Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels

• Autores: Navone, N.M.; Polo, C.F.; Frisardi, A.L.; Andrade, N.E.; del C. Baille, a.M.
• Año de publicación: 1990
• Idioma: inglés
• Tipo de recurso: artículo
• Fuente: Int. J. Biochem. 1990;22(12):1407-1411
• Materia: porphobilinogen synthase; porphyrin; article; breast cancer; explant; heme synthesis; histology; human; human cell; priority journal; Adult; Aged; Ammonia-Lyases; Breast; Breast Neoplasms; Female; Heme; Human; Middle Age; Porphobilinogen Synthase; Support, Non-U.S. Gov't; Tissue Culture; Uroporphyrinogen Decarboxylase
• Institución: Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales

1. 1. Porphyrin biosynthesis from 5-aminoevulinic acid (ALA) was investigated using the technique of tissue explant cultures, in both human breast cancer and its original normal tissue. 2. 2. The activity of ALA-dehydratase, porphobilinogenase and uroporphyrinogen decarboxylase was directly determined in both tumor and normal mammary tissues. 3. 3. Porphyrin synthesis capacity of human breast carcinoma was 20-fold enhanced, as compared with normal tissue, at least between the stages of porphobilinogen and coproporphyrinogen formation. 4. 4. The activity of the three enzymes examined was always lower in normal tissue than in tumoral tissue. 5. 5. Present findings show that porphyrin biosynthesis is increased in breast cancer tissue. © 1990.