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1.
Ecancermedicalscience ; 13: 893, 2019.
Article in English | MEDLINE | ID: mdl-30792810

ABSTRACT

Breast cancer is the leading cause of cancer death among women worldwide. While triple-negative breast cancer is less common among various sub-types of breast cancer, it tends to affect younger women and is more aggressive, having a higher rate of early recurrence and mortality compared to other sub-types. We know about the association between triple-negative breast cancer and BRCA mutations, which are highly prevalent in founding populations of European origin, but the true prevalence of these mutations in Latin American populations is unknown. There is also very little information about the demographic and epidemiological aspects of triple-negative breast cancer in Latin America, which we will try to summarise in this article. In addition, we will try to provide a brief introduction to the most common recommendations for treating this histological class in Latin America.

2.
Biol Res ; 38(1): 69-82, 2005.
Article in English | MEDLINE | ID: mdl-15977412

ABSTRACT

We have isolated and sequenced the genes encoding the heat shock proteins 60 (Hsp60) and 70 (Hsp70) of the salmon pathogen Piscirickettsia salmonis. The sequence analysis revealed the expected two open reading frames that encode proteins with calculated molecular weights of 60,060 and 70,400. The proteins exhibit a 70-80% homology with other known prokaryotic Hsp60 and Hsp70 sequences. The coding regions have been expressed in E. coli as thioredoxin fusion proteins. Both recombinant proteins were shown to elicit a humoral response when injected intraperitoneally in Atlantic salmon and also conferred protection to fish challenged with P. salmonis. The present data will facilitate further studies on the involvement of heat shock proteins in protective immunity of fish to infection by P. salmonis and their potential use in recombinants vaccines against this intracellular pathogen.


Subject(s)
Chaperonin 60/biosynthesis , DNA, Bacterial/genetics , HSP70 Heat-Shock Proteins/biosynthesis , Piscirickettsiaceae/immunology , Salmon/microbiology , Animals , Antibodies, Bacterial/immunology , Base Sequence , Chaperonin 60/genetics , Chaperonin 60/immunology , Genomic Library , HSP70 Heat-Shock Proteins/genetics , HSP70 Heat-Shock Proteins/immunology , Molecular Sequence Data , Polymerase Chain Reaction , Salmon/immunology
3.
Biol. Res ; 38(1): 69-82, 2005. ilus, graf
Article in English | LILACS | ID: lil-404829

ABSTRACT

We have isolated and sequenced the genes encoding the heat shock proteins 60 (Hsp60) and 70 (Hsp70) of the salmon pathogen Piscirickettsia salmonis. The sequence analysis revealed the expected two open reading frames that encode proteins with calculated molecular weights of 60,060 and 70,400. The proteins exhibit a 70-80 percent homology with other known prokaryotic Hsp60 and Hsp70 sequences. The coding regions have been expressed in E. coli as thioredoxin fusion proteins. Both recombinant proteins were shown to elicit a humoral response when injected intraperitoneally in Atlantic salmon and also conferred protection to fish challenged with P. salmonis. The present data will facilitate further studies on the involvement of heat shock proteins in protective immunity of fish to infection by P. salmonis and their potential use in recombinants vaccines against this intracellular pathogen.


Subject(s)
Animals , /biosynthesis , DNA, Bacterial/genetics , /biosynthesis , Piscirickettsiaceae/immunology , Salmon/microbiology , Antibodies, Bacterial/immunology , Base Sequence , /genetics , Genomic Library , /genetics , Molecular Sequence Data , Polymerase Chain Reaction , Salmon/immunology
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