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1.
Int J Mol Sci ; 24(22)2023 Nov 15.
Article in English | MEDLINE | ID: mdl-38003516

ABSTRACT

Interleukin-33 (IL-33), a member of the interleukin-1(IL-1) family of cytokines, remains poorly understood in the context of human breast cancer and its impact on treatment outcomes. This study aimed to elucidate IL-33 expression patterns within tumor samples from a cohort of Brazilian female breast cancer patients undergoing neoadjuvant chemotherapy while exploring its correlation with clinicopathological markers. In total, 68 samples were meticulously evaluated, with IL-33 expression quantified through a quantitative polymerase chain reaction. The findings revealed a substantial upregulation of IL-33 expression in breast cancer patient samples, specifically within the Triple-negative and Luminal A and B subtypes, when compared to controls (healthy breast tissues). Notably, the Luminal B subtype displayed a marked elevation in IL-33 expression relative to the Luminal A subtype (p < 0.05). Moreover, a progressive surge in IL-33 expression was discerned among Luminal subtype patients with TNM 4 staging criteria, further underscoring its significance (p < 0.005). Furthermore, chemotherapy-naïve patients of Luminal A and B subtypes exhibited heightened IL-33 expression (p < 0.05). Collectively, our findings propose that chemotherapy could potentially mitigate tumor aggressiveness by suppressing IL-33 expression in breast cancer, thus warranting consideration as a prognostic marker for gauging chemotherapy response and predicting disease progression in Luminal subtype patients. This study not only sheds light on the intricate roles of IL-33 in breast cancer but also offers valuable insights for future IL-33-related research endeavors within this context.


Subject(s)
Breast Neoplasms , Humans , Female , Breast Neoplasms/metabolism , Interleukin-33/genetics , Interleukin-33/therapeutic use , Neoadjuvant Therapy , Brazil , Treatment Outcome , Biomarkers, Tumor , Antineoplastic Combined Chemotherapy Protocols/therapeutic use , Receptor, ErbB-2/metabolism
2.
J Sci Food Agric ; 96(13): 4337-44, 2016 Oct.
Article in English | MEDLINE | ID: mdl-26801736

ABSTRACT

BACKGROUND: Artisanal 'Coalho' cheese is a product typically popular in the Brazilian north-eastern region. Production of this cheese represents about 9.2% of the internal crude product of Pernambuco State. Several peptides are generated from hydrolysis of αS1 -, αS2 -, ß-, and κ-caseins during manufacture of this cheese. The commercial importance of Brazilian artisanal 'Coalho' cheese justifies the examination of both the protein and peptide profiles of cheeses from six cities of the semi-arid region of Pernambuco State, Brazil. RESULTS: SDS-PAGE of the aqueous extracts of 'Coalho' cheeses (WSP) showed bands of lactoferrin, ß-lactoglobulin, ß-lactoglobulin (dimer), α-lactoalbumin, bovine serum albumin, α-casein, ß-casein, κ-casein and para-κ-casein. A total of 57 to 72 peptides were confirmed by mass spectra in the different samples of 'Coalho' cheese which 32 known peptides (11 from αS1 -casein, three from αS2 -casein, 15 from ß-casein and three from κ-casein), comprising seven caseinphosphopeptides. Among the unidentified peptides, three showed high intensity peaks in all 'Coalho' cheeses studied (with molecular weights of 1597, 1725/1726, 2778/2779 Da). CONCLUSION: The proteomic studies revealed peptides that may represent molecular markers or fingerprints for investigating the quality control and regional characterisation of these 'Coalho' cheeses. © 2016 Society of Chemical Industry.


Subject(s)
Cheese/analysis , Diet , Food Quality , Milk Proteins/analysis , Peptide Fragments/analysis , Animals , Biomarkers/analysis , Brazil , Cattle , Desert Climate , Diet/ethnology , Food Inspection/methods , Humans , Milk Proteins/chemistry , Milk Proteins/metabolism , Molecular Weight , Oligopeptides/analysis , Oligopeptides/chemistry , Oligopeptides/metabolism , Peptide Fragments/chemistry , Peptide Fragments/metabolism , Peptide Mapping , Phosphoproteins/analysis , Phosphoproteins/chemistry , Phosphoproteins/metabolism , Proteolysis , Proteomics/methods , Solubility , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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