title: Effect of adenosine triphosphate analogues on skeletal muscle fibers in rigor.
abstract: It is commonly believed, for both vertebrate striated and insect flight muscle, that when the ATP analogue adenyl-5'-yl imidodiphosphate (AMPPNP) is added to the muscle fiber in rigor, it causes the fiber to lengthen by 0.15%. This has been interpretated (Marston S.B., C.D. Roger, and R.T. Tregear. 1976. J. Mol. Biol. 104:263-267) as suggesting (a) that in rigor the crossbridge is fixed to, i.e., almost never detaches from the actin filament; (b), that the crossbridge remains fixed to the actin filament after AMPPNP addition; and (c) that the ability of AMPPNP to cause apparent lengthening of a muscle fiber is due to its ability to cause a conformational change in the myosin crossbridge that has an axial component of approximately 1.6 nm/half-sarcomere. The present study, done only on chemically-skinned rabbit psoas fibers, confirms that AMPPNP can cause muscle fibers to lengthen by 0.15% but only for a narrow set of experimental conditions. When experimental conditions are varied over a wider range, it becomes apparent that the extent of lengthening of a rigor muscle fiber upon AMPPNP addition depends almost entirely on the strain present in the rigor fiber before AMPPNP addition. Addition of AMPPNP to an unstrained rigor fiber (one supporting zero tension), induces zero length change while addition of AMPPNP to very highly strained rigor fibers induces length changes greater than 0.15%. The data thus do not support the hypotheses that the crossbridges remain fixed to the actin filament after AMPPNP addition and that the size of the apparent length change induced by AMPPNP is related to the size of the axial component of a conformational change. Instead, the data support the idea that the ability of AMPPNP to cause lengthening of a rigor muscle fiber is related to its ability to accelerate the rate at which strained crossbridges detach from actin and reattach in positions in lesser strain. The data do not rule out a conformational change upon AMPPNP binding, they simply make clear that any attempt to measure a force response conceivably due to a conformational change, would be more than obscured by the force changes due to crossbridges detaching and reattaching in positions of lesser strain.
authors.affiliation: Laboratory of Physical Biology, National Institutes of Arthritis and Musculoskeletal and Skin Diseases, Bethesda, Maryland 20892.
authors.forename: M
authors.initials: M
authors.lastname: Schoenberg
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives*; D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology*; D000818:Animals; D011756:Diphosphates / Q000494:pharmacology*; D066298:In Vitro Techniques; D007700:Kinetics; D009119:Muscle Contraction / Q000187:drug effects*; D009132:Muscles / Q000187:drug effects / Q000502:physiology*; D011817:Rabbits
chemical_list: D011756:Diphosphates; D000266:Adenylyl Imidodiphosphate; D000255:Adenosine Triphosphate