Search PubMed⌕ Search

Biomedical subjects

K Güth

Publications and source records attributed to K Güth.

28 records · Page 2Linked to original sources
PubMed1982

Low Ca2+ impedes cross-bridge detachment in chemically skinned Taenia coli.

Muscle force is generated by cycling cross-bridges between actin and myosin filaments. In smooth muscle, cyclic attachment and detachment of cross-bridges is thought to be induced by a Ca2+- and calmodulin-dependent myosin light chain kinase which phosphorylates myosin. The relaxation that occurs after Ca2+ removal is usually ascribed to dephosphorylation of myosin by a phosphatase as non-phosphorylated myosin is unable to form force-generating criss-bridges. Recently, Dillon et al. claimed, however, that dephosphorylation of attached cross-bridges may impede cross-bridge detachment, thus forming so-called 'latch bridges'. Here we present evidence that after a Ca2+- and calmodulin-induced contraction of chemically skinned guinea pig Taenia coli, the rapid removal of Ca2+ impedes the detachment of the myosin cross-bridges from the actin filament; force can then be maintained without energy consumption. The extremely slowly detaching cross-bridges which maintain the force after Ca2+ removal may indeed correspond to the 'latch bridges' mentioned above.

Actins↗
PubMed1982

Decrease in stiffness during shortening in calcium activated skinned muscle fibers.

Single fibers from frog sartorius or semitendinosus muscle were mechanically skinned and activated in ATP salt solution containing 10 micro M Ca2+ (7 degrees C). After development of an isometric contraction, fibers were released at constant speed (0.03-2.4 s-1). During ramp shortening, stiffness was determined from the slope of the tension-length diagram obtained during superimposed quick stretches. Both force and stiffness decreased, as the ramp shortening proceeded and approached a steady value after about 60 ms. An increase in speed of shortening caused a decrease in fiber tension and stiffness and an increase in the ratio of stiffness to tension, suggesting a decrease in both the number of attached crossbridges and in the average force per crossbridge.

Animals↗
PubMed1980

Polarization of tryptophan fluorescence measurements in muscle. A re-evaluation.

The degree of polarization of the intrinsic tryptophan fluorscence of glycerinated simgle muscle fibres or fibre bundles (rabbit psoas or dorsal longitudinal muscle of Lethocerus maximus) was measured: a) With sufficiently high (15 mM) ATP concentration or when an ATP regenerating system was used no difference in the degree of polarization of a contracting and a relaxed muscle was detected, whereas a distinct difference was detected between the relaxed and the rigor state. In contrast a distinct difference between the relaxed and contracting state was obtained at low ATP concentrations (5 mM). This difference is interpreted to be caused by an ATP-free core (rigor core) in the centre of the fibre. b) No change in the polarization degree was detected after a rapid release of the contracting muscle. c) In rigor state no difference in the degree of polarization of the tryptophan fluorescence was observed in the presence or absence of AMPPNP (concentration 0.5 mM). These findings and the lack of difference between the polarization degree of the contracting and the relaxed muscle is interpreted to indicate that the polarization degree of the tryptophan fluorescence is not sensitive to the orientation of the cross bridges, or that the cross bridges do not rotate.

Adenosine Triphosphate↗
PubMed1980

Cross bridge slippage in skinned frog muscle fibres.

Mechanically skinned single fibres of the semitendinosus muscles of Rana esculenta were investigated at ca. 4 degrees C. The fibres were activated by a Ca2+ jump technique, which allowed the development of a steady isometric tension within several seconds of entering a calcium rich solution at 4 degrees C. Sequences of length changes of different duration and amplitude were applied to the fibre. It could be demonstrated that the fibre behaved as a Hookean spring in the case of small amplitude length changes (up to 0.5% L0, ramp duration 0.5 ms) and that a sequence of length changes induced reversible changes in fibre state. In contrast, large stretches (greater than 1% L0) induced a muscle "give" if the stretch were not immediately preceded by a release. The data was interpreted on the basis of a strain induced detachment of cross bridges in combination with a rapid reattachment of presumably the same cross bridges in a discharged position. The rates of strain induced detachment and reattachment depended on the stretch amplitude. At amplitudes exceeding 2% L0 the rates were estimated to be at least several thousands per second.

Actomyosin↗
PubMed1980

ATPase activity in rapidly activated skinned muscle fibres.

The ATPase activity of single mechanically skinned fibres from semitendinosus muscle of Rana esculenta was measured. The method was based on the fluorimetrically detected consumption of NADH inside the fibre. NADH breakdown is caused by the reaction of an ATP regenerating system coupled to an NADH oxidising system. The time resolution was about 5 s. The initial rise in ATPase activity was delayed when a fibre was activated by Ca, and ATPase activity reached its plateau at the same time as fibre tension. An activated fibre that was isolated from the incubation solution by immersing it into oil showed a temporary decrease in tension without corresponding decrease in the ATPase activity.

Adenosine Triphosphatases↗
PubMed1978

Evidence for cross bridge slippage in a stretched muscle fibre.

Bundles of glycerol-extracted psoas fibres which were contracted by immersion in a saline containing 15 mM MgATP and 12 micron free Ca++ were subjected to up to 3 stretches (rise time 0.8 msec) each of amplitude 1% Li at intervals of 10 msec. The elastic tension responses to these stretches were all of comparable size and the peak tensions reached during the stretches were in each case followed by a rapid tension decline almost to the tension values before the stretches. This indicates that stretch-induced detachment and reattachment of cross bridges to the actin filament occurred within 10 msec (slippage).

Actins↗