transplant MOMary OsbornGoethe University Frankfurt RNRüdiger NaveMax Planck Society

Discussion

Member takes

Implication

Clarifies titin polarity in sarcomeres; extends structural models while leaving cardiac functional implications open.

Key Points

This research aims to characterize the organization of titin filaments in sarcomeres using monoclonal antibodies.
Immunoblotting and fluorescence microscopy to characterize mAbs for titin and nebulin.
Immunoelectron microscopy on relaxed chicken breast muscle to investigate titin epitope patterns.
Identification of ten distinct titin epitopes across various regions in the sarcomere.
Ten distinct titin antibodies produced unique transverse striping patterns in sarcomeres.
A linear epitope map was established with positions starting at the Z line and extending to near the M line.
Antibodies T20 and T21 specifically recognized the insoluble titin TI component at the Z line.

Structured PICO

Population

Relaxed chicken breast muscle

Intervention

Monoclonal antibodies specific for titin or nebulin

Outcome

Epitope mapping of titin and nebulin in the half-sarcomere

This study maps the organization of titin filaments in the half-sarcomere, demonstrating that titin molecules are polar structures spanning from the Z line to near the M line.

Cite This Study

Fürst et al. (1988) studied this question.

synapsesocial.com/papers/6a18aef1673175fe754ac729 https://doi.org/10.1083/jcb.106.5.1563

View Full Paper

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May 1, 1988The Journal of Cell BiologyOpen Access

The 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.

View Full Paper

Ask AI

Bookmark

Population

Relaxed chicken breast muscle

Design

Preclinical

Authors

DFDieter O. FürstHeart Failure & Transplant MOMary OsbornGoethe University Frankfurt RNRüdiger NaveMax Planck Society

Discussion

Member takes

Implication

Clarifies titin polarity in sarcomeres; extends structural models while leaving cardiac functional implications open.

Key Points

This research aims to characterize the organization of titin filaments in sarcomeres using monoclonal antibodies.
Immunoblotting and fluorescence microscopy to characterize mAbs for titin and nebulin.
Immunoelectron microscopy on relaxed chicken breast muscle to investigate titin epitope patterns.
Identification of ten distinct titin epitopes across various regions in the sarcomere.
Ten distinct titin antibodies produced unique transverse striping patterns in sarcomeres.
A linear epitope map was established with positions starting at the Z line and extending to near the M line.
Antibodies T20 and T21 specifically recognized the insoluble titin TI component at the Z line.

Structured PICO

Population

Relaxed chicken breast muscle

Intervention

Monoclonal antibodies specific for titin or nebulin

Outcome

Epitope mapping of titin and nebulin in the half-sarcomere

This study maps the organization of titin filaments in the half-sarcomere, demonstrating that titin molecules are polar structures spanning from the Z line to near the M line.

Cite This Study

Fürst et al. (1988) studied this question.

synapsesocial.com/papers/6a18aef1673175fe754ac729 https://doi.org/10.1083/jcb.106.5.1563

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

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