Ca2+-CaM activation of AMP deaminase contributes to adenine nucleotide dysregulation and phosphatidylserine externalization in human sickle erythrocytes
| Autor: | Richard L. Sabina, Cheryl A. Hillery, Nancy J. Wandersee |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Inosine monophosphate
Erythrocytes Anemia Sickle Cell Phosphatidylserines Biology Statistics Nonparametric Article AMP Deaminase Pathogenesis chemistry.chemical_compound Adenosine Triphosphate Calmodulin Inosine Monophosphate Adenine nucleotide hemic and lymphatic diseases Humans p-Methoxy-N-methylphenethylamine Cells Cultured Calcium metabolism Adenine Nucleotides Adenine AMP deaminase Hematology Phosphatidylserine Flow Cytometry Molecular biology chemistry Biochemistry Adenosine triphosphate Ex vivo |
| Zdroj: | British Journal of Haematology. 144:434-445 |
| ISSN: | 1365-2141 0007-1048 |
| DOI: | 10.1111/j.1365-2141.2008.07473.x |
| Popis: | Ca2+-calmodulin (Ca2+-CaM) activates erythrocyte adenosine monophosphate deaminase (AMPD) in conditions of disturbed calcium homeostasis, prompting us to investigate adenine nucleotide metabolic dysregulation in sickle cell disease (SCD). However, higher ATP concentrations in reticulocytes, compared to erythrocytes, confound a comparative evaluation of SCD and normal RBCs. Therefore, a combination of centrifugation and antiCD71-labelled magnetic bead selection was used to prepare reticulocyte-poor fractions (reticulocytes |
| Databáze: | OpenAIRE |
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