Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions
Identifieur interne : 000158 ( Pmc/Checkpoint ); précédent : 000157; suivant : 000159Dynamics 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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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions</title><author><name sortKey="Hosoi, Kazuo" sort="Hosoi, Kazuo" uniqKey="Hosoi K" first="Kazuo" last="Hosoi">Kazuo Hosoi</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af2-ijms-21-01182">Kosei Pharmaceutical Co., Ltd., Osaka-shi, Osaka 540–0039, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Kosei Pharmaceutical Co., Ltd., Osaka-shi, Osaka 540–0039</wicri:regionArea><wicri:noRegion>Osaka 540–0039</wicri:noRegion></affiliation></author><author><name sortKey="Yao, Chenjuan" sort="Yao, Chenjuan" uniqKey="Yao C" first="Chenjuan" last="Yao">Chenjuan Yao</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation></author><author><name sortKey="Hasegawa, Takahiro" sort="Hasegawa, Takahiro" uniqKey="Hasegawa T" first="Takahiro" last="Hasegawa">Takahiro Hasegawa</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation></author><author><name sortKey="Yoshimura, Hiroshi" sort="Yoshimura, Hiroshi" uniqKey="Yoshimura H" first="Hiroshi" last="Yoshimura">Hiroshi Yoshimura</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation></author><author><name sortKey="Akamatsu, Tetsuya" sort="Akamatsu, Tetsuya" uniqKey="Akamatsu T" first="Tetsuya" last="Akamatsu">Tetsuya Akamatsu</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af3-ijms-21-01182">Field of Biomolecular Functions and Technology, Division of Bioscience and Bioindustry, Graduate School of Technology, Industrial and Social Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8513, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Field of Biomolecular Functions and Technology, Division of Bioscience and Bioindustry, Graduate School of Technology, Industrial and Social Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8513</wicri:regionArea><wicri:noRegion>Tokushima 770-8513</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">32053992</idno><idno type="pmc">7072788</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7072788</idno><idno type="RBID">PMC:7072788</idno><idno type="doi">10.3390/ijms21041182</idno><date when="2020">2020</date><idno type="wicri:Area/Pmc/Corpus">000A33</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000A33</idno><idno type="wicri:Area/Pmc/Curation">000A33</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000A33</idno><idno type="wicri:Area/Pmc/Checkpoint">000158</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000158</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions</title><author><name sortKey="Hosoi, Kazuo" sort="Hosoi, Kazuo" uniqKey="Hosoi K" first="Kazuo" last="Hosoi">Kazuo Hosoi</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af2-ijms-21-01182">Kosei Pharmaceutical Co., Ltd., Osaka-shi, Osaka 540–0039, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Kosei Pharmaceutical Co., Ltd., Osaka-shi, Osaka 540–0039</wicri:regionArea><wicri:noRegion>Osaka 540–0039</wicri:noRegion></affiliation></author><author><name sortKey="Yao, Chenjuan" sort="Yao, Chenjuan" uniqKey="Yao C" first="Chenjuan" last="Yao">Chenjuan Yao</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation></author><author><name sortKey="Hasegawa, Takahiro" sort="Hasegawa, Takahiro" uniqKey="Hasegawa T" first="Takahiro" last="Hasegawa">Takahiro Hasegawa</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation></author><author><name sortKey="Yoshimura, Hiroshi" sort="Yoshimura, Hiroshi" uniqKey="Yoshimura H" first="Hiroshi" last="Yoshimura">Hiroshi Yoshimura</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation></author><author><name sortKey="Akamatsu, Tetsuya" sort="Akamatsu, Tetsuya" uniqKey="Akamatsu T" first="Tetsuya" last="Akamatsu">Tetsuya Akamatsu</name><affiliation><nlm:aff id="af1-ijms-21-01182">Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af3-ijms-21-01182">Field of Biomolecular Functions and Technology, Division of Bioscience and Bioindustry, Graduate School of Technology, Industrial and Social Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8513, Japan</nlm:aff><country xml:lang="fr">Japon</country><wicri:regionArea>Field of Biomolecular Functions and Technology, Division of Bioscience and Bioindustry, Graduate School of Technology, Industrial and Social Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8513</wicri:regionArea><wicri:noRegion>Tokushima 770-8513</wicri:noRegion></affiliation></author></analytic><series><title level="j">International Journal of Molecular Sciences</title><idno type="eISSN">1422-0067</idno><imprint><date when="2020">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Preston, G M" uniqKey="Preston G">G.M. Preston</name></author><author><name sortKey="Carroll, T P" uniqKey="Carroll T">T.P. Carroll</name></author><author><name sortKey="Guggino, W B" uniqKey="Guggino W">W.B. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Int J Mol Sci</journal-id><journal-id journal-id-type="iso-abbrev">Int J Mol Sci</journal-id><journal-id journal-id-type="publisher-id">ijms</journal-id><journal-title-group><journal-title>International Journal of Molecular Sciences</journal-title></journal-title-group><issn pub-type="epub">1422-0067</issn><publisher><publisher-name>MDPI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">32053992</article-id><article-id pub-id-type="pmc">7072788</article-id><article-id pub-id-type="doi">10.3390/ijms21041182</article-id><article-id pub-id-type="publisher-id">ijms-21-01182</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Hosoi</surname><given-names>Kazuo</given-names></name><xref ref-type="aff" rid="af1-ijms-21-01182">1</xref><xref ref-type="aff" rid="af2-ijms-21-01182">2</xref><xref rid="c1-ijms-21-01182" ref-type="corresp">*</xref><xref ref-type="author-notes" rid="fn1-ijms-21-01182">†</xref></contrib><contrib contrib-type="author"><name><surname>Yao</surname><given-names>Chenjuan</given-names></name><xref ref-type="aff" rid="af1-ijms-21-01182">1</xref></contrib><contrib contrib-type="author"><name><surname>Hasegawa</surname><given-names>Takahiro</given-names></name><xref ref-type="aff" rid="af1-ijms-21-01182">1</xref></contrib><contrib contrib-type="author"><name><surname>Yoshimura</surname><given-names>Hiroshi</given-names></name><xref ref-type="aff" rid="af1-ijms-21-01182">1</xref><xref rid="c1-ijms-21-01182" ref-type="corresp">*</xref></contrib><contrib contrib-type="author"><name><surname>Akamatsu</surname><given-names>Tetsuya</given-names></name><xref ref-type="aff" rid="af1-ijms-21-01182">1</xref><xref ref-type="aff" rid="af3-ijms-21-01182">3</xref></contrib></contrib-group><aff id="af1-ijms-21-01182"><label>1</label>Department of Molecular Oral Physiology, Division of Oral Science, Graduate School of Biomedical Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8504, Japan;<email>ychenjuan@tokushima-u.ac.jp</email> (C.Y.);<email>thase@tokushima-u.ac.jp</email> (T.H.);<email>akamatsu_t@tokushima-u.ac.jp</email> (T.A.)</aff><aff id="af2-ijms-21-01182"><label>2</label>Kosei Pharmaceutical Co., Ltd., Osaka-shi, Osaka 540–0039, Japan</aff><aff id="af3-ijms-21-01182"><label>3</label>Field of Biomolecular Functions and Technology, Division of Bioscience and Bioindustry, Graduate School of Technology, Industrial and Social Sciences, Tokushima University, Tokushima-shi, Tokushima 770-8513, Japan</aff><author-notes><corresp id="c1-ijms-21-01182"><label>*</label>Correspondence: <email>khosoi@tokushima-u.ac.jp</email> (K.H.); <email>hyoshimu@tokushima-u.ac.jp</email> (H.Y.)</corresp><fn id="fn1-ijms-21-01182"><label>†</label><p>Professor emeritus, Tokushima University.</p></fn></author-notes><pub-date pub-type="epub"><day>11</day><month>2</month><year>2020</year></pub-date><pub-date pub-type="collection"><month>2</month><year>2020</year></pub-date><volume>21</volume><issue>4</issue><elocation-id>1182</elocation-id><history><date date-type="received"><day>10</day><month>1</month><year>2020</year></date><date date-type="accepted"><day>07</day><month>2</month><year>2020</year></date></history><permissions><copyright-statement>© 2020 by the authors.</copyright-statement><copyright-year>2020</copyright-year><license license-type="open-access"><license-p>Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>).</license-p></license></permissions><abstract><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></abstract><kwd-group><kwd>aquaporin 5 (AQP5)</kwd><kwd>submandibular gland (SMG)</kwd><kwd>parotid gland (PG)</kwd><kwd>chorda tympani nerve</kwd><kwd>isoproterenol (IPR)</kwd><kwd>lipopolysaccharide (LPS)</kwd><kwd>mitogen-activated protein kinase (MAPK)</kwd><kwd>nuclear factor-kappa B (NF-κB)</kwd><kwd>phosphorylation</kwd></kwd-group></article-meta></front><floats-group><fig id="ijms-21-01182-f001" orientation="portrait" position="float"><label>Figure 1</label><caption><p>Expression and localization of aquaporin 5 (AQP5) in the developing submandibular gland (SMG) of rats (<bold>a</bold>), and in the ligated SMG of mice (<bold>b</bold>). (<bold>a</bold>) Expression of <italic>AQP5 mRNA</italic> in the embryonic rat SMG was analyzed by reverse transcriptase-polymerase chain reaction (RT-PCR) and Northern blot analyses. Localization of AQP5 protein was analyzed by immunohistochemistry in the rat SMG at the indicated prenatal and postnatal days. In the right panel, “d” indicates typical duct, and a scale bar, 25 µm; (<bold>b</bold>) Effects of duct ligation of the mouse SMG on changes in the immunohistochemical localization of AQP5 was analyzed. Green fluorescence indicates the localization of AQP5 on the indicated day after ligation. Arrowheads and asterisks indicate typical acini and ducts, respectively. A scale bar, 100 µm. (<bold>a</bold>,<bold>b</bold>) modified from [<xref rid="B15-ijms-21-01182" ref-type="bibr">15</xref>,<xref rid="B27-ijms-21-01182" ref-type="bibr">27</xref>], respectively.</p></caption><graphic xlink:href="ijms-21-01182-g001"></graphic></fig><fig id="ijms-21-01182-f002" orientation="portrait" position="float"><label>Figure 2</label><caption><p>Hypothetical mechanism for regulation of salivary gland AQP5 by the autonomic nervous system and chemical transmitters. (<bold>a</bold>) Suppression of autophagosome activation by chorda tympani nerve leading to maintenance of membrane AQP5 levels in the rat SMG. Chorda tympani denervation (CTD; parasympathectomy) un-suppresses autophagosome activation leading to degradation of AQP5; (<bold>b</bold>) IPR-induced increase in the membrane AQP5 protein and <italic>AQP5 mRNA</italic> in the PG of mice. Green dots in this figure represent AQP5 protein molecule.</p></caption><graphic xlink:href="ijms-21-01182-g002"></graphic></fig><fig id="ijms-21-01182-f003" orientation="portrait" position="float"><label>Figure 3</label><caption><p>Hypothetical mechanism for lipopolysaccharide (LPS)-induced signaling and downregulation of <italic>AQP5</italic> transcription via cross-coupling of mitogen-activated protein kinase (AP-1) and nuclear factor-kappa B (NF-κB) (a model proposed from mouse experiment). TIS, transcription initiation site.</p></caption><graphic xlink:href="ijms-21-01182-g003"></graphic></fig></floats-group></pmc><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></noCountry><country name="Japon"><noRegion><name sortKey="Hosoi, Kazuo" sort="Hosoi, Kazuo" uniqKey="Hosoi K" first="Kazuo" last="Hosoi">Kazuo Hosoi</name></noRegion><name sortKey="Akamatsu, Tetsuya" sort="Akamatsu, Tetsuya" uniqKey="Akamatsu T" first="Tetsuya" last="Akamatsu">Tetsuya Akamatsu</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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