What is the clinical evidence from this study?

Study design: Other. Intervention: Titin (T2) purification and electron microscopy.

What question did this study set out to answer?

To isolate native titin-2 and characterize its physical dimensions, flexibility, and assembly into the sarcomeric lattice.

June 1, 1984Proceedings of the National Academy of SciencesOpen Access

Titin is an extraordinarily long, flexible, and slender myofibrillar protein.

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Key result

Titin (T2) chains self-assembled into extremely long (0.1 to over 1.0 µm), flexible, and extensible slender strands (4-5 nm in diameter) with axial periodicity.

Population

Rabbit skeletal muscle (50 g fresh rabbit back muscle)

Design

Preclinical

Authors

KWK WangThe University of Texas at Austin RRR Ramirez-MitchellThe University of Texas at Austin DPD Palter

Discussion

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Implication

Native titin-2 purification enables sarcomere studies; leaves open cardiac mechanics applications.

Key Points

To isolate native titin-2 and characterize its physical dimensions, flexibility, and assembly into the sarcomeric lattice.
Extracted native titin-2 (T2) protein doublet from striated muscle tissue using Guba-Straub solution followed by chromatography purification.
Visualized native T2 structural morphology using low-angle rotary shadowing and negative-staining electron microscopy.
Purified T2 chains self-assembled into slender strands measuring 4 to 5 nm in diameter and ranging from 0.1 µm to over 1.0 µm in length with axial periodicity.
T2 strands associated into flexible, extensible filamentous bundles and interconnected meshwork structures capable of serving as a template for thick and thin filaments.

Structured PICO

Population

Rabbit skeletal muscle (50 g fresh rabbit back muscle)

Intervention

Purification of native titin-2 (T2) by extraction with Guba-Straub solution and chromatography, followed by electron microscopy

Outcome

Molecular morphology, width, length, axial periodicity, and association of native titin strands

Titin (T2) forms extremely long, flexible, and extensible strands, supporting its proposed role as a major component of an elastic cytoskeletal lattice in the sarcomere.

Limitations

Intact titin (T1) is difficult to extract from myofibrils with benign solvents.
Contour length of highly convoluted titin molecules was difficult to measure with precision.
Titin strands are extremely prone to aggregation, especially at air/water interfaces.

Cite This Study

Wang et al. (1984) studied this question. Titin (T2) purification and electron microscopy was evaluated. Titin (T2) chains self-assembled into extremely long (0.1 to over 1.0 µm), flexible, and extensible slender strands (4-5 nm in diameter) with axial periodicity.

synapsesocial.com/papers/6a6bc06256128ae23fcb4c9c https://doi.org/10.1073/pnas.81.12.3685

View Full Paper

Ask AI

Bookmark

Titin is an extraordinarily long, flexible, and slender myofibrillar protein.

Discussion

Member takes

Implication

Key Points

Structured PICO

Limitations

Cite This Study

Titin is an extraordinarily long, flexible, and slender myofibrillar protein.

Discussion

Member takes

Implication

Key Points

Structured PICO

Limitations

Cite This Study

Also Consider

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