By Apolinary Sobieszek (auth.), Dr. David Raeburn, Dr. Mark A. Giembycz (eds.)
1. soft Muscle Myosin: Molecule Conformation, Filament meeting and linked Regulatory Enzymes.- 2. Actin and Thin-Filament-Associated Proteins in tender Muscle.- three. present recommendations on Mechanisms of strength iteration in airlines soft Muscle.- four. Phosphoinositidase C, Inositol Polyphosphates and strength iteration of airlines tender Muscle.- five. The Intracellular Calcium shop in airlines delicate Muscle.- 6. present recommendations on Mechanisms of strength upkeep in airlines gentle Muscle.- 7. Diglyceride, Protein Kinase C and strength upkeep of airlines soft Muscle.- eight. assets of Activator Calcium for strength iteration and upkeep of airlines soft Muscle.- nine. G-Proteins in airlines soft Muscle.- 10. Cyclic AMP and the keep an eye on of airlines soft Muscle Tone.- eleven. Myosin Dephosphorylation as a Mechanism of leisure of airlines delicate Muscle.- 12. Cyclic GMP and the regulate of airlines tender Muscle Tone.- thirteen. Cyclic Nucleotide Phosphodiesterases in airlines tender Muscle.- 14. Modulation of Agonist-Stimulated Phosphoinositide Turnover in airlines gentle Muscle via Cyclic Nucleotide-Dependent and self reliant Mechanisms.- 15. airlines tender Muscle Cells in tradition.
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Extra resources for Airways Smooth Muscle: Biochemical Control of Contraction and Relaxation
The only functional form of actin is F-actin. 3 kDa [5, 6]. It contains I mole of tightly bound divalent cation, Ca2+ or Mg2+ (in vivo probably Mg2 +), and I mole of ATP (or ADP), both of which act to stabilize its structure . G-actin also binds mono- or divalent R. D 4 browska 32 cations at lower affinity binding sites; this binding is important for activation of monomers during the initial step of actin polymerization [8, 9]. 2. Isoforms The primary structure of actin is highly conserved. For example, yeast and rabbit skeletal muscle actin are 88% homologous in amino acid sequence .
J Mol BioI 1971; 60: 249-61. 98. Applegate D, Pardee JD. Actin-facilitated assembly of smooth muscle myosin induces formation of actomyosin fibrils. J Cell BioI 1992; 117: 1223-30. 99. Kamm KE, Stull JT. Regulation of smooth muscle contractile elements by second messengers. Ann Rev Physiol 1989; 51: 299-313. 100. Kamm KE, Hsu L-C, Kubota Y, Stull JT. Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists. J BioI Chern 1989; 264: 21223-9. 101. Itoh T, Ikebe M, Kargacin GJ, Hartshorne DJ, Kemp BE, Fay FS.
Sobieszek 10. Phosphorylation Kinetics From a kinetics point of view, the two heads of the myosin molecule can be phosphorylated independently (random phosphorylation) or in an ordered fashion. In the latter case there could be either negative or positive co-operativity such that the first head would either inhibit or promote the phosphorylation of the second one. These three mechanisms would result in a different relationship between the extent of myosin phosphorylation and the actin-activated ATPase activity.