ABSTRACT
Introducción: El tejido adiposo blanco (TAB) subcutáneo (Sc) humano podría variar dependiendo de su localización anatómica, con diferencias en su perfil proteómico. Pacientes y métodos: Se obtuvieron aspirados de TAB-Sc de 6 mujeres con IMC > 25kg/m2, a las que se les había realizado una liposucción. Dicho TAB-Sc se obtuvo de 6 localizaciones anatómicas: abdominal superior e inferior, muslo, dorsal, flanco y cadera, analizándose su perfil proteómico mediante electroforesis bidimensional. En muslo y abdomen superior se compararon, además, las muestras obtenidas de las 2 capas del TAB-Sc (profunda y superficial). Resultados: Se detectaron 21 proteínas que mostraban una intensidad de expresión diferente entre las 6 localizaciones anatómicas y 14 entre las capas superficial y profunda de una misma región. Entre las proteínas identificadas se incluyen: vimentina (proteína estructural); proteínas heat shock (HSP), superóxido-dismutasa (estrés/chaperoninas); proteína fijadora de ácidos grasos 4 (FABP-4) y alfa-enolasa (metabolismo lipídico y de los hidratos de carbono, respectivamente) y ATP-sintetasa (producción de energía). Entre las regiones estudiadas, el TAB-Sc dorsal mostraba un perfil proteómico particular, con menor expresión de proteínas implicadas en la producción de energía y metabolismo (ATP-sintetasa, alfa-enolasa, HSP y FABP-4) que el resto de regiones. Conclusiones: Los niveles de expresión de diversas proteínas en el TAB-Sc humano no son homogéneos, difiriendo entre localizaciones anatómicas. Esto señala la existencia de diferencias funcionales en el TAB-Sc de acuerdo con su localización anatómica, lo que debe considerarse antes de asumir la extrapolación de los datos derivados del TAB-Sc de una determinada localización al de otras partes de la anatomía(AU)
Background: Human subcutaneous (SQ) white adipose tissue (WAT) can vary according to its anatomical location, with subsequent differences in its proteomic profile. Patients and methods: SQ-WAT aspirates were obtained from six overweight (BMI >25kg/m2) women who underwent extensive liposuction. SQ-WAT was removed from six different locations (upper abdominal, lower abdominal, thigh, back, flank, and hip), and the protein profiles were determined by two-dimensional gel electrophoresis. In addition, the proteomic profiles of upper abdominal and hip SQ-WAT were subjected to further analysis, comparing samples obtained from two layers of WAT (deep and superficial). Results: Twenty one protein spots showed differential intensities among the six defined anatomical locations, and 14 between the superficial and the deep layer. Among the proteins identified were, vimentin (structural protein), heat-shock proteins (HSPs), superoxide-dismutase (stress-resistance/chaperones), fatty-acid-binding protein (FABP) 4, and alpha-enolase (lipid and carbohydrate metabolism), and ATP-synthase (energy production). Among the WAT samples analyzed, the back sub-depot showed significant differences in the levels of selected proteins when compared to the other locations, with lower level of expression of several proteins involved in energy production and metabolism (ATP-synthase, alpha-enolase, HSPs and FABP-4). Conclusions: The levels of several proteins in human SQ-WAT are not homogeneous between different WAT depots. These changes suggest the existence of inherent functional differences in subcutaneous fat depending upon its anatomical location. Thus, caution must be used when extrapolating data from one subcutaneous WAT region to other depots(AU)
Subject(s)
Humans , Female , Proteome/analysis , Adipose Tissue/ultrastructure , Electrophoresis, Gel, Two-Dimensional/methods , Adipose Tissue, White/anatomy & histology , Subcutaneous Fat/anatomy & histology , LipectomyABSTRACT
BACKGROUND: Human subcutaneous (SQ) white adipose tissue (WAT) can vary according to its anatomical location, with subsequent differences in its proteomic profile. PATIENTS AND METHODS: SQ-WAT aspirates were obtained from six overweight (BMI>25kg/m(2)) women who underwent extensive liposuction. SQ-WAT was removed from six different locations (upper abdominal, lower abdominal, thigh, back, flank, and hip), and the protein profiles were determined by two-dimensional gel electrophoresis. In addition, the proteomic profiles of upper abdominal and hip SQ-WAT were subjected to further analysis, comparing samples obtained from two layers of WAT (deep and superficial). RESULTS: Twenty one protein spots showed differential intensities among the six defined anatomical locations, and 14 between the superficial and the deep layer. Among the proteins identified were, vimentin (structural protein), heat-shock proteins (HSPs), superoxide-dismutase (stress-resistance/chaperones), fatty-acid-binding protein (FABP) 4, and alpha-enolase (lipid and carbohydrate metabolism), and ATP-synthase (energy production). Among the WAT samples analyzed, the back sub-depot showed significant differences in the levels of selected proteins when compared to the other locations, with lower level of expression of several proteins involved in energy production and metabolism (ATP-synthase, alpha-enolase, HSPs and FABP-4). CONCLUSIONS: The levels of several proteins in human SQ-WAT are not homogeneous between different WAT depots. These changes suggest the existence of inherent functional differences in subcutaneous fat depending upon its anatomical location. Thus, caution must be used when extrapolating data from one subcutaneous WAT region to other depots.
Subject(s)
Proteome , Subcutaneous Fat/anatomy & histology , Female , Humans , Subcutaneous Fat/chemistryABSTRACT
Technology surrounding genomics, or the study of an organism's genome and its gene use, has advanced rapidly resulting in an abundance of readily available genomic data. Although genomics is extremely valuable, proteins are ultimately responsible for controlling most aspects of cellular function. The field of proteomics, or the study of the full array of proteins produced by an organism, has become the premier arena for the identification and characterization of proteins. Yet the task of characterizing a proteomic profile is more complex, in part because many unique proteins can be produced by the same gene product and because proteins have more diverse chemical structures making sequencing and identification more difficult. Proteomic profiles of a particular organism, tissue or cell are influenced by a variety of environmental stimuli, including those brought on by infectious disease. The intent of this review is to highlight applications of proteomics used in the study of pathogenesis, etiology and pathology of infectious disorders. While many infectious agents have been the target of proteomic studies, this review will focus on those infectious diseases which rank among the highest in worldwide mortalities, such as HIV/AIDS, tuberculosis, malaria, measles, and hepatitis.
