ArticleThe Biochemical journal1991
Functional interrelationship between calponin and caldesmon.
Article in The Biochemical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 94 citations in OpenAlex.
- Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026Review
- Mechanoregulation and function of calponin and transgelin.Biophysics reviews · 2024Review
- Myofibroblastic sarcoma in breast: a case report and literature review.Frontiers in oncology · 2024Article
- Muscle Contraction.Cold Spring Harbor perspectives in biology · 2018Review
- Structure and dynamics of the actin-based smooth muscle contractile and cytoskeletal apparatus.Journal of muscle research and cell motility · 2012Review
- Phosphorylation of h1 calponin by PKC epsilon may contribute to facilitate the contraction of uterine myometrium in mice during pregnancy and labor.Reproductive biology and endocrinology : RB&E · 2012Article
- The effect of L-arginine on bladder dysfunction following ovariectomy in a rabbit model.International urogynecology journal · 2011Article
- Article
- Calponin is required for agonist-induced signal transduction--evidence from an antisense approach in ferret smooth muscle.The Journal of physiology · 2001Article
- Myosin light chain kinase binding to a unique site on F-actin revealed by three-dimensional image reconstruction.The Journal of cell biology · 2001Article
- A role for serine-175 in modulating the molecular conformation of calponin.The Biochemical journal · 2000Article
- Correlation between calponin and myosin subfragment 1 binding to F-actin and ATPase inhibition.The Biochemical journal · 1997Article
- Inhibition by calponin of isometric force in demembranated vascular smooth muscle strips: the critical role of serine-175.The Biochemical journal · 1996Article
- Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle.Journal of muscle research and cell motility · 1996Article
- Calponin induces actin polymerization at low ionic strength and inhibits depolymerization of actin filaments.The Biochemical journal · 1995Article
- Stretch affects phenotype and proliferation of vascular smooth muscle cells.Molecular and cellular biochemistry · 1995Article
- Interaction of calponin with actin and its functional implications.The Biochemical journal · 1995Article
- Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin.Protein science : a publication of the Protein Society · 1994Article
- Effects of exogenously applied calponin on Ca(2+)-regulated force in skinned smooth muscle of the rabbit mesenteric artery.Pflugers Archiv : European journal of physiology · 1994Article
- Calponin phosphorylation in vitro and in intact muscle.The Biochemical journal · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calponin and caldesmon, constituents of smooth-muscle thin filaments, are considered to be potential modulators of smooth-muscle contraction. Both of them interact with actin and inhibit ATPase activity of smooth- and skeletal-muscle actomyosin. Here we show that calponin and caldesmon could bind simultaneously to F-actin when used in subsaturating amounts, whereas each one used in excess caused displacement of the other from the complex with F-actin. Calponin was more effective than caldesmon in this competition: when F-actin was saturated with calponin the binding of caldesmon was eliminated almost completely, whereas even at high molar excess of caldesmon one-third of calponin (relative to the saturation level) always remained bound to actin. The inhibitory effects of low concentrations of calponin and caldesmon on skeletal-muscle actomyosin ATPase were additive, whereas the maximum inhibition of the ATPase attained at high concentration of each of them was practically unaffected by the other one. These data suggest that calponin and caldesmon cannot operate on the same thin filaments. CA(2+)-calmodulin competed with actin for calponin binding, and at high molar excess dissociated the calponin-actin complex and reversed the calponin-induced inhibition of actomyosin ATPase activity.
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