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Institute of Biomedicine/Anatomy (I.V., M.K., N.P., T.K., Y.T.K.), Haartmaninkatu 8, University of Helsinki, FIN-00014 Helsinki, Finland; Hospital for Children and Adolescents, Helsinki University Central Hospital (M.K.), Stenbäckinkatu 11, FIN-00029 Hus, Finland; Department of Experimental Pathology, University of Lund (L.M.S.), SE-22362 Lund, Sweden; Department of Integrative Medical Biology, Section for Anatomy, Umea University (L.-E.T.), SE-90187 Umea, Sweden; and Department of Medicine/Invärtes Medicin, Helsinki University Central Hospital, ORTON Research Institute and the Orthopedic Hospital of the Invalid Foundation (Y.T.K.), FIN-00280 Helsinki, Finland
Address all correspondence and requests for reprints to: Prof. Ismo Virtanen, M.D., Institute of Biomedicine/Anatomy, P.O. Box 63, Haartmaninkatu 8, University of Helsinki, FIN-00014 Helsinki, Finland. E-mail: ismo.virtanen{at}helsinki.fi.
Laminin has been proposed to influence the function of human adrenal cortex. We have studied the distribution of laminin (Ln) chains using immunofluorescence in human fetal and adult adrenal cortex. In the fetal gland Ln
2- and
5-chains were weakly expressed in the definitive zone, whereas Ln
4-, ß1-, and
1-chains occurred around vessels. In the adult gland, Ln
2-,
5-, and
1-chains were found in epithelial basement membranes (BM) in all cortical zones, Ln
4-chain in vessels, Ln ß1-chain in outer zone, and Ln ß2-chain in the two inner zones of the cortex, respectively. Among the integrins in adult gland, integrin
3-subunit was confined to basal surfaces of cortical cells,
6 to vessels,
1 to the stroma, and
2 diffusely to epithelial cells. Lutheran glycoprotein and dystroglycan occurred in the fetal gland diffusely in the definitive zone and throughout the epithelium in the adult. The isoform composition of BM of the adult adrenal gland is distinct, with Ln-2 and -10 in BM of the outer zone and Ln-4 and -11 in BM of the two inner zones. The results suggest that integrin
3ß1 and Lutheran are candidate receptors for Ln-10 and -11, whereas dystroglycan probably binds Ln-2 and -4.
This work was supported by clinical EVO research grants (TYH 0056, TYH 0215, TYH 0341, and TYH 8307), an Invalid Foundation 9750/2 grant, Finska Läkaresällskapet, the Academy of Finland, Center for Technological Advancement, Ministry of Education, and University of Helsinki Group of Excellence scheme.
Abbreviations: BM, Basement membrane; ECM, extracellular matrix; Int, integrin; Ln, laminin; Lu, Lutheran; MAb, monoclonal antibodies; ZF, zona fasciculata; ZG, zona glomerulosa; ZR, zona reticularis.
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