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	Titin - Wikipedia, the free encyclopedia
		Titin, also known as connectin, (UniProt name: Q10466_HUMAN; accession number: Q10466) is a protein that is important in the contraction of striated muscle tissues.
		Titin connects the Z line to the M line in the sarcomere.
		Titin is the largest known protein, consisting of 26,926 amino acids.
	en.wikipedia.org /wiki/Titin (231 words)

	Biophysical Journal: Titin-actin interaction in mouse myocardium: Passive tension modulation and its regulation by ...
		Titin is a giant protein that spans the length of the halfsarcomere to form a third filament system (in addition to the thin and thick filaments) in vertebrate striated muscle (for recent reviews see Wang 1996; Labeit et al., 1997; Gregorio et al., 1999; Trinick and Tskhovrebova 1999).
		In the I-band, titin filaments exhibit elastic behavior upon sarcomere stretch, resulting in a force that is a primary contributor to the passive tension of cardiac muscle (Granzier and Irving 1995; Wu et al., 2000).
		This suggestion is supported by titin's close proximity to the thin filament in the I-band, and by previous reports of binding between titin and actin, both in vitro and in situ (Kimura et al., 1984; Funatsu et al., 1993; Jin 1995; Kellermayer and Granzier 1996a,b; Linke et al., 1997; Trombitas and Granzier 1997).
	www.findarticles.com /p/articles/mi_qa3938/is_200110/ai_n8960096 (1330 words)

	The NH2 Terminus of Titin Spans the Z-Disc: Its Interaction with a Novel 19-kD Ligand (T-cap) Is Required for ...
		Titin is a giant elastic protein in vertebrate striated muscles with an unprecedented molecular mass of 3-4 megadaltons.
		Titin residues 200-430 are predicted to extend to the center of the Z-line.
		Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly.
	www.jcb.org /cgi/content/full/143/4/1013 (8060 words)

	Not Authorized!
		The authors suggest titin functions in a similar way in condensing chromosomes and in muscles in the actual mechanism-as a molecular ruler so as not to allow chromosome breakage during mitosis by providing elasticity.
		In addition, after deletingt he titin gen, the expression vectors mentioned above, could be selected for mutated forms of the gene using resistence to ampicillan and disruption of the lac Z gene.
		Since titin is such a big protein certain areas of the protein could be narrowed down to exact roles in chromosomal condensation.
	www.bio.davidson.edu /Courses/Molbio/MolStudents/spring99/sarah/only/paper.html (2624 words)

	Global configuration of single titin molecules observed through chain-associated rhodamine dimers -- Grama et al. 98 ...
		Titins are 3.0-3.7 MDa filamentous proteins extending between the Z- and M-lines of the sarcomere (1-4).
		titin, induced by acidic denaturation, is not reflected in a significant
		titin chain is at least 10× shorter than that of the native chain.
	www.pnas.org /cgi/content/full/98/25/14362 (4043 words)

	Titin-based contribution to shortening velocity of rabbit skeletal myofibrils -- Minajeva et al. 540 (1): 177 -- The ... (Site not responding. Last check: 2007-10-20)
		Although the involvement of titin in determining the viscoelasticity of muscle fibres has been studied thoroughly in recent years, no attempt has been made, to our knowledge, to take a fresh look at the function of titin as a contributor to shortening velocity.
		For comparison, we investigated whether the integrity of titin might be affected by incubation of myofibrils at a temperature of 30 °C in the absence of trypsin, but in the presence of the protease inhibitor leupeptin (the two right lanes in Fig.
		Although the spring-like behaviour of titin implies that the protein is somehow involved in determining the shortening characteristics of stretched muscle, we know of no attempt aimed at quantifying the titin-based contribution to shortening velocity.
	jp.physoc.org /cgi/content/full/540/1/177 (7613 words)

	Molecular biomechanics of the giant protein titin (Site not responding. Last check: 2007-10-20)
		Titin is a giant filamentous polypeptide of multi-domain construction spanning between the Z- and M-lines of the sarcomere.
		To explore titin’s mechanical properties we (1) stretched single molecules by using force-measuring laser tweezers, and (2) studied titin isoforms by using immunoelectron microscopy (IEM) and cellular biomechanics.
		Titin was found to behave as an entropic spring whose behavior can be described with the wormlike chain (WLC) model (Kellermayer et al., Science, 276, 1112).
	www.dac.neu.edu /biology/r.marsh/WebSEB2000/Granzier.Abstract.html (281 words)

	Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of ...
		Titin (Wang et al., 1979; described as connectin by Maruyama et al., 1977) is believed to function as the organizer of the sarcomere by providing specific, spatially defined binding sites for other sarcomeric proteins over the entire distance from Z-disk to M-band (see reviews by Trinick, 1994, 1996; Maruyama, 1997).
		In a systematic quest for ligands of titin in the region that we mapped to the central Z-disk at the ultrastructural level, we used several cDNA baits (summarized in Figure 1A) from that region to screen a skeletal muscle cDNA library in the two-hybrid system.
		The titin Z-repeat fragment zr2−zr3 was assayed in a co-precipitation assay ('pull-down') for binding to the
	www.nature.com /emboj/journal/v17/n6/full/7590876a.html (8619 words)

	The Rude Mechanicals [PSC] (Site not responding. Last check: 2007-10-20)
		When muscle is stretched, titin extends — holding the sarcomere together and providing passive force, like a stretched rubber band, that pulls it back to its unstretched state.
		AFM experiments with titin show that, compared to proteins that don't have a mechanical role, it requires considerable stretching force to unfold the molecule.
		As titin stretches, moreover, the pulling force rises and falls in a series of peaks, like a sawtooth pattern — as if you're pulling on a knotted rope and the knots let go one at a time.
	www.psc.edu /science/schulten.html (1531 words)

	Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently -- Trombitás et al. 281 ...
		Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently -- Trombitás et al.
		Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently
		The force of titin is derived from the I-band region of the molecule
	ajpheart.physiology.org /cgi/content/full/281/4/H1793 (3631 words)

	Titin Determines the Frank-Starling Relation in Early Diastole -- Helmes et al. 121 (2): 97 -- The Journal of General ... (Site not responding. Last check: 2007-10-20)
		proteolytic degradation of titin with the trypsin protocol as
		Of the eight proteins, six were identified as titin fragments (shown in bold), while the remaining two were not identifiable.
		The titin- myosin composite filament is a dual-stage molecular spring.
	www.jgp.org /cgi/content/full/121/2/97 (6508 words)

	A targeted deletion of the C-terminal end of titin, including the titin kinase domain, impairs myofibrillogenesis -- ...
		Two bands for titin kinase can be seen in both the wild-type samples, however, only one band can be seen in both c20 samples when probed with the anti-kinase antibody.
		downstream of the titin kinase, interferes with myofibrillogenesis.
		The NH terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity.
	jcs.biologists.org /cgi/content/full/116/23/4811 (6314 words)

	Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may ...
		Triple-labeling studies in GFP–MURF-1–transfected cells (h), using Texas red–conjugated phalloidin (j) and antibodies to titin A168–170 (i), determined that thin filament integrity is not affected upon disruption of COOH-terminal titin in identical myofibrils.
		Costaining of titin A168-170–transfected myocytes with antibodies against thick filament components, including myomesin (g and h), reveals that the integrity of the thick filaments is perturbed compared with myocytes transfected with titin M8-M9-M10-GFP (i and j) or titin kinase–GFP (k and l).
		I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure.
	www.jcb.org /cgi/content/full/157/1/125 (7420 words)

	Biophysical Journal: Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils (Site not responding. Last check: 2007-10-20)
		These findings suggest that in the sarcomere, titin's Ig-domain regions may act as entropic springs capable of adjusting their contour length in response to a stretch.
		A single titin molecule spans the length of a half-sarcomere, connecting the Z-line to the thick filaments (First et al., 1988), but only the titin section located within the I-band region is functionally extensible.
		A model emerges in which titin's poly-Ig regions can be viewed as dynamic WLC elements capable of responding particularly to higher stretch forces with adjustment of their contour length.
	www.findarticles.com /p/articles/mi_qa3938/is_200103/ai_n8944020 (1354 words)

	Titin (Site not responding. Last check: 2007-10-20)
		Strands of titin, a large protein molecule, extend from each sarcomere's Z discs to its M-lines, and anchor the myosin molecules that participate in the production of active force.
		Titin, therefore, maintains the proximity of actin and myosin for active force production, and also contributes to the muscle's passive-elastic properties.
		The schematic diagram of titin to the right is from Scott (2000)
	moon.ouhsc.edu /dthompso/namics/titin.htm (108 words)

	Regulation of the actin-myosin interaction by titin -- Niederländer et al. 271 (22): 4572 -- FEBS Journal (Site not responding. Last check: 2007-10-20)
		Titin is known to interact with actin thin filaments within
		Kellermayer, M.S. and Granzier, H.L. (1996) Calcium-dependent inhibition of in vitro thin-filament motility by native titin.
		Astier, C., Raynaud, F., Lebart, M.C., Roustan, C. and Benyamin, Y. (1998) Binding of a native titin fragment to actin is regulated by PiP2.
	content.febsjournal.org /cgi/content/full/271/22/4572 (6558 words)

	Titin Isoform Switch in Ischemic Human Heart Disease -- Neagoe et al. 106 (11): 1333 -- Circulation
		N2BA-to-N2B titin isoform ratio measured on 2.8% gels changed little with protein load (top) and was similar to that measured on 2% to 10% polyacrylamide gradient gels.
		N2BA titin, and N2B and BD6 to all cardiac titin isoforms.
		C, Titin isoform composition in 4 HH groups studied (N2B+N2BA=100%), expressed as mean of means (see Table).
	circ.ahajournals.org /cgi/content/full/106/11/1333 (4260 words)

	Titin antibody [T11] (ab7034) datasheet
		The antibody localizes titin (connectin) in skeletal and heart muscle of a wide variety of species from cold-blooded vertebrates to human.
		If Titin antibody [T11] (ab7034) does not perform as described on this datasheet, notify us within 90 days of delivery using this form, so that we can help you or offer you a replacement or a refund.
		Monoclonal antibodies to titin in conjunction with antibodies to desmin separate rhabdomyosarcomas from other tumor types.
	www.abcam.com /?datasheet=7034 (544 words)

	Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal ... (Site not responding. Last check: 2007-10-20)
		of calpain 1 is substantiated by binding assays with two titin
		Z8–I5 region and the N1-line region of titin, and an 800
		These two titin fragments are shown to tightly bind
	content.febsjournal.org /cgi/content/abstract/272/10/2578 (319 words)

	Characterizing titin's I-band Ig domain region as an entropic spring -- Linke et al. 111 (11): 1567 -- Journal of Cell ...
		Characterizing titin's I-band Ig domain region as an entropic spring -- Linke et al.
		this region's contribution to titin elasticity, we measured the elastic
		Secondary calpain3 deficiency in 2q-linked muscular dystrophy: Titin is the candidate gene
	jcs.biologists.org /cgi/content/abstract/111/11/1567 (1140 words)

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