Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels
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...
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1990
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n12_p1407_Navone http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v22_n12_p1407_Navone_oai |
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I28-R145-paper_0020711X_v22_n12_p1407_Navone_oai2020-10-19 Navone, N.M. Polo, C.F. Frisardi, A.L. Andrade, N.E. del C. Baille, a.M. 1990 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. application/pdf http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n12_p1407_Navone info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Int. J. Biochem. 1990;22(12):1407-1411 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 Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v22_n12_p1407_Navone_oai |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-145 |
| collection |
Repositorio Digital de la Universidad de Buenos Aires (UBA) |
| topic |
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 |
| spellingShingle |
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 Navone, N.M. Polo, C.F. Frisardi, A.L. Andrade, N.E. del C. Baille, a.M. Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels |
| topic_facet |
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 |
| description |
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. |
| format |
Artículo Artículo publishedVersion |
| author |
Navone, N.M. Polo, C.F. Frisardi, A.L. Andrade, N.E. del C. Baille, a.M. |
| author_facet |
Navone, N.M. Polo, C.F. Frisardi, A.L. Andrade, N.E. del C. Baille, a.M. |
| author_sort |
Navone, N.M. |
| title |
Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels |
| title_short |
Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels |
| title_full |
Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels |
| title_fullStr |
Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels |
| title_full_unstemmed |
Heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels |
| title_sort |
heme biosynthesis in human breast cancer-mimetic "in vitro" studies and some heme enzymic activity levels |
| publishDate |
1990 |
| url |
http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n12_p1407_Navone http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v22_n12_p1407_Navone_oai |
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| _version_ |
1766026539608047616 |