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Correction to: Clin Transl Oncol https://doi.org/10.1007/s12094-017-1801-4.
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The increased incidence and decreased mortality of breast cancer have produced an increased number of breast cancer survivors. The type of sequelae and comorbidities that these patients present call for a collaborative follow-up by hospital-based specialized care and primary care. In this document, we present a guideline drafted and agreed among scientific societies whose members care for breast cancer survivors. The purpose of this guideline is to achieve the shared and coordinated follow-up of these patients by specialized care and primary care professionals. In it, we review the health issues derived from the treatments performed, with recommendations about the therapeutic approach to each of them, as well as a proposal for joint follow-up by primary and specialized care.
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Assistência ao Convalescente , Neoplasias da Mama/terapia , Sobreviventes de Câncer , Guias de Prática Clínica como Assunto/normas , Sociedades Médicas , Feminino , Humanos , EspanhaRESUMO
Breast cancer is a burden for western societies, and an increasing one in emerging economies, because of its high incidence and enormous psychological, social, sanitary and economic costs. However, breast cancer is a preventable disease in a significant proportion. Recent developments in the armamentarium of effective drugs for breast cancer prevention (namely exemestane and anastrozole), the new recommendation from the National Institute for Health and Care Excellence to use preventative drugs in women at high risk as well as updated Guidelines from the US Preventive Services Task Force and the American Society of Clinical Oncology should give renewed momentum to the pharmacological prevention of breast cancer. In this article we review recent major developments in the field and examine their ongoing repercussion for breast cancer prevention. As a practical example, the potential impact of preventive measures in Spain is evaluated and a course of practical actions is delineated.
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Neoplasias da Mama/prevenção & controle , Antineoplásicos Hormonais/uso terapêutico , Proteína BRCA1/genética , Neoplasias da Mama/genética , Feminino , Humanos , Tamoxifeno/uso terapêuticoRESUMO
OBJECTIVE: The aim of this study is to evaluate if it is necessary to remove all the radioactive sentinel lymph nodes (SLNs) not seen on lymphoscintigraphy in order to accurately stage breast cancer patients. MATERIAL AND METHODS: From March 1999 to March 2006, SLN biopsy was performed in 461 patients. All patients were only injected with radioisotope. Lymphoscintigraphy was performed in all the patients. The mean number of SLNs removed was 2.1 (range 1-15). RESULTS: The SLN was positive in 133 patients (28.8%). Lymphoscintigraphy accurately predicted the number of SLNs identified intraoperatively in 243 patients (52.7%). In 175 patients (37.9%) there were more SLNs identified intraoperatively than were seen on lymphos cintigraphy. In 11 (6.2%) of these 175 patients, additional SLNs identified intraoperatively harboured metastasis. Type of injection, need for a second injection, tumour location and age were not identified as statistically significantly associated with additional positive SLNs identified intraoperatively and not seen on lymphoscintigraphy. CONCLUSIONS: Lymphoscintigraphy does not accurately predict the number of SLNs identified intraoperatively, this number being underestimated. Surgeons should remove all radioactive SLNs to improve the detection of positive SLNs.
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Neoplasias da Mama/patologia , Neoplasias da Mama/cirurgia , Metástase Linfática/diagnóstico , Biópsia de Linfonodo Sentinela/métodos , Feminino , Humanos , CintilografiaRESUMO
Three fatty acid-binding proteins (FABPs) from the liver of the shark Halaetunus bivius were isolated and characterized: one of them belongs to the liver-type FABP family and the other two to the heart-type FABP family. The complete primary structure of the first FABP, and partial primary structures of the two others, were determined. The liver-type FABP constitutes 69% of the total FABPs, and its amino acid sequence presents the highest identity with chicken, catfish, iguana and elephant fish liver basic FABPs. The L-FABP protein has low affinity for palmitic and oleic acids and high affinity for linoleic and arachidonic acids and other hydrophobic ligands, all of them important for the metabolic functions of the liver. In contrast, both heart-type FABPs have the highest affinity for palmitic acid, the principal fatty acid mobilized from fat deposits for beta-oxidation.
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Proteínas de Transporte/química , Fígado/metabolismo , Proteína P2 de Mielina/química , Proteínas de Neoplasias , Tubarões/metabolismo , Sequência de Aminoácidos , Animais , Ligação Competitiva , Proteínas de Transporte/isolamento & purificação , Proteínas de Ligação a Ácido Graxo , Ácidos Graxos/metabolismo , Ácidos Graxos Insaturados/metabolismo , Dados de Sequência Molecular , Proteína P2 de Mielina/isolamento & purificação , Miocárdio/metabolismo , Fragmentos de Peptídeos/química , Isoformas de Proteínas , Alinhamento de Sequência , Análise de Sequência , TripsinaRESUMO
A fatty acid-binding protein from the cytosolic fraction of the armadillo Chaetophractus villosus Harderian gland was purified to homogeneity by a procedure based on gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The protein has an apparent molecular mass of 14 kDa. N-terminal sequence analysis showed that the protein has a blocked N-terminus. For internal amino acid sequencing, the protein was digested in-gel and the resulting peptides were fractionated by reverse-phase high performance liquid chromatography and subjected to automated Edman degradation. Partial amino acid sequencing suggests that it belongs to the heart type. Moreover, it cross-reacted with anti-serum to rat heart fatty acid-binding protein but not with rat intestinal and liver anti-sera. A very slow cross-reaction was also found with anti-serum to rat ALBP. This is the first time that a fatty acid-binding protein has been reported in a Harderian gland.
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Proteínas de Transporte/isolamento & purificação , Proteínas de Transporte/metabolismo , Glândula de Harder/metabolismo , Proteína P2 de Mielina/isolamento & purificação , Proteína P2 de Mielina/metabolismo , Proteínas de Neoplasias , Proteínas do Tecido Nervoso , Sequência de Aminoácidos , Animais , Tatus , Proteínas de Transporte/genética , Cromatografia Líquida de Alta Pressão , Proteína 7 de Ligação a Ácidos Graxos , Proteínas de Ligação a Ácido Graxo , Dados de Sequência Molecular , Proteína P2 de Mielina/genética , Ratos , Alinhamento de SequênciaRESUMO
Five fatty-acid-binding proteins from the liver of the elephant fish (Callorhynchus callorhynchus), a chimaera fish that belongs--together with the elasmobranchs--to the ancient chondrichthyes class were isolated and characterized. The purification procedures for these proteins involved gel filtration, anion-exchange chromatography, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a last step. They were submitted to "in gel" tryptic or cyanogen bromide digestion and the resulting peptides were separated by high performance liquid chromatography and then sequenced by Edman degradation. According to their partial amino acid sequences, one of them presents the highest identity with fatty-acid-binding proteins from human and catfish liver, another three with those from mammalian heart or adipose tissue and the fifth with the mammalian intestinal fatty-acid-binding protein. The presence of various members of this protein family, as now found in elephant fish and previously in catfish (Rhamdia sapo) liver, does not occur in mammalian liver which express only one a characteristic fatty-acid-binding protein.
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Adipócitos/química , Proteínas de Transporte/análise , Peixes/metabolismo , Intestinos/química , Fígado/química , Proteína P2 de Mielina/análise , Miocárdio/química , Proteínas de Neoplasias , Proteínas do Tecido Nervoso , Proteínas Supressoras de Tumor , Sequência de Aminoácidos , Animais , Western Blotting , Peixes-Gato/metabolismo , Cromatografia por Troca Iônica , Proteína 7 de Ligação a Ácidos Graxos , Proteínas de Ligação a Ácido Graxo , Humanos , Soros Imunes , Dados de Sequência Molecular , Peso Molecular , RatosRESUMO
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is a powerful purification technique in protein chemistry research. This procedure is frequently used as a last step in protein purification for sequencing. For proteins which are N-terminal blocked, 'in gel' digestion offers a useful approach for the generation of internal sequence data from proteins purified by SDS-PAGE. In this study, we propose a procedure where proteins purified by this method are chemically cleaved 'in gel' by using CNBr and the resulting peptides are isolated in a second SDS-PAGE. After that, electroblotting is performed onto PVDF membranes and the electroblotted and Coomassie-stained peptide, from each band is then sequenced by Edman degradation. Proteins often have a small number of methionines whose cleavage allows the obtention of long peptides suitable to sequence a good deal of residues. Three standard proteins of different molecular mass have been assayed by this procedure and the 'in situ' cleavage profile compared with direct chemical digestion in a protein solution.
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Eletroforese em Gel de Poliacrilamida/métodos , Proteínas/química , Análise de Sequência/métodos , Sequência de Aminoácidos , Western Blotting , Brometo de Cianogênio , Dodecilsulfato de SódioRESUMO
The fatty acid-binding protein (FABP) from armadillo liver was purified to homogeneity by a procedure involving gel filtration and two anion exchange chromatography steps. The purified protein proved to have a pI between 5.0 and 5.2 and migrated by sodium dodecyl sulfate-polyacrilamyde gel electrophoresis as a single entity of approximately 14 kDa. The armadillo FABP cross-reacted with antiserum against rat liver FABP but not against rat intestinal FABP. The same as other members of the family, it has a blocked N-terminus. Amino acid sequencing of peptides obtained by cyanogen bromide cleavage and in-gel tryptic digestion shows that the armadillo, despite being one of the less evolved mammals, has a liver FABP of the same type as that of highly evolved mammals.
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Tatus/metabolismo , Proteínas de Transporte/isolamento & purificação , Ácidos Graxos/metabolismo , Fígado/metabolismo , Proteína P2 de Mielina/isolamento & purificação , Proteínas de Neoplasias , Proteínas do Tecido Nervoso , Proteínas Supressoras de Tumor , Sequência de Aminoácidos , Aminoácidos/análise , Animais , Tatus/genética , Proteínas de Transporte/química , Proteínas de Transporte/genética , Reações Cruzadas , Citosol/metabolismo , Evolução Molecular , Proteína 7 de Ligação a Ácidos Graxos , Proteínas de Ligação a Ácido Graxo , Humanos , Imunoquímica , Ponto Isoelétrico , Dados de Sequência Molecular , Peso Molecular , Proteína P2 de Mielina/química , Proteína P2 de Mielina/genética , Filogenia , Ratos , Homologia de Sequência de AminoácidosRESUMO
The intracellular lipid-binding proteins are a group of homologous proteins which bind and facilitate the transport of fatty acids, bile acids and retinoids. The evolutionary relationship of 51 family members from vertebrates and invertebrates was analyzed. The inferred phylogeny implies the occurrence of at least 14 gene duplications and contains five regions where the branching order is statistically non-significant--this uncertainty explaining most inconsistencies between previous phylogenetic analyses. The phylogeny also suggests that the intestinal fatty acid-binding protein and the liver fatty acid-binding protein/ileal lipid-binding protein subfamilies diverged from the other subfamilies before the vertebrate-invertebrate split. Finally, results presented herein indicate that the putative fatty acid-binding domain of NMDA receptor 1 is unlikely to be a member of this family.