What question did this study set out to answer?

To survey the presence, electrophoretic mobility, and isoform diversity of high molecular weight myofibrillar proteins across diverse vertebrate and invertebrate muscle types.

April 1, 1986The Journal of Biochemistry

A Comparative Study of High Molecular Weight Proteins in Various Types of Muscle Across the Animal Kingdom

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Authors

RLR.H. LockerUniversity of Cambridge DWDavid WildFriedrich-Alexander-Universität Erlangen-Nürnberg

Discussion

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Implication

No immediate clinical implications for titin-related cardiomyopathies; leaves open evolutionary context for future vertebrate sarcomere research.

Key Points

To survey the presence, electrophoretic mobility, and isoform diversity of high molecular weight myofibrillar proteins across diverse vertebrate and invertebrate muscle types.
Screened muscle tissues across multiple animal phyla—including vertebrates, worms, molluscs, insects, crustaceans, and echinoderms—alongside human blood platelets using SDS-PAGE.
Assessed the distribution and relative mobility of connectin (titin), nebulin, filamin isoforms, and C-protein isoforms across skeletal, cardiac, and smooth muscle types.
Connectin (titin) showed constant mobility in vertebrate striated muscle but was absent in smooth muscle, whereas invertebrate homologs exhibited variable amounts with greater electrophoretic mobility.
Nebulin was present across vertebrate skeletal muscles and multiple invertebrate taxa but was consistently absent from vertebrate cardiac muscle.
Characterized muscle-specific filamin isoforms across vertebrate muscle classes and resolved four C-protein isoforms in rabbit muscle: white, alpha-red (X-protein), beta-red, and cardiac.

Cite This Study

Locker et al. (1986) studied this question.

synapsesocial.com/papers/6a8bdf4da42d46e0ffcad2bd https://doi.org/10.1093/oxfordjournals.jbchem.a135617

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April 1, 1986The Journal of Biochemistry

A Comparative Study of High Molecular Weight Proteins in Various Types of Muscle Across the Animal Kingdom

View Full Paper

Ask AI

Bookmark

Authors

RLR.H. LockerUniversity of Cambridge DWDavid WildFriedrich-Alexander-Universität Erlangen-Nürnberg

Discussion

Member takes

Implication

No immediate clinical implications for titin-related cardiomyopathies; leaves open evolutionary context for future vertebrate sarcomere research.

Key Points

To survey the presence, electrophoretic mobility, and isoform diversity of high molecular weight myofibrillar proteins across diverse vertebrate and invertebrate muscle types.
Screened muscle tissues across multiple animal phyla—including vertebrates, worms, molluscs, insects, crustaceans, and echinoderms—alongside human blood platelets using SDS-PAGE.
Assessed the distribution and relative mobility of connectin (titin), nebulin, filamin isoforms, and C-protein isoforms across skeletal, cardiac, and smooth muscle types.
Connectin (titin) showed constant mobility in vertebrate striated muscle but was absent in smooth muscle, whereas invertebrate homologs exhibited variable amounts with greater electrophoretic mobility.
Nebulin was present across vertebrate skeletal muscles and multiple invertebrate taxa but was consistently absent from vertebrate cardiac muscle.
Characterized muscle-specific filamin isoforms across vertebrate muscle classes and resolved four C-protein isoforms in rabbit muscle: white, alpha-red (X-protein), beta-red, and cardiac.

Cite This Study

Locker et al. (1986) studied this question.

synapsesocial.com/papers/6a8bdf4da42d46e0ffcad2bd https://doi.org/10.1093/oxfordjournals.jbchem.a135617

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