title: Transient occurrence of 27 kDa heat-shock protein in the terminal tubule cells during postnatal development of the rat submandibular gland.
abstract: It has been suggested that the 27 kDa heat-shock protein (Hsp27) plays a role at crucial cellular checkpoints for proliferation, apoptosis, and differentiation. We examined the immunolocalization of Hsp27 in the rat submandibular gland during postnatal development, wherein acinar cells proliferate and differentiate at earlier postnatal periods. At 2 weeks of age, weak Hsp27 immunoreactivity was distributed diffusely over all gland components. At 3 weeks, Hsp27 immunoreactivity disappeared in most parts of the acini and ducts, but was intensely accumulated in a small cell population located in the acinar center. This population was composed mostly of terminal tubule (TT) type I cells. At 4 weeks, the Hsp27-immunopositive cell population in the acinar center was composed primarily of immature (type II) acinar cells, partly of immature (granulated) intercalated duct (ID) cells, and occasionally of apoptotic cells. After 5 weeks, all acinar components became mature and were no longer immunoreactive for Hsp27. When acinar cell differentiation was accelerated by administration of isoproterenol to 3-week-old rats for 7 days, the number of Hsp27-positive cells was significantly lower than in the control gland at 4 weeks, confirming that Hsp27 expression is downregulated in mature acinar cells. These results suggest that at around 3-4 weeks in postnatal development, the centroacinar TT cells stop proliferating and begin to differentiate into acinar and ID cells, and occasionally undergo apoptosis. Hsp27 is transiently expressed in the centroacinar TT cells during this critical period, and thus may play a role in their differentiation into the immediate descendants.
authors.affiliation: Department of Histology and Embryology, Kanazawa University Graduate School of Medical Science, Kanazawa, Japan.
authors.forename: O
authors.initials: O
authors.lastname: Amano
authors.forename: Y
authors.initials: Y
authors.lastname: Kudo
authors.forename: M
authors.initials: M
authors.lastname: Shimada
authors.forename: T
authors.initials: T
authors.lastname: Wakayama
authors.forename: M
authors.initials: M
authors.lastname: Yamamoto
authors.forename: S
authors.initials: S
authors.lastname: Iseki
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002452:Cell Count; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D007124:Immunoenzyme Techniques; D017403:In Situ Hybridization; D007545:Isoproterenol / Q000494:pharmacology; D008297:Male; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013363:Submandibular Gland / Q000187:drug effects / Q000254:growth & development* / Q000378:metabolism*
chemical_list: D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D007545:Isoproterenol