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T-tubule - Wikipedia, the free encyclopedia
A T-tubule (or transverse tubule ) is a deep invagination of the sarcolemma, which is the plasma membrane, only found in skeletal and cardiac muscle cells. These invaginations allow depolarization...
en.wikipedia.org/wiki/T-tubule |
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We have developed a procedure to isolate, from skeletal muscle, enriched terminal cisternae of sarcoplasmic reticulum (SR), ... Kim, E., Tam, M., Siems, W. F., Kang, C. (2005). Effects of Drugs with Muscle-Related Side Effects and Affinity for Calsequestrin on the Calcium Regulatory Function of Sarcoplasmic Reticulum Microsomes.
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Recently, we have described the isolation of purified fractions referable to terminal and longitudinal cisternae of sarcoplasmic reticulum. Junctional terminal cisternae are distinct in that they have a low net energized Ca2+ loading, which can be enhanced 5-fold or more by addition of ruthenium red.
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First described for their role in liver function, the hepatic nuclear factor ... 5B), identified as Golgi cisternae in higher magnification images (data not shown). ... Thus, our data suggest that maintaining Hnf6 expression in postnatal endocrine cells prevents terminal differentiation of insulin-producing cells into mature,
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Sarcomeres compose myofibrils that are surrounded by the sarcoplasmic reticulum (SR). Near the A-I junctions terminal cisternae and T tubules form triads, which regulate the Ca2+release and transport. (Adapted from Rogers 1983) ... Myofiber function and survival are dependent on this link, which stabilizes the sarcolemma...
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The terminal cisternae are filled with electron-opaque contents which serve as a Ca2+ reservoir. The longitudinal tubules consist mainly of the calcium pump membrane. In this study, we describe a new longitudinal tubule fraction (F2) and ... The results indicate that the isoforms have a somewhat specialized function.
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Calcium is sequestered primarily in the terminal cisternae near the transverse (t) tubules. The cisternae of the SR contain a protein called calsequestrin which acts as a binding site for calcium.
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