Search for biomarkers from peptides expressed in breast cancer biopsies


Carlos Muza Briseño1, William Haskins3, Guillermo Cazares Urbina4, Raúl Rodríguez Herrera2, Madeleine Zaehringer4, Alejandro Zugasti Cruz2, Jesús Antonio Morlett Chávez1,2,5

1 Departamento de Análisis Clínicos y Diagnóstico Molecular.
2 Laboratorio de Biología Molecular, Departamento de Investigación en Alimentos, Facultad de Ciencias Químicas. Universidad Autónoma de Coahuila, Boulevard. Venustiano Carranza esquina con José Cárdenas. República. CP 25280, Saltillo, Coahuila, México
3 RCMI Proteomics & Protein Biomarkers Cores, Dept. of Biology-BSE 3.108A. One UTSA Circle, University of Texas at San Antonio. San Antonio, Texas
4 Centro Médico Universidad. Ave Universidad 768 altos, Col. Los Maestros, CP 25160. Saltillo, Coahuila, México.
5 Depto. de Laboratorio Clínico, Hospital General de Zona con Medicina Familiar No.2, Instituto Mexicano del Seguro Social, Blvd. Venustiano Carranza y Humberto Hinojosa s/n. Col., Kiosco. CP 2520. Saltillo Coahuila.

Breast cancer (BC) is one of the leading causes of death in Mexico. Moreover, BC is the main cause of death in women between 15-29 years old in northern Mexico. Proteomic techniques have been used in order to achieve a better understanding of the genes involved in the development of BC. The proteins in BC extracted from 50 fresh breast cancer tissues (FBCT), 50 paraffin embedded breast cancer tissues (PEBCT) and 10 biopsies from women suspected of cancer (SC), residing in Coahuila, Mexico were analyzed in this paper. The quantity of protein extracted was similar in both samples FBCT and PEBCT. However, protein quality was lower in PEBCT than FBCT. Subsequently, these proteins were resolved in SDS-PAGE and 2DE. Differences were noticed in protein profile and all those suspect proteins were analyzed by LC/MS/MS. Amino acidic fingerprint allowed for the identification of peptides associated with a) cell migration, b) tumor suppression, c) oxidative stress or heat shock.

19 ART 2017 copia