RESUMEN
RATIONALE: The ecological application of stable isotope analysis (SIA) relies on taxa- and tissue-specific stable carbon (Δ13 C) and nitrogen (Δ15 N) isotope discrimination factors, determined with captive animals reared on known diets for sufficient time to reflect dietary isotope ratios. However, captive studies often prohibit lethal sampling, are difficult with endangered species, and reflect conditions not experienced in the wild. METHODS: We overcame these constraints and determined the Δ13 C and Δ15 N values for skin and cortical bone from green sea turtles (Chelonia mydas) that died in captivity and evaluated the utility of a mathematical approach to predict discrimination factors. Using stable carbon (δ13 C values) and nitrogen (δ15 N values) isotope ratios from captive and wild turtles, we established relationships between bone stable isotope (SI) ratios and those from skin, a non-lethally sampled tissue, to facilitate comparisons of SI ratios among studies using multiple tissues. RESULTS: The mean (±SD) Δ13 C and Δ15 N values () between skin and bone from captive turtles and their diet (non-lipid-extracted) were 2.3 ± 0.3 and 4.1 ± 0.4 and 2.1 ± 0.6 and 5.1 ± 1.1, respectively. The mathematically predicted Δ13 C and Δ15 N values were similar (to within 1) to the experimentally derived values. The mean δ15 N values from bone were higher than those from skin for captive (+1.0 ± 0.9) and wild (+0.8 ± 1.0) turtles; the mean δ13 C values from bone were lower than those from skin for wild turtles (-0.6 ± 0.9), but the same as for captive turtles. We used linear regression equations to describe bone vs skin relationships and create bone-to-skin isotope conversion equations. CONCLUSIONS: For sea turtles, we provide the first (a) bone-diet SI discrimination factors, (b) comparison of SI ratios from individual-specific bone and skin, and (c) evaluation of the application of a mathematical approach to predict stable isotope discrimination factors. Our approach opens the door for future studies comparing different tissues, and relating SI ratios of captive to wild animals.
Asunto(s)
Animales Salvajes/fisiología , Animales de Zoológico/fisiología , Huesos/química , Piel/química , Tortugas/fisiología , Animales , Isótopos de Carbono/análisis , Modelos Lineales , Masculino , Espectrometría de Masas , México , Isótopos de Nitrógeno/análisis , Océano PacíficoRESUMEN
Tumor MUC1 expression as well as levels of MUC1, MUC1 circulating immune complexes (MUC1-CIC) and free antibodies against MUC1 (IgG and IgM-MUC1) were evaluated in 70 breast cancer patients with different stages of disease. Controls included: 135 serum samples from healthy women, normal mammary tissue samples (n = 7) and benign breast disease specimens (n = 6). In all assays, pre- and post-vaccination serum samples from breast cancer patients belonging to a vaccination protocol developed at the Memorial Sloan Kettering Cancer Center (New York, USA) were included as controls. Serum MUC1 was measured through Cancer Associated Serum Antigen test and CA15-3 test. Employing ELISA, MUC1-CIC-IgG/M were measured with either C595 or SM3 monoclonal antibodies (MAb) as catchers and also free antibodies against MUC1 (IgG and IgM) using 100mer peptide as catcher. Employing multivariate statistical analysis, results were correlated with age, tumor type, stage of disease and grade of differentiation. By quantitative immunohistochemistry using three anti-MUC1 core protein MAbs (C595, HMFG2 and SM3), tumor MUC1 was detected in 60/70 (86%) breast cancer specimens which reacted with at least one of these MAbs. High MUCI serum levels were detected in 14/67 (21%); IgG and IgM anti-MUC1 antibodies were found elevated in 32 and 14%, respectively, while IgG-MUC1-CIC-measured with C595 in 42% and IgM-MUC1-CIC in 54%; finally, SM3 was positive in 43 and 18%, respectively. Results of these studies demonstrate that in a group of breast cancer patients, MUC1 was detected both in tissue specimens as well as free in serum samples; furthermore, MUC1 can also circulate complexed with IgG and IgM antibodies; thus an accurate measurement should include free and complexed forms. On the other hand, immunohistochemical studies on breast cancer tissues may contribute to reveal different MUC1 glycoforms.