title: Elafin expression in human fetal and adult submandibular glands.
abstract: Elafin, a bifunctional protein, has the NH(2)-terminal domain functions as a transglutaminase substrate for crosslinking to lysine-containing proteins and the COOH-terminal whey acidic protein domain as a potent anti-elastase. Human fetal submandibular glands (n=100) and adult submandibular glands (n=10) were used to elucidate the expression pattern of elafin in the developmental processes of human submandibular gland by immunohistochemistry, in situ hybridization, and western blot analysis. Elafin mRNA was expressed both in the gland epithelium and intralobular mesenchymal tissue of fetal submandibular gland in an early developmental stage (10-18 weeks) and an early intermediate developmental stage (EIDS; 19-24 weeks). The elafin antigen was also found in the intralobular mesenchyme of submandibular gland in the same stages. Thereafter, elafin was transitionally expressed in the ducts and acini of submandibular glands. In the late intermediate developmental stage (LIDS; 25-32 weeks) and the late developmental stage (LDS; 33-40 weeks), elafin became markedly positive in the excretory and striated ducts but weakly positive in the intralobular mesenchymal tissue. The elafin was heavily present in the excretory and striated ducts of adult submandibular gland, while it was sparse in the intralobular mesenchymal tissues. Western blot analysis showed the protein extracts from submandibular glands of EIDS, LIDS, and LDS, adult submandibular gland, fetal tissues (8 weeks), and adult parotid saliva migrated into multiple bands, about 25, 50, 65, and 140 kDa, which were higher than the putative size of elafin protein, 12 kDa. These data suggest that elafin, anti-elastase, is an essential component highly utilized during the morphogenetic processes of fetal salivary gland development and continuously plays a role for the protection of the tubuloalveolar structures of adult salivary gland.
authors.affiliation: Department of Oral Pathology, College of Dentistry, Kangnung National University, Korea.
authors.forename: Suk Keun
authors.initials: SK
authors.lastname: Lee
authors.forename: Sang Shin
authors.initials: SS
authors.lastname: Lee
authors.forename: Shigehisa
authors.initials: S
authors.lastname: Hirose
authors.forename: Sang Chul
authors.initials: SC
authors.lastname: Park
authors.forename: Je Geun
authors.initials: JG
authors.lastname: Chi
authors.forename: Soo Il
authors.initials: SI
authors.lastname: Chung
authors.forename: Masahiko
authors.initials: M
authors.lastname: Mori
mesh_terms: D015153:Blotting, Western; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D014176:Protein Biosynthesis; D053491:Proteinase Inhibitory Proteins, Secretory; D011506:Proteins / Q000235:genetics*; D013363:Submandibular Gland / Q000737:chemistry / Q000196:embryology / Q000378:metabolism*; D013997:Time Factors
chemical_list: D053491:Proteinase Inhibitory Proteins, Secretory; D011506:Proteins