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Article: Myosin II is present in gastric parietal cells and required for lamellipodial dynamics associated with cell activation

TitleMyosin II is present in gastric parietal cells and required for lamellipodial dynamics associated with cell activation
Authors
Issue Date2003
PublisherAmerican Physiological Society. The Journal's web site is located at http://intl-ajpcell.physiology.org/
Citation
American Journal Of Physiology - Cell Physiology, 2003, v. 285 n. 3 54-3, p. C662-C673 How to Cite?
AbstractNonmuscle myosin II has been shown to participate in organizing the actin cytoskeleton in polarized epithelial cells. Vectorial acid secretion in cultured parietal cells involves translocation of proton pumps from cytoplasmic vesicular membranes to the apical plasma membrane vacuole with coordinated lamellipodial dynamics at the basolateral membrane. Here we identify nonmuscle myosin II in rabbit gastric parietal cells. Western blots with isoform-specific antibodies indicate that myosin IIA is present in both cytosolic and particulate membrane fractions whereas the IIB isoform is associated only with particulate fractions. Immunofluorescent staining demonstrates that myosin IIA is diffusely located throughout the cytoplasm of resting parietal cells. However, after stimulation, myosin IIA is rapidly redistributed to lamellipodial extensions at the cell periphery; virtually all the cytoplasmic myosin IIA joins the newly formed basolateral membrane extensions. 2,3-Butanedione monoximine (BDM), a myosin-ATPase inhibitor, greatly diminishes the lamellipodial dynamics elicited by stimulation and retains the pattern of myosin IIA cytoplasmic staining. However, BDM had no apparent effect on the stimulation associated redistribution of H,K-ATPase from a cytoplasmic membrane compartment to apical membrane vacuoles. The myosin light chain kinase inhibitor 1-(5-iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine (ML-7) also did not alter the stimulation-associated recruitment of H,K-ATPase to apical membrane vacuoles, but unlike BDM it had relatively minor inhibitory effects on lamellipodial dynamics. We conclude that specific disruption of the basolateral actomyosin cytoskeleton has no demonstrable effect on recruitment of H,K-ATPase-rich vesicles into the apical secretory membrane. However, myosin II plays an important role in regulating lamellipodial dynamics and cortical actomyosin associated with parietal cell activation.
Persistent Identifierhttp://hdl.handle.net/10722/136785
ISSN
2015 Impact Factor: 3.395
2015 SCImago Journal Rankings: 1.893
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhou, Ren_HK
dc.contributor.authorWatson, Cen_HK
dc.contributor.authorFu, Cen_HK
dc.contributor.authorYao, Xen_HK
dc.contributor.authorForte, JGen_HK
dc.date.accessioned2011-07-29T02:12:11Z-
dc.date.available2011-07-29T02:12:11Z-
dc.date.issued2003en_HK
dc.identifier.citationAmerican Journal Of Physiology - Cell Physiology, 2003, v. 285 n. 3 54-3, p. C662-C673en_HK
dc.identifier.issn0363-6143en_HK
dc.identifier.urihttp://hdl.handle.net/10722/136785-
dc.description.abstractNonmuscle myosin II has been shown to participate in organizing the actin cytoskeleton in polarized epithelial cells. Vectorial acid secretion in cultured parietal cells involves translocation of proton pumps from cytoplasmic vesicular membranes to the apical plasma membrane vacuole with coordinated lamellipodial dynamics at the basolateral membrane. Here we identify nonmuscle myosin II in rabbit gastric parietal cells. Western blots with isoform-specific antibodies indicate that myosin IIA is present in both cytosolic and particulate membrane fractions whereas the IIB isoform is associated only with particulate fractions. Immunofluorescent staining demonstrates that myosin IIA is diffusely located throughout the cytoplasm of resting parietal cells. However, after stimulation, myosin IIA is rapidly redistributed to lamellipodial extensions at the cell periphery; virtually all the cytoplasmic myosin IIA joins the newly formed basolateral membrane extensions. 2,3-Butanedione monoximine (BDM), a myosin-ATPase inhibitor, greatly diminishes the lamellipodial dynamics elicited by stimulation and retains the pattern of myosin IIA cytoplasmic staining. However, BDM had no apparent effect on the stimulation associated redistribution of H,K-ATPase from a cytoplasmic membrane compartment to apical membrane vacuoles. The myosin light chain kinase inhibitor 1-(5-iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine (ML-7) also did not alter the stimulation-associated recruitment of H,K-ATPase to apical membrane vacuoles, but unlike BDM it had relatively minor inhibitory effects on lamellipodial dynamics. We conclude that specific disruption of the basolateral actomyosin cytoskeleton has no demonstrable effect on recruitment of H,K-ATPase-rich vesicles into the apical secretory membrane. However, myosin II plays an important role in regulating lamellipodial dynamics and cortical actomyosin associated with parietal cell activation.en_HK
dc.languageengen_US
dc.publisherAmerican Physiological Society. The Journal's web site is located at http://intl-ajpcell.physiology.org/en_HK
dc.relation.ispartofAmerican Journal of Physiology - Cell Physiologyen_HK
dc.subject.meshAminopyrine - pharmacokineticsen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshAnti-Inflammatory Agents, Non-Steroidal - pharmacokineticsen_HK
dc.subject.meshCells, Cultureden_HK
dc.subject.meshCholinesterase Reactivators - pharmacologyen_HK
dc.subject.meshCyclic AMP-Dependent Protein Kinases - metabolismen_HK
dc.subject.meshCytoplasm - metabolismen_HK
dc.subject.meshCytoskeleton - physiologyen_HK
dc.subject.meshDiacetyl - analogs & derivatives - pharmacologyen_HK
dc.subject.meshGastric Acid - secretionen_HK
dc.subject.meshNonmuscle Myosin Type IIA - metabolismen_HK
dc.subject.meshNonmuscle Myosin Type IIB - metabolismen_HK
dc.subject.meshParietal Cells, Gastric - cytology - metabolismen_HK
dc.subject.meshPseudopodia - metabolismen_HK
dc.subject.meshRabbitsen_HK
dc.titleMyosin II is present in gastric parietal cells and required for lamellipodial dynamics associated with cell activationen_HK
dc.typeArticleen_HK
dc.identifier.emailFu, C:chuanhai@hku.hken_HK
dc.identifier.authorityFu, C=rp01515en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid12724136-
dc.identifier.scopuseid_2-s2.0-0042889385en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0042889385&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume285en_HK
dc.identifier.issue3 54-3en_HK
dc.identifier.spageC662en_HK
dc.identifier.epageC673en_HK
dc.identifier.isiWOS:000184549600020-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhou, R=8353462900en_HK
dc.identifier.scopusauthoridWatson, C=7402883686en_HK
dc.identifier.scopusauthoridFu, C=8583808400en_HK
dc.identifier.scopusauthoridYao, X=7402530401en_HK
dc.identifier.scopusauthoridForte, JG=26425932500en_HK

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