Immunohistochemical characterization of epithelial cells in human lacrimal glands. I. Normal major and accessory lacrimal glands

• Published in: Graefe's archive for clinical and experimental ophthalmology Vol. 228; no. 1; p. 58
• Main Authors: Vigneswaran, N, Wilk, C M, Heese, A, Hornstein, O P, Naumann, G O
• Format: Journal Article
• Language: English
• Published: Germany 1990
• Subjects: Actins - metabolism; Antibodies, Monoclonal; Antibody Specificity; Biomarkers; Epithelium - metabolism; Humans; Immunoenzyme Techniques; Keratins - metabolism; Lacrimal Apparatus - cytology; Lacrimal Apparatus - metabolism; Lactoferrin - metabolism; Muramidase - metabolism; S100 Proteins - metabolism; Vimentin - metabolism
• ISSN: 0721-832X; 1435-702X
• DOI: 10.1007/BF02764293

Expression patterns of cytokeratins (CKs), actin, lactoferrin (Lf), lysozyme (Ly), vimentin, and S-100 protein were immunohistochemically examined in paraffin sections from eight normal major and accessory lacrimal glands (LGs). Luminal duct cells and a number of secretory cells stained with the antibodies (ABs) KL1 and Pkk1 (CK 7, 8, 17, 18), while basal duct and myoepithelial cells reacted with the AB 34 beta E12 (CK 5). Myoepithelial cells expressing CK 5 and actin were restricted to acini and intralobular ducts, and their number was greater in major LGs than accessory ones. Lf and Ly were found in 50%-75% of acini and intralobular ducts. Vimentin was absent in parenchyma of LGs. S-100 protein reaction was observed in a number of acinar and luminal duct cells of major LGs whereas epithelia of accessory LGs remained negative. Distribution patterns of CKs, Lf, and Ly in major and accessory LGs are identical. The difference with respect to the number of myoepithelial cells as well as S-100 protein reactivity between major and accessory LGs reactivity appeared to be relevant to the differences in their secretory mechanisms and local environment.