title: Expression of genes coding for proteoglycans and Wilms' tumour susceptibility gene 1 (WT1) by variously differentiated benign human mesothelial cells.
abstract: Mesothelial cells are of mesenchymal origin, although they also have epithelial characteristics. Such cells obtained from benign effusions are not terminally differentiated and can be kept in short-term cultures. These cultures grow with an either epithelial or fibroblast-like phenotype, a pattern which is stable through the early passages. Several factors have been associated with mesothelial differentiation. The Wilms' tumour susceptibility gene 1 (WT1) is expressed during transitions of mesenchyme to epithelial tissues, as in the embryonic kidney, and it has been suggested as a marker for the mesothelial lineage. The proteoglycans (PGs) and hyaluronan are also differentially synthesised by epithelial and fibroblastic malignant mesothelioma cells and the cell surface PGs seem to indicate phenotypic differentiation even in epithelial tumours. To investigate how the epithelial and fibroblast-like differentiation of benign mesothelial cells was correlated to WT1, PGs and hyaluronan synthase, we studied their expression by semiquantitative reverse transcriptase polymerase chain reaction (RT-PCR) analyses. The expressions of these genes were all associated with a variation in phenotypic differentiation. Cell lines with epithelial morphology expressed more mRNA coding for WT1 and cell surface PGs than did the fibroblastic ones, the difference being greatest for syndecan-4 and glypican. The increase in WT1-associated mRNA was about as great as that of syndecans. Fibroblast-like cells, on the other hand, expressed substantially more of the matrix PGs versican and biglycan, while decorin expression was detected in only trace amounts in both morphological phenotypes. Hyaluronan synthase varied individually between the cell lines, although epithelial cells often expressed higher levels. The results indicate that the regulation of mesothelial differentiation is multifactorial and also involves WT1 and several PGs.
authors.affiliation: Department of IMPI, Division of Pathology, Karolinska Institute, F46, Huddinge University Hospital, S-14186 Huddinge, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Gulyás
authors.forename: K
authors.initials: K
authors.lastname: Dobra
authors.forename: A
authors.initials: A
authors.lastname: Hjerpe
mesh_terms: D000199:Actins / Q000096:biosynthesis; D064032:Calbindin 2; D002454:Cell Differentiation / Q000235:genetics*; D002478:Cells, Cultured; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000235:genetics*; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism* / Q000648:ultrastructure; D015870:Gene Expression; D014453:Glucuronosyltransferase / Q000096:biosynthesis; D016695:Glycosyltransferases; D006801:Humans; D000076002:Hyaluronan Synthases; D007150:Immunohistochemistry; D007633:Keratins / Q000096:biosynthesis; D008565:Membrane Proteins; D008855:Microscopy, Electron, Scanning; D010996:Pleural Effusion / Q000166:cytology; D011509:Proteoglycans / Q000096:biosynthesis / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D064030:S100 Calcium Binding Protein G / Q000096:biosynthesis; D014157:Transcription Factors / Q000096:biosynthesis / Q000235:genetics*; D014166:Transferases; D014746:Vimentin / Q000096:biosynthesis; D025721:WT1 Proteins; D029867:Xenopus Proteins
chemical_list: D000199:Actins; D064032:Calbindin 2; D004268:DNA-Binding Proteins; D008565:Membrane Proteins; D011509:Proteoglycans; D064030:S100 Calcium Binding Protein G; D014157:Transcription Factors; D014746:Vimentin; D025721:WT1 Proteins; D029867:Xenopus Proteins; D007633:Keratins; D014166:Transferases; D016695:Glycosyltransferases; D014453:Glucuronosyltransferase; C056944:HAS1 protein, Xenopus; D000076002:Hyaluronan Synthases