Download Airways Smooth Muscle: Biochemical Control of Contraction by Apolinary Sobieszek (auth.), Dr. David Raeburn, Dr. Mark A. PDF

By Apolinary Sobieszek (auth.), Dr. David Raeburn, Dr. Mark A. Giembycz (eds.)

ISBN-10: 3034876831

ISBN-13: 9783034876834

1. gentle Muscle Myosin: Molecule Conformation, Filament meeting and linked Regulatory Enzymes.- 2. Actin and Thin-Filament-Associated Proteins in delicate Muscle.- three. present ideas on Mechanisms of strength new release in airlines tender Muscle.- four. Phosphoinositidase C, Inositol Polyphosphates and strength new release of airlines tender Muscle.- five. The Intracellular Calcium shop in airlines soft Muscle.- 6. present strategies on Mechanisms of strength upkeep in airlines tender Muscle.- 7. Diglyceride, Protein Kinase C and strength upkeep of airlines delicate Muscle.- eight. resources of Activator Calcium for strength new release and upkeep of airlines gentle Muscle.- nine. G-Proteins in airlines gentle Muscle.- 10. Cyclic AMP and the keep watch over of airlines delicate Muscle Tone.- eleven. Myosin Dephosphorylation as a Mechanism of rest of airlines soft Muscle.- 12. Cyclic GMP and the keep watch over of airlines gentle Muscle Tone.- thirteen. Cyclic Nucleotide Phosphodiesterases in airlines gentle Muscle.- 14. Modulation of Agonist-Stimulated Phosphoinositide Turnover in airlines gentle Muscle through Cyclic Nucleotide-Dependent and autonomous Mechanisms.- 15. airlines delicate Muscle Cells in tradition.

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Additional info for Airways Smooth Muscle: Biochemical Control of Contraction and Relaxation

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Tropomyosin: Tropomyosins are a diverse group of proteins with distinct isoforms found in muscle (skeletal, cardiac and smooth) and various non-muscle cells (reviewed in [104, 105]). They are encoded by multiple genes and expression of isoforms is known to be regulated by transcriptional and alternative splicing mechanisms [106]. At least nine isoforms, expressed in a tissue specific manner, have been identified in human cells [107]. All isoforms fall into two groups based on the apparent molecular masses determined by SDS-polyacrylamide gel electrophoresis and amino acid sequence: a high molecular mass (3646 kDa) and low molecular mass (30-36 kDa) species comprising 286 and 248 amino acid residues, respectively [108-113].

Thus, although ATP hydrolysis is not a sine qua non for polymerization to occur [51], it is exploited to drive treadmilling of subunits through the filament under steady-state conditions [52]. The elongation step of actin filaments is accompanied by end-to-end annealing of short filaments. This annealing does not require A TP hydrolysis and, together with the F-actin severing process, may contribute to the dynamics of actin filaments in vivo [53]. Polymerization of actin and the rate of ATP hydrolysis on the filament strongly depend on the nature of the tightly bound metal ion.

J Biochem 1982; 91: 1699-705. 67. Ikebe M, Hinkins S, Hartshorne OJ. Correlation of enzymatic properties and conformation of smooth muscle myosin. Biochemistry 1983; 22: 4580-7. 68. Ikebe M, Kortez J, Hartshorne OJ. Effects of phosphorylation of light chain residues threonine 18 and serine 19 on the properties and conformation of smooth muscle myosin. J Bioi Chern 1988; 263: 6432-7. 69. Cross RA. Smooth muscle contraction. What is \OS myosin for? J Muscle Res Cell Motil 1988; 9: \08-\0. 70. Sobieszek A.

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