Glycosylation is a widely utilized chemical modification of proteins and lipids in mammalian cells during which saccharide units are covalently attached to the target structures and then sequentially elongated and branched - reactions facilitated by a large number of various glycosyltransferases. Alterations in this process have been associated with malignant transformation. To clarify the critical role of glycosyltransferases, altered Mucins (MUC), and RTKs in human ovarian and endometrial neoplasms, the study will examine the immunohistochemical expression profiles of glycosyltransferases (including β-1,4-Galactosyltransferase 1 (B4GALT1), β-1,4-Galactosyltransferase 3 (B4GALT3), β-1,4-N-Acetyl-Galactosaminyl Transferase 3 (B4GALNT3), Polypeptide N-Acetylgalactosaminyltransferase 2 (GALNT2), Polypeptide N-Acetylgalactosaminyltransferase 6 (GALNT6), β1,4-N-acetylglucosaminyltransferase III (GlcNAcT-III), β1,4-N-acetylglucosaminyltransferase V (GlcNAcT-V), and Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1 (C1GALT1), Mucins (including MUC1, MUC3, MUC15, and MUC20) and receptor tyrosin kinases (RTKs) family (including epidermal growth factor receptor (EGFR), Src, VEGFR, and c-Met) in various stages and/or histologic subtypes of human ovarian and endometrial neoplasms and tissue microarrays, and compare them with clinicopathologic factors including outcome of the patients.
