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

Mostrar todas las versiones(3)

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 determin...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Navone, N.M., Polo, C.F., Frisardi, A.L., Andrade, N.E., del C. Baille, a.M.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 1990
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n12_p1407_Navone
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

Ejemplares similares