Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Language
Publication year range
2.
Toxicol Pathol ; 47(8): 1088-1095, 2019 12.
Article in English | MEDLINE | ID: mdl-31554482

ABSTRACT

A wide range of career options is available globally in the environmental toxicologic pathology (ETP) arena including academia, government, contract research organizations, and the agrichemical/chemical industry. This small and specialized subset of toxicologic pathologists addresses the effects of contaminants and pollutants on human, animal, and ecological health (One Health). Veterinary students and pathology trainees are primarily exposed to diagnostic pathology and often have limited exposure to toxicologic pathology and even less so to the issues and opportunities in environmental toxicology. The speakers provided a brief overview of global opportunities in their work sector and personal perspectives of their careers in ETP. The following panel discussion provided an opportunity to discuss issues related to careers in this specialty.


Subject(s)
Career Choice , Ecotoxicology , Pathology , Societies, Scientific , Congresses as Topic , Ecotoxicology/education , Ecotoxicology/trends , Pathology/education , Pathology/trends , Schools, Medical , United States , United States Government Agencies , Universities
3.
J Biol Chem ; 282(6): 4124-35, 2007 Feb 09.
Article in English | MEDLINE | ID: mdl-17142833

ABSTRACT

Dematin and adducin are actin-binding proteins of the erythrocyte "junctional complex." Individually, they exert modest effects on erythrocyte shape and membrane stability, and their homologues are expressed widely in non-erythroid cells. Here we report generation and characterization of double knock-out mice lacking beta-adducin and the headpiece domain of dematin. The combined mutations result in altered erythrocyte morphology, increased membrane instability, and severe hemolysis. Peripheral blood analysis shows evidence of severe hemolytic anemia with reduced number of erythrocytes/hematocrit/hemoglobin and an approximately 12-fold increase in the number of circulating reticulocytes. The presence of a variety of misshapen and fragmented erythrocytes correlates with increased osmotic fragility and reduced in vivo life span. Despite the apparently normal protein composition of the mutant erythrocyte membrane, the retention of the spectrin-actin complex in the membrane under low ionic strength conditions is significantly reduced by the double mutation. Atomic force microscopy reveals an increase in grain size and a decrease in filament number of the mutant membrane cytoskeleton, although the volume parameter is similar to wild type erythrocytes. Aggregated, disassembled, and irregular features are visualized in the mutant membrane, consistent with the presence of large protein aggregates. Importantly, purified dematin binds to the stripped inside-out vesicles in a saturable manner, and dematin-membrane binding is abolished upon pretreatment of membrane vesicles with trypsin. Together, these results reveal an essential role of dematin and adducin in the maintenance of erythrocyte shape and membrane stability, and they suggest that the dematin-membrane interaction could link the junctional complex to the plasma membrane in erythroid cells.


Subject(s)
Actins/metabolism , Anemia, Hemolytic/blood , Blood Proteins/genetics , Calmodulin-Binding Proteins/genetics , Erythrocyte Membrane/pathology , Gene Deletion , Osmotic Fragility/genetics , Phosphoproteins/genetics , Spectrin/metabolism , Actins/physiology , Anemia, Hemolytic/genetics , Animals , Blood Proteins/deficiency , Blood Proteins/metabolism , Blood Proteins/physiology , Calmodulin-Binding Proteins/blood , Calmodulin-Binding Proteins/deficiency , Cytoskeletal Proteins , Disease Models, Animal , Erythrocyte Membrane/metabolism , Erythrocyte Membrane/ultrastructure , Humans , Mice , Mice, Knockout , Microscopy, Atomic Force , Phosphoproteins/deficiency , Phosphoproteins/metabolism , Phosphoproteins/physiology , Spectrin/physiology
SELECTION OF CITATIONS
SEARCH DETAIL
...