ArticleThe Journal of general physiology2001
Substrate and product dependence of force and shortening in fast and slow smooth muscle.
Article in The Journal of general physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Signaling and metabolic properties of fast and slow smooth muscle types from mice.Pflugers Archiv : European journal of physiology · 2018Article
- Isoforms Confer Characteristic Force Generation and Mechanosensation by Myosin II Filaments.Biophysical journal · 2015Article
- Thick filament length and isoform composition determine self-organized contractile units in actomyosin bundles.Biophysical journal · 2013Article
- Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle.American journal of physiology. Cell physiology · 2008Article
- Myosin heavy chain isoform expression regulates shortening velocity in smooth muscle: studies using an SMB KO mouse line.Journal of muscle research and cell motility · 2004Article
- Nonmuscle Myosin motor of smooth muscle.The Journal of general physiology · 2003Article
- The smooth muscle myosin seven amino acid heavy chain insert's kinetic role in the crossbridge cycle for mouse bladder.The Journal of physiology · 2003Article
- The kinetic properties of smooth muscle: how a little extra weight makes myosin faster.Journal of muscle research and cell motility · 2003Review
- Smooth, slow and smart muscle motors.Journal of muscle research and cell motility · 2003Review
- Decreased shortening velocity and altered myosin isoforms in guinea-pig hypertrophic intestinal smooth muscle.The Journal of physiology · 2002Article
- Effects of thyroxine on myosin isoform expression and mechanical properties in guinea-pig smooth muscle.The Journal of physiology · 2002Article
- Mechanical properties of (urinary bladder) smooth muscle.Journal of muscle research and cell motility · 2002Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To explore the molecular mechanisms responsible for the variation in smooth muscle contractile kinetics, the influence of MgATP, MgADP, and inorganic phosphate (P(i)) on force and shortening velocity in thiophosphorylated "fast" (taenia coli: maximal shortening velocity Vmax = 0.11 ML/s) and "slow" (aorta: Vmax = 0.015 ML/s) smooth muscle from the guinea pig were compared. P(i) inhibited active force with minor effects on the V(max). In the taenia coli, 20 mM P(i) inhibited force by 25%. In the aorta, the effect was markedly less (< 10%), suggesting differences between fast and slow smooth muscles in the binding of P(i) or in the relative population of P(i) binding states during cycling. Lowering of MgATP reduced force and V(max). The aorta was less sensitive to reduction in MgATP (Km for Vmax: 80 microM) than the taenia coli (Km for Vmax: 350 microM). Thus, velocity is controlled by steps preceding the ATP binding and cross-bridge dissociation, and a weaker binding of ATP is not responsible for the lower V(max) in the slow muscle. MgADP inhibited force and V(max). Saturating concentrations of ADP did not completely inhibit maximal shortening velocity. The effect of ADP on Vmax was observed at lower concentrations in the aorta compared with the taenia coli, suggesting that the ADP binding to phosphorylated and cycling cross-bridges is stronger in slow compared with fast smooth muscle.
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