These studies have driven microscopists to investigate and observe the expression of ENaC subunits both in vivo and in vitro of human osteoblasts, chondrocytes, and of the anterior cruciate ligament. The expression of ?ENaC within human cartilage is demonstrated in most gynecological microscopy researches. Both the expressions of the ? and ? ENaC subunits found in human chondrocyte-like cells can be seen in most gynecological microscope experiments. By the use of polyclonal antigens put up against ?, ? and ? ENaC subunits, the evidence for the existence of the ? and ? subunits of ENaC in the site of human chondrocytes and also in the human chondrocyte cell line. And also, by the use of a molecular approach, the ? and ? subunits of ENaC in osteoblasts derived from human femoral bone can be identified.
In the latest study utilizing obstetric microscopes, researchers investigated the probable co-localization of ß1-integrins together with ? ENaC subunit in organoid cultures that were derived collected from limb-buds of 12-day-old mice. In that study, indirect immunofluorescence and inverted-microscopes for gynecological examinations were used to find out the interaction of ß1-integrin and ENaC within chondroblasts located in limb bud. Moreover, the co-immunoprecipitation experiments have been a precursor in the discovery that ß1-integrins associate with ?ENaC subunit. These observations have led to the conclusion that chondrocyte responses and signaling cascades is affected by the influx of sodium through the mechanosensitive ENaC channels, and they could be regulated more effectively if the ENaC channels were placed around ß1-integrins with the associated receptors, cytoskeletal complexes and kinases placed around them.
Therefore, ENaC expression is not bounded to the epithelia only. In fact, ENaC expression has been also shown in epidermal keratinocytes that can be found surrounding touch sensitive hair follicles. Almost all the evidence collected leads to the existence of functional epithelial sodium channels that is located in the plasma membranes of mechanosensitive cells and it also leads to the speculation that ENaC or its corresponding homologues can mediate the observation of the fetal cell transfer between the mother host and the fetus as viewed from a gynecological microscope. Another support for this hypothesis comes from the cloning studies done by the use of nuclear-transfer microscopes, where another homologue of C. elegans is assumed to interact with type IV collagen, which further gives evidence that electrochemical signals within the cells may transducer the mechanostimulation of the extracellular matrix. The channel could be opened by the possible interaction of the extracellular domain of the protein encoded by unc-105 and the collagen on the extracellular face and also the mechanical forces applied on the collagen network.



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