{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kim HR"],"funding":["NHLBI NIH HHS"],"pagination":["888-97"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3135848"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["44(6)"],"pubmed_abstract":["Actin cytoskeletal remodeling is an important mechanism of airway smooth muscle (ASM) contraction. We tested the hypothesis that mechanical strain modulates the cholinergic receptor-mediated cytoskeletal recruitment of actin-binding and integrin-binding proteins in intact airway smooth muscle, thereby regulating the mechanical energetics of airway smooth muscle. We found that the carbachol-stimulated cytoskeletal recruitment of actin-related protein-3 (Arp3), metavinculin, and talin were up-regulated at short muscle lengths and down-regulated at long muscle lengths, suggesting that the actin cytoskeleton--integrin complex becomes enriched in cross-linked and branched actin filaments in shortened ASM. The mechanical energy output/input ratio during sinusoidal length oscillation was dependent on muscle length, oscillatory amplitude, and cholinergic activation. The enhancing effect of cholinergic stimulation on mechanical energy output/input ratio at short and long muscle lengths may be explained by the length-dependent modulation of cytoskeletal recruitment and crossbridge cycling, respectively. We postulate that ASM functions as a hybrid biomaterial, capable of switching between operating as a cytoskeleton-based mechanical energy store at short muscle lengths to operating as an actomyosin-powered mechanical energy generator at long muscle lengths. This postulate predicts that targeting the signaling molecules involved in cytoskeletal recruitment may provide a novel approach to dilating collapsed airways in obstructive airway disease."],"journal":["American journal of respiratory cell and molecular biology"],"pubmed_title":["Length-dependent modulation of cytoskeletal remodeling and mechanical energetics in airway smooth muscle."],"pmcid":["PMC3135848"],"funding_grant_id":["R56 HL052714","R56 HL052714-09A2"],"pubmed_authors":["Liu K","Kim HR","Hai CM","Roberts TJ"],"additional_accession":[]},"is_claimable":false,"name":"Length-dependent modulation of cytoskeletal remodeling and mechanical energetics in airway smooth muscle.","description":"Actin cytoskeletal remodeling is an important mechanism of airway smooth muscle (ASM) contraction. We tested the hypothesis that mechanical strain modulates the cholinergic receptor-mediated cytoskeletal recruitment of actin-binding and integrin-binding proteins in intact airway smooth muscle, thereby regulating the mechanical energetics of airway smooth muscle. We found that the carbachol-stimulated cytoskeletal recruitment of actin-related protein-3 (Arp3), metavinculin, and talin were up-regulated at short muscle lengths and down-regulated at long muscle lengths, suggesting that the actin cytoskeleton--integrin complex becomes enriched in cross-linked and branched actin filaments in shortened ASM. The mechanical energy output/input ratio during sinusoidal length oscillation was dependent on muscle length, oscillatory amplitude, and cholinergic activation. The enhancing effect of cholinergic stimulation on mechanical energy output/input ratio at short and long muscle lengths may be explained by the length-dependent modulation of cytoskeletal recruitment and crossbridge cycling, respectively. We postulate that ASM functions as a hybrid biomaterial, capable of switching between operating as a cytoskeleton-based mechanical energy store at short muscle lengths to operating as an actomyosin-powered mechanical energy generator at long muscle lengths. This postulate predicts that targeting the signaling molecules involved in cytoskeletal recruitment may provide a novel approach to dilating collapsed airways in obstructive airway disease.","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Jun","modification":"2025-04-04T23:39:50.524Z","creation":"2019-03-27T03:07:03Z"},"accession":"S-EPMC3135848","cross_references":{"pubmed":["20705939"],"doi":["10.1165/rcmb.2010-0144OC","10.1165/rcmb.2010-0144oc"]}}