{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T13:45:23Z","timestamp":1791121523170,"version":"4.1.0"},"reference-count":61,"publisher":"American Physiological Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Gastrointestinal and Liver Physiology"],"published-print":{"date-parts":[[2010,11]]},"abstract":"<jats:p> Chorda tympani denervation (CTD) of rats was earlier shown to result in loss of submandibular gland (SMG) weight (at only 1 wk) and in continued reduction in aquaporin 5 (AQP5) protein expression (until 4 wk), without affecting its mRNA synthesis (Li X, Azlina A, Karabasil MR, Purwanti N, Hasegawa T, Yao C, Akamatsu T, Hosoi K. Am J Physiol Gastrointest Liver Physiol 295: G112\u2013G123, 2008). The present study indicated that despite elevation of bax, a proapoptosis protein, by CTD, the operation also increased the level of bcl-2, an antiapoptosis protein, in the SMG. Terminal deoxynucleotidyl transferase dUTP nick-end labeling (TUNEL assay) showed no increase in the number of apoptotic cells in the SMG. CTD, however, induced strongly and transiently (at 1\u20133 days) the protein expression of LC3B-II, a marker protein of autophagosomes, suggesting that the reduction in the gland weight was due to onset of autophagy by CTD. Upon CTD, Lamp2, a lysosomal marker, gradually increased in amount, reaching a peak at the 14th day. Immunohistochemical analysis revealed an increase in the number of lysosome-like structures positive for both AQP5 and Lamp2 in the acinar cells of the SMG after CTD; similar changes were observed also for AQP5 and LC3Bs. These data suggest that AQP5 in the SMG entered autophagosomes and\/or lysosomes for degradation upon CTD. In vitro AQP5-degrading activity was found in the SMG extracts, and such activity was shown to be increased by CTD. Inhibitor experiments implied cathepsins B and L to be candidate enzymes for this degradation under normal and CTD conditions, respectively. <\/jats:p>","DOI":"10.1152\/ajpgi.00194.2010","type":"journal-article","created":{"date-parts":[[2010,8,6]],"date-time":"2010-08-06T03:37:33Z","timestamp":1281065853000},"page":"G1106-G1117","source":"Crossref","is-referenced-by-count":25,"title":["Roles of lysosomal proteolytic systems in AQP5 degradation in the submandibular gland of rats following chorda tympani parasympathetic denervation"],"prefix":"10.1152","volume":"299","author":[{"given":"Ahmad","family":"Azlina","sequence":"first","affiliation":[{"name":"Department of Molecular Oral Physiology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Purevjav","family":"Javkhlan","sequence":"additional","affiliation":[{"name":"Department of Molecular Oral Physiology, and"},{"name":"Department of Periodontology and Endodontology, Institute of Health Biosciences, The University of Tokushima Graduate School, Tokushima, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuka","family":"Hiroshima","sequence":"additional","affiliation":[{"name":"Department of Molecular Oral Physiology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takahiro","family":"Hasegawa","sequence":"additional","affiliation":[{"name":"Department of Molecular Oral Physiology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chenjuan","family":"Yao","sequence":"additional","affiliation":[{"name":"Department of Molecular Oral Physiology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tetsuya","family":"Akamatsu","sequence":"additional","affiliation":[{"name":"Department of Molecular Oral Physiology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuo","family":"Hosoi","sequence":"additional","affiliation":[{"name":"Department of Molecular Oral Physiology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"24","reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1007\/s00424-003-1109-9"},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.1152\/ajpgi.00316.2004"},{"key":"B3","first-page":"387","volume":"110","author":"Bichet DG","year":"1998","journal-title":"Proc Assoc Am Physicians"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.1113\/expphysiol.2008.045112"},{"key":"B5","doi-asserted-by":"publisher","DOI":"10.1016\/j.jneuroim.2004.10.020"},{"key":"B6","doi-asserted-by":"publisher","DOI":"10.1007\/s11695-008-9453-7"},{"key":"B7","doi-asserted-by":"publisher","DOI":"10.1016\/S0169-328X(98)00223-X"},{"key":"B8","first-page":"330","volume":"16","author":"Dibas A","year":"2010","journal-title":"Mol Vis"},{"key":"B9","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2005.09.171"},{"key":"B10","doi-asserted-by":"publisher","DOI":"10.1159\/000061124"},{"key":"B11","doi-asserted-by":"publisher","DOI":"10.1152\/ajprenal.0158.2001"},{"key":"B12","doi-asserted-by":"publisher","DOI":"10.1016\/j.archoralbio.2004.02.005"},{"key":"B13","doi-asserted-by":"publisher","DOI":"10.1261\/rna.1399509"},{"key":"B14","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0808691105"},{"key":"B15","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(81)90184-3"},{"key":"B16","doi-asserted-by":"publisher","DOI":"10.1038\/361549a0"},{"key":"B17","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamem.2009.03.009"},{"key":"B18","doi-asserted-by":"publisher","DOI":"10.1038\/nature02503"},{"key":"B19","doi-asserted-by":"publisher","DOI":"10.2535\/ofaj.80.41"},{"key":"B20","doi-asserted-by":"publisher","DOI":"10.1007\/s10157-008-0118-6"},{"key":"B21","doi-asserted-by":"publisher","DOI":"10.1152\/ajpregu.1994.267.3.R747"},{"key":"B22","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0608384104"},{"key":"B23","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.ph.58.030196.003155"},{"key":"B24","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.1997.273.5.C1541"},{"key":"B25","unstructured":"Kirschke H , Cathepsin L.  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