By Károly Trombitás (auth.), Henk L. Granzier, Gerald H. Pollack (eds.)
Elastic filaments refer quite often to titin, the most important of all identified proteins. Titin was once stumbled on firstly in muscle cells, the place it interconnects the thick filament with the Z-line. Titin varieties a molecular spring that's liable for protecting the structural integrity of contracting muscle, making sure effective muscle contraction. extra lately, it has develop into transparent that titin isn't constrained to muscle cells on my own. for instance, titin is located in chromosomes of neurons and likewise in blood platelets. This subject is speedy turning into a focus for examine in figuring out viscoelastic homes on the molecular, mobile, and tissue degrees. In titin could lie a known foundation for organic viscoelasticity. It has develop into transparent that titin may well carry the major to definite medical anomalies. for instance, it's transparent that titin-based ventricular stiffness is modulated via calcium and that titin is answerable for the altered stiffness in cardiomyopathies. it's also transparent from proof from a bunch of Finnish households that titin mutations could underlie a few muscular dystrophies and that with different mutations chromatids fail to split in the course of mitosis. therefore, it's transparent that this protein may have vital medical implications stemming from its biomechanical function. One element of this box is the bringing jointly of bioengineers with medical researchers and biologists. Genetic and biochemical elements of titin-related proteins are being studied including front-line engineering techniques designed to degree the mechanics of titin both in small aggregates or in unmarried molecules.
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Extra info for Elastic Filaments of the Cell
Elastic properties of titin filaments demonstrated using a freeze-fracture technique. Cell Motil CytoskelI993;24:274-283 Trombitas K, Jin Jp, Granzier H. The mechanically active domain of titin in cardiac muscle. eirc Res 1995;77:856-861. Trombitas K, Greaser M, Labeit S, Jin JP, Kellermayer M, Helmes M, Granzier H. Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments. J Cell BiolI998a;140:853-859. Trombitas K, Greaser M, French G, Granzier H.
Fragments were extracted from an agarose matrix by using the Jetsorb kit (Genomed, Bad Oyenhausen, Germany). 8 x lOx Y-Tango buffer (MBI Fermentas, Vilnius, Lithunia). After incubation for 2 hours at 37°C, restriction enzymes were inactivated by a phenol extraction, excess phenol was removed by an isopropanol precipitation, followed by a 70% ethanol wash. Obtained fragments were then ligated into a pET9D vector (Studier and Moffat, 1986) which was modified to express their insert sequences as N-terminal His6tags fusions.
The following libraries have been amplified and aliquots are being used for titin subclone construction: human cardiac cDNA library in larnbda-ZapII vector backbone (Stratagene #936208), human skeletal cDNA library in gtlO Centner, Fougerousse, Freiburg, Witt, Beckmann, Trombittis, Gregorio, and Labeit 39 (Clontech, Cat. # HL1024) and human skeletal muscle cDNA library in pGADlO (Clontech, Cat. # HL4010AB). This latter library (with cDNA inserts in the plasmid vector) has become our "default template" because the amplification efficiency of the PCR reaction is higher in comparison with cDNA pools inserted into the 50 kb GC-rich lambda phage vector backbone.