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The glycosylation of proteins is known to change in tumor cells during the development of HCC as the result of alterations in the levels of glycosyltransferases, such as increased fucosylation of Golgi Protein 73 and \u03b1\u2010fetoprotein. These structural changes can influence the function or physiochemical properties of a protein, resulting in abnormal cancer cell behavior. Therefore, identification of HCC\u2010related glycoprotein markers and analysis of glycan structural alterations might assist in the early detection of HCC. Here, we summarize lectin\u2010based glycoproteomic strategies for the discovery of relevant biomarkers of HCC. The carbohydrate\u2010binding specificities of different lectins offer a biological affinity approach that complements existing MS capabilities. These strategies involve the enrichment of glycoproteins or glycopeptides by lectins, followed by releasing carbohydrates with peptide\u2010<jats:italic>N<\/jats:italic>\u2010glycosidase F or reductive \u03b2\u2010elimination. The obtained glycopeptides are then identified by automated MS\/MS and structural analysis of glycans is performed through modern methods such as quadrupole IT\u2010TOF, MALDI\u2010TOF\/TOF and lectin microarray. These strategies will lead to faster and more clinically adaptable tests with greater sensitivity and specificity.<\/jats:p>","DOI":"10.1002\/elps.200900064","type":"journal-article","created":{"date-parts":[[2009,8,26]],"date-time":"2009-08-26T08:14:06Z","timestamp":1251274446000},"page":"2957-2966","source":"Crossref","is-referenced-by-count":64,"title":["Lectin\u2010based glycoproteomics to explore and analyze hepatocellular carcinoma\u2010related glycoprotein markers"],"prefix":"10.1002","volume":"30","author":[{"given":"Zhi","family":"Dai","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jian","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuang\u2010Jian","family":"Qiu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yin\u2010Kun","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jia","family":"Fan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,8,26]]},"reference":[{"key":"e_1_2_9_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/nbt0303-255"},{"key":"e_1_2_9_3_2","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200600129"},{"key":"e_1_2_9_4_2","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/3.2.97"},{"key":"e_1_2_9_5_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M311627200"},{"key":"e_1_2_9_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0304-4165(02)00404-X"},{"key":"e_1_2_9_7_2","first-page":"5309","volume":"56","author":"Hakomori S.","year":"1996","journal-title":"Cancer Res."},{"key":"e_1_2_9_8_2","doi-asserted-by":"publisher","DOI":"10.1023\/A:1006961532182"},{"key":"e_1_2_9_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.23.13811"},{"key":"e_1_2_9_10_2","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1093\/clinchem\/46.6.795","volume":"46","author":"Durand G.","year":"2000","journal-title":"Clin. 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