By K. Maruyama (auth.)
Comparative features of muscle elastic proteins.- The titin cDNA series and partial genomic sequences: insights into molecular genetics, cellphone biology and body structure of the titin filament system.- The physiological function of titin in striated muscle.- keep watch over of sarcomeric meeting: the move of data on titin.- The elastic filament method in myogenesis.- constitution and meeting of the sarcomeric M band.-The C-protein relatives: regulators of contraction and sarcomere formation?- The genetics and molecular biology of the titin/connectin-like proteins of invertebrates.
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Additional resources for Reviews of Physiology, Biochemistry and Pharmacology
This approach demonstrated that the different partial titin cDNAs hybridize to a giant mRNA species (Fig. 4). 1). Finally, the DNA extension methods showed that all partial cDNAs are part of a single, giant, full-length mRNA. Therefore, we demonstrated that indeed titin consists of a single three to four megadalton chain. It will be challenging to understand how the synthesis, assembly, and turnover of this huge protein is controlled in living cells. Fig. 4. Northern blot analysis of muscle RNAs with titin (left) and nebulin (right) probes.
During this process, no significant passive tension is generated (see resting tension curve on inset top right). B to D: At larger amounts of stretch, most of the extension occurs in the PEVK region, and a progressively increasing passive tension response is developed. The amount of extension detected in the PEVK region suggests that this domain completely unfolds (taken from Linke et al. 1996) 50 B. Kolmerer et al. cause for familial limb-girdle muscular dystrophy, type LGMD type 2A (Richard et al.
These studies have shown that the nebulin gene, but not the titin gene, is within the region of the NEM2 locus. Therefore, the nebulin gene is a good candidate gene for the NEM2-form of the nemaline myopathy. Interestingly, the nemaline rod-like inclusion bodies found in the patients' muscles are regular assemblies of Z-disc proteins, but the assemblies are distinct from those found in normal Z-bands (Schultheiss et al. 1992b; Schroeter et al. 1996). Therefore, it will be interesting to see how mutations in alpha-tropomyosin and perhaps in nebulin may disturb the precise arrangement of the structural Z-disc proteins.
Reviews of Physiology, Biochemistry and Pharmacology by K. Maruyama (auth.)