| Summary: | Lectins act as effective diagnostic tools for screening potential cancer biomarkers because of their ability to recognize the carbohydrate moiety of glycoproteins present in most complex tissues and fluids. This study aimed to propose an ideal procedure for the precise recovery of glycoprotein-derived oligosaccharides using freshwater microalgal lectins and to validate their effectiveness in the enrichment of glycoproteins present in the sera. A total of 5 ovarian cancer (OC) patients with grade III were included in the present study to identify potential biomarkers present in the serum samples. Proteomic analysis of OC serum samples was carried out using lectin-affinity entrapment followed by affinity chromatography coupled with liquid chromatography-electrospray ionization-quadrupole-time of flight-mass spectrometry (LC-ESI-Q-TOF-MS/MS) methods. Proteins with the highest Mascot score were found to be expressed in the OC III serum group and were identified as serotransferrin (TRF), haptoglobin, hemopexin, serine protease 1 (Sp1), ceruloplasmin, alpha-1-antitrypsin, alpha-1-antichymotrypsin (ACT), alpha-2-HS glycoprotein (AHSG), and immunoglobulins (Igs). Among them serine protease 1 was recovered at a high-level using lectin-affinity techniques. PRSS 1 gene is responsible for the expression of Sp1 in OC serum. The present study evaluated the usefulness of microalgal lectins in the identification of molecular markers present in serum samples of OC. This data provide novel insights regarding the presence of Sp1 in OC serum specimen, paving the way for further investigations related to glycosylation patterns of Sp1 and clinical applicability.
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