NDLI: Myosin II–actin interaction in MDCK cells: role in cell shape changes in response to Ca2+ variations

Please wait, while we are loading the content...

Identification of the photocrosslinking sites in troponin-I with 4-maleimidobenzophenone labelled mutant troponin-Cs having single cysteines at positions 158 and 21

ATPase kinetics of the Dictyostelium discoideum myosin II motor domain

Optical rotation signals recorded from a single skeletal muscle fibre of a frog

Dethiophalloidin increases Ca2+ responsiveness of skinned cardiac muscle

Different phenotypes among slow/beta myosin heavy chain-containing fibres of rabbit masseter muscle: a novel type of diversity in adult muscle

Activation of skinned muscle fibres from the Norway lobster Nephrops norvegicus L. by manganese ions

Contractile properties and histochemical characteristics of the rat diaphragm after prolonged triamcinolone treatment and nutritional deprivation

Myosin II–actin interaction in MDCK cells: role in cell shape changes in response to Ca2+ variations

Journal of Muscle Research & Cell Motility : Volume 19, Issue 4, May 1998

Journal of Muscle Research & Cell Motility : Volume 19, Issue 3, April 1998

Journal of Muscle Research & Cell Motility : Volume 19, Issue 2, February 1998

Journal of Muscle Research & Cell Motility : Volume 19, Issue 1, January 1998

Journal of Muscle Research & Cell Motility : Volume 18

Myosin II–actin interaction in MDCK cells: role in cell shape changes in response to Ca2+ variations

Content Provider	Springer Nature Link
Author	Castillo, Aida M. Lagunes, Roberto Urbán, Mercedes Frixione, Eugenio Meza, Isaura
Copyright Year	1998
Abstract	Cultured MDCK cell monolayers respond to a low level of extracellular calcium ([Ca2+]e≤5μm) with a loss of transepithelial electrical resistance and transport function, and changes in position of a circumferential ring of actin filaments tethered to the plasma membrane at the zonula adhaerens. Keeping this cytoskeletal structure in place seems necessary to preserve the architecture of the tight junctions and therefore their sealing capacity. All three effects are reversible upon restituting normal [Ca2+]e. Recent work provided evidence of actin–myosin interactions at the filament ring, thus suggesting a contraction process involved in the alteration of the actin cytoskeleton. We now report that active contraction does occur and causes an extensive morphological transformation of MDCK cells. A marked increase in cell height simultaneous with a decrease in width and area of contact to the substratum was seen within 10min of removal of [Ca2+]e; recovery began immediately after replacing calcium, although it took longer for completion. Conventional and confocal epifluorescence studies showed actin colocalized with myosin II at various planes of resting or contracted cells, in particular at the ring level. Electron-micrographs revealed the circumferential actin ring associated with the plasma membrane in a waist-like constriction when Ca2+ was removed from the cultures. Contraction, as well as relaxation, in response to [Ca2+]e variations were inhibited by cytochalasin-D (an actin-filament disrupting drug), by okadaic acid (an inhibitor of myosin light-chain dephosphorylation), and by 2,3-butanedione monoxime (a blocker of myosin II ATPase activity). Similarly, no response was observed in cells previously depleted of metabolic energy by 2,4-dinitrophenol and 2-deoxy-D-glucose preincubation. The actin–myosin mediated reversible structural transformation of MDCK cells in response to [Ca2+]e poses new questions for the interpretation of in vitro experiments, as well as for the understanding of epithelial function.
Starting Page	557
Ending Page	574
Page Count	18
File Format	PDF
ISSN	01424319
Journal	Journal of Muscle Research & Cell Motility
Volume Number	19
Issue Number	5
e-ISSN	15732657
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1998-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biomedicine general Proteomics Cell Biology Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Actin cytoskeleton role in the structural response of epithelial (MDCK) cells to low extracellular Ca2+

Conformational changes in actin–myosin isoforms probed by Ni(II)·Gly–Gly–His reactivity

Allosteric communication in Dictyostelium myosin II

Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity

Actin sliding on reconstituted myosin filaments containing only one myosin heavy chain isoform

Myosin phosphatase and myosin phosphorylation in differentiating C2C12 cells

Caldesmon Tethers Myosin V to Actin and Facilitates in vitro Motility

Myogenic cells express multiple myosin isoforms

2,3-Butanedione monoxime (BDM), a potent inhibitor of actin–myosin interaction, induces ion and fluid transport in MDCK monolayers

Myosin II–actin interaction in MDCK cells: role in cell shape changes in response to Ca2+ variations

Similar Documents

Actin cytoskeleton role in the structural response of epithelial (MDCK) cells to low extracellular Ca2+

Conformational changes in actin–myosin isoforms probed by Ni(II)·Gly–Gly–His reactivity

Allosteric communication in Dictyostelium myosin II

Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity

Actin sliding on reconstituted myosin filaments containing only one myosin heavy chain isoform

Myosin phosphatase and myosin phosphorylation in differentiating C2C12 cells

Caldesmon Tethers Myosin V to Actin and Facilitates in vitro Motility

Myogenic cells express multiple myosin isoforms

2,3-Butanedione monoxime (BDM), a potent inhibitor of actin–myosin interaction, induces ion and fluid transport in MDCK monolayers

Myosin II–actin interaction in MDCK cells: role in cell shape changes in response to Ca2+ variations