Publication: ß1-integrins co-localize with Na, K-ATPase,
epithelial sodium channels (ENaC) and voltage
activated calcium channels (VACC) in mechanoreceptor
complexes of mouse limb-bud chondrocytes
Authors
Shakibaei, M. ; Mobasheri, A.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Interactions between chondrocytes and their
extracellular matrix are partly mediated by ß1-integrin
receptors. Recent studies have shown that ß1-integrins
co-localize with a variety of cytoskeletal complexes,
signaling proteins and growth factor receptors. Since
mechanosensitive ion channels and integrins have been
proposed to participate in skeletal mechanotransduction,
in this study, we investigated the possible co-localization
of ß1-integrins with two ion channels and a P-type
ATPase in mouse limb-bud chondrocytes. The a
subunits of Na, K-ATPase, the epithelial sodium channel
(ENaC) and the voltage activated calcium channel
(VACC) were immunostained in organoid cultures
derived from limb-buds of 12-day-old mice using wellcharacterized
antibodies . Indirect immunofluorescence
revealed abundant expression of ß1-integrins and each of
the selected systems in limb-bud chondrocytes. Twofluorochrome
immunostaining demonstrated that ß1-
integrin, Na, K-ATPase, ENaC and VACC co-localize in
chondrocytes. Co-imunoprecipitation experiments
revealed co-localization and association of integrins with
ENaC, VACC and Na, K-ATPase. Cellular responses and
signaling cascades initiated by the influx of calcium or
sodium through putative mechanosensitive channels may
be regulated more effectively if such channels were
organized around integrins with receptors, kinases and
cytoskeletal complexes clustered about them. The close
proximity of ATPase ion pumps such as Na, K-ATPase
to chondrocyte mechanoreceptor complexes could
facilitate rapid homeostatic responses to the ionic
perturbations brought about by activation of
mechanically gated cation channels and efficiently
regulate the intracellular milieu of chondrocytes.
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