Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions
Identifieur interne : 000F25 ( Ncbi/Checkpoint ); précédent : 000F24; suivant : 000F26Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions
Auteurs : Kazuo Hosoi [Japon] ; Chenjuan Yao ; Takahiro Hasegawa ; Hiroshi Yoshimura ; Tetsuya Akamatsu [Japon]Source :
- International Journal of Molecular Sciences [ 1422-0067 ] ; 2020.
Abstract
Aquaporin 5 (AQP5) plays an important role in the salivary gland function. The
Url:
DOI: 10.3390/ijms21041182
PubMed: 32053992
PubMed Central: 7072788
Affiliations:
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PMC:7072788Le document en format XML
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<series><title level="j">International Journal of Molecular Sciences</title>
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<front><div type="abstract" xml:lang="en"><p>Aquaporin 5 (AQP5) plays an important role in the salivary gland function. The <italic>mRNA</italic>
and protein for AQP5 are expressed in the acini from embryonic days E13-16 and E17-18, respectively and for entire postnatal days. Ligation-reopening of main excretory duct induces changes in the AQP5 level which would give an insight for mechanism of regeneration/self-duplication of acinar cells. The AQP5 level in the submandibular gland (SMG) decreases by chorda tympani denervation (CTD) via activation autophagosome, suggesting that its level in the SMG under normal condition is maintained by parasympathetic nerve. Isoproterenol (IPR), a β-adrenergic agonist, raised the levels of membrane AQP5 protein and its <italic>mRNA</italic>
in the parotid gland (PG), suggesting coupling of the AQP5 dynamic and amylase secretion-restoration cycle. In the PG, lipopolysaccharide (LPS) is shown to activate mitogen-activated protein kinase (MAPK) and nuclear factor-kappa B (NF-κB) signalings and potentially downregulate AQP5 expression via cross coupling of activator protein-1 (AP-1) and NF-κB. In most species, Ser-156 and Thr-259 of AQP5 are experimentally phosphorylated, which is enhanced by cAMP analogues and forskolin. cAMP-dependent phosphorylation of AQP5 does not seem to be markedly involved in regulation of its intracellular trafficking but seems to play a role in its constitutive expression and lateral diffusion in the cell membrane. Additionally, Ser-156 phosphorylation may be important for cancer development.</p>
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<affiliations><list><country><li>Japon</li>
</country>
</list>
<tree><noCountry><name sortKey="Hasegawa, Takahiro" sort="Hasegawa, Takahiro" uniqKey="Hasegawa T" first="Takahiro" last="Hasegawa">Takahiro Hasegawa</name>
<name sortKey="Yao, Chenjuan" sort="Yao, Chenjuan" uniqKey="Yao C" first="Chenjuan" last="Yao">Chenjuan Yao</name>
<name sortKey="Yoshimura, Hiroshi" sort="Yoshimura, Hiroshi" uniqKey="Yoshimura H" first="Hiroshi" last="Yoshimura">Hiroshi Yoshimura</name>
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