An electron microscopic and biochemical study of the effects of glucagon on glycogen autophagy in the liver and heart of newborn rats
| dc.contributor.author | Kondomerkos, D. J. | en |
| dc.contributor.author | Kalamidas, S. A. | en |
| dc.contributor.author | Kotoulas, O. B. | en |
| dc.date.accessioned | 2015-11-24T19:36:38Z | |
| dc.date.available | 2015-11-24T19:36:38Z | |
| dc.identifier.issn | 1059-910X | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/23915 | |
| dc.rights | Default Licence | - |
| dc.subject | Animals | en |
| dc.subject | Animals, Newborn | en |
| dc.subject | Autophagy/*drug effects | en |
| dc.subject | Glucagon/*pharmacology | en |
| dc.subject | Glucosidases/metabolism | en |
| dc.subject | Glycogen/*metabolism | en |
| dc.subject | Heart/drug effects/physiology | en |
| dc.subject | Hepatocytes/drug effects/metabolism/ultrastructure | en |
| dc.subject | Liver/drug effects/*metabolism/ultrastructure | en |
| dc.subject | Maltose/metabolism | en |
| dc.subject | Microscopy, Electron | en |
| dc.subject | Myocardium/*metabolism/ultrastructure | en |
| dc.subject | Protein Synthesis Inhibitors/*pharmacology | en |
| dc.subject | Rats | en |
| dc.subject | Time Factors | en |
| dc.title | An electron microscopic and biochemical study of the effects of glucagon on glycogen autophagy in the liver and heart of newborn rats | en |
| heal.abstract | The effects of glucagon on the ultrastructural appearance and acid glucosidase activities in the liver and heart of newborn rats were studied. Liver or heart glycogen-hydrolyzing activity of acid glucosidase increased 3 hours after birth and gradually decreased from 3 to 9 hours. Maltose-hydrolyzing activity of acid glucosidase also rose 3 hours after birth, maintained a plateau between 3 and 6 hours, and fell at 9 hours. The administration of glucagon increased autophagic activity in the hepatocytes at the age of 6 hours. Glycogen inside the autophagic vacuoles was decreased, apparently due to the increased glycogen degradation. Glycogen-hydrolyzing activity was elevated in both the liver and the heart. Maltose-hydrolyzing activity was elevated in the liver, but not in the heart. The results of this study suggest that the glycogen-hydrolyzing and maltose-hydrolyzing activities of acid glucosidase are due to different enzymes. Glucagon's effect on the glycogen-hydrolyzing acid glucosidase activity and autophagosomal morphology is similar in both the liver and the heart. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | 10.1002/jemt.20000 | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/14722905 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/jemt.20000/asset/20000_ftp.pdf?v=1&t=h1ym2otu&s=baa2c067da9c06303add4a48b0b7fd11905f3150 | - |
| heal.journalName | Microsc Res Tech | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2004 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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