2011, Número 4
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Neumol Cir Torax 2011; 70 (4)
Determinación del perfil de glicosilación de los glicoconjugados de membrana de la línea celular A427 de adenocarcinoma pulmonar humano mediante el uso de lectinas
Serrato JA, Lascurain R, García-Herrera D, Gorocica RP
Idioma: Español
Referencias bibliográficas: 36
Paginas: 236-242
Archivo PDF: 98.87 Kb.
RESUMEN
Gracias a los avances recientes en el área de la glicobiología, los glicanos presentes en los glicoconjugados de la superficie celular han adquirido potencial como biomarcadores para el diagnóstico específico y oportuno del cáncer pulmonar. Sin embargo, la ubicuidad inherente a los glicanos celulares dificulta en gran medida la identificación de estructuras sacarídicas específicas de células tumorales. El uso de líneas celulares es una estrategia que ayuda en el proceso de identificación de estructuras sacarídicas específicas cuando se desea desarrollar un método de diagnóstico. En el presente estudio se determinó, mediante el uso de lectinas, el perfil de glicosilación de los glicoconjugados de la línea celular A427 de adenocarcinoma pulmonar humano con la finalidad de identificar oligosacáridos que se expresan abundantemente en la membrana celular. Se utilizaron nueve lectinas para la identificación de estructuras de N- y O-oligosacáridos específicos. El análisis del perfil de glicosilación mostró mayor abundancia relativa de moléculas del tipo
Sialil-Tn, estructuras de
lactosamina y O-glicanos cortos como el antígeno
T, en comparación con los N-glicanos de tipo complejo, híbridos y de alta manosa. Los resultados del presente estudio sugieren que dichas moléculas pueden constituir marcadores potenciales de adenocarcinoma pulmonar.
REFERENCIAS (EN ESTE ARTÍCULO)
Hayat MJ, Howlader N, Reichman ME, Edwards BK. Cancer statistics, trends, and multiple cancer analisys from the Surveillance, Epidemiology, and End Results (SEER) Program. Oncologist 2007;12:20-37.
Jemal A, Siegel R, Ward E, Murray T, Xu J, Thun MJ. Cancer statistics, 2007. CA Cancer J Clin 2007;57:43-66.
Hammerschmidt S, Wirtz H. Lung cancer: current diagnosis and treatment. Dtsch Arztebl Int 2009;106:809-818.
Ludwig JA, Weinstein JN. Biomarkers in cancer staging, prognosis and treatment selection. Nat Rev Cancer 2005;5:845-856.
Perkins GL, Slater ED, Sanders GK, Prichard JG. Serum tumor markers. Am Fam Physician 2003;68:1075-1082.
Peracaula MR. Altered glycosylation in tumour proteins: biological implications. Afinidad 2007;64:346-355.
Varki A, editor. Essentials of glycobiology. 2nd ed. NY, USA: Cold Spring Harbor Laboratory Press; 2009.
Boland M, Rudd PM. Disease related glycosylation changes and biomarker discovery: challenges and possibilities in an emerging field [editorial]. Dis Markers 2008;25:189-192.
Durand G, Seta N. Protein glycosylation and diseases: blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring. Clin Chem 2000;46(6, Pt 1):795-805.
Rudd PM, Dwek RA. Structural glycobiology in medicine: Carbohydrates and glycoconjugates. Curr Opin Struct Biol 2006;16:559-560.
Dube DH, Bertozzi CR. Glycans in cancer and inflammation: potential for therapeutics and diagnostics. Nat Rev Drug Discov 2005;4:477-488.
Peracaula R, Barrabés S, Sarrats A, Rudd PM, de Llorens R. Altered glycosylation in tumours focused to cancer diagnosis. Dis Markers 2008;25: 207-218.
Shariat SF, Karam JA, Margulis V, Karakiewics PI. New blood-based biomarkers for the diagnosis, staging and prognosis of prostate cancer. BJU Int 2008;101:675-683.
Giard DJ, Aaronson SA, Todaro GJ, et ál. In vitro cultivation of human tumors: establishment of cell lines derived from a series of solid tumors. J Natl Cancer Inst 1973;51:1417-1423.
Odonkor CA, Achilefu S. Differential activity of caspase-3 regulates susceptibility of lung and breast tumor cell lines to Paclitaxel. Open Biochem J 2008;2:121-128.
Nilsson CL, editor. Lectins analytical technologies. Amsterdam, The Netherlands: Elsevier; 2007.
Savage D, Mattson G, Desai S, Nielander G, Morgensen S, Conklin E, editors. Biotinylation reagents. In: Avidin-biotin chemistry: a handbook. Rockford IL, USA: Pierce Chemical; 1992:41-48.
Erdile LF, Smith D, Berd D. Whole cell ELISA for detection of tumor antigen expression in tumor samples. J Immunol Methods 2001;258:47-53.
Ravindranath MH, Bauer PM, Cornillez-Ty C, García J, Morton DL. Quantitation of the density of cell surface carbohydrate antigens on cancer cells with a sensitive cell-suspension ELISA. J Immunol Methods 1996;197:51-67.
Álvarez-Fernández E, Carretero-Albiñana L. Lectin histochemistry of normal bronchopulmonary tissues and common forms of bronchogenic carcinoma. Arch Pathol Lab Med 1990;114:475-481.
Barkhordari A, Stoddart RW, McClure SF, McClure J. Lectin histochemistry of normal human lung. J Mol Histol 2004;35:147-156.
Thöm I, Schult-Kronefeld O, Burkholder I, et ál. Lectin histochemistry of metastatic adenocarcinomas of the lung. Lung Cancer 2007;56:391-397.
Osinaga E. Expression of cancer-associated simple mucin-type O-glycosylated antigens in parasites. IUBMB Life 2007;59:269-273.
Croce MV, Rabassa ME, Price MR, Segal-Eiras A. MUC1 mucin and carbohydrate associated antigens as tumor markers in head and neck squamous cell carcinoma. Pathol Oncol Res 2001;7:284-291.
Brockhausen I. Pathways of O-glycan biosynthesis in cancer cells. Biochim Biophys Acta 1999;1473:67-95.
Rose MC, Voynow JA. Respiratory tract mucin genes and mucin glycoproteins in health and disease. Physiol Rev 2006;86:245-278.
Springer GF, Chandrasekaran EV, Desai PR, Tegtmeyer H. Blood group Tn-active macromolecules from human carcinomas and erythrocytes: characterization of and specific reactivity with mono- and poly-clonal anti-Tn antibodies induced by various immunogens. Carbohydr Res 1988;178:271-292.
Springer GF. Tn epitope (N-acetyl-D-galactosamine alpha-O-serine/threonine) density in primary breast carcinoma: a functional predictor of aggressiveness. Mol Immunol 1989;26:1-5.
Srinivasan N, Bane SM, Ahire SD, Ingle AD, Kalraiya RD. Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3. Glycoconj J 2009;26:445-456.
Byrd JC, Bresalier RS. Mucins and mucin binding proteins in colorectal cancer. Cancer Metastasis Rev 2004;23:77-99.
Hernández P, Tetaert D, Vergoten G, et ál. Specificity of Amaranthus leucocarpus syn. hypocondriacus lectin for O-glycopeptides. Biochim Biophys Acta 2004;1674:282-290.
Irazoqui FJ, Vides MA, Nores GA. Structural requirements of carbohydrates to bind Agaricus bisporus lectin. Glycobiology 1999;9:59-64.
Matsushita Y, Cleary KR, Ota DM, Hoff SD, Irimura T. Sialyl-dimeric Lewis-X antigen expressed on mucin-like glycoproteins in colorectal cancer metastases. Lab Invest 1990;63:780-791.
Kim YS, Gum J Jr, Brockhausen I. Mucin glycoproteins in neoplasia. Glycoconj J 1996;13:693-707.
Chakraborty AK, Sousa JF, Chakraborty D, et ál. GnT-V expression and metastatic phenotypes in macrophage-melanoma fusion hybrids is down- regulated by 5-Aza-dC: evidence for methylation sensitive, extragenic regulation of GnT-V transcription. Gene 2006;374:166-173.
Brockhausen I. Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions. EMBO Rep 2006;7:599-604.