Activity of AMP-Regulated Protein Kinase and AMP-Deaminase in the Heart of Mice Fed High-Fat Diet
Autor: | Pawel Romaszko, Paulina Żukowska, Marcin Lipiński, Ryszard T. Smolenski, Ewa M. Slominska, Iwona Rybakowska |
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Rok vydání: | 2014 |
Předmět: |
Blood Glucose
Male medicine.medical_specialty Energy metabolism Peptide Diet High-Fat Biochemistry AMP Deaminase Mice Internal medicine Genetics medicine Animals Protein kinase A chemistry.chemical_classification Chemistry Activator (genetics) Myocardium Adenylate Kinase Body Weight AMPK Heart AMP deaminase High fat diet General Medicine Endocrinology AMPK activity Molecular Medicine |
Zdroj: | Nucleosides, Nucleotides and Nucleic Acids. 33:347-352 |
ISSN: | 1532-2335 1525-7770 |
DOI: | 10.1080/15257770.2014.880480 |
Popis: | AMP-regulated protein kinase (AMPK) is involved in numerous regulatory processes and its role in control of cardiac energy metabolism is particularly important. This activity could be affected by AMP-deaminase (AMPD) since substrate of AMPD is AMPK activator. Hearts of male mouse, fed for six weeks with normal or high-fat diet, were fractionated to enrich AMPK activity. Purified fraction was incubated with AMARA peptide for up to 5 minutes and then conversion of AMARA to pAMARA was determined by liquid chromatography-mass spectrometry (LC/MS) using mass detector. Activity of AMPK in heart was 0.038±0.012 pmol/min/mg protein for mice fed high-fat diet and that was not different to control (0.032±0.01 pmol/min/mg protein). We observed change in AMPD activity. It was 5.39±1.5 nmol/mg tissue/min in heart of mice fed high-fat diet while in heart of mice fed low-fat diet it was 2.29±0.32 nmol/mg tissue/min. Data we present indicate that while total AMPK activity is not changed decrease in AMPD activity may affect AMPK signaling in diabetic heart. |
Databáze: | OpenAIRE |
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