
Florentina Negoita
Visiting research fellow

Aquaglyceroporins and orthodox aquaporins in human adipocytes
Author
Summary, in English
Aquaporins play a crucial role in water homeostasis in the human body, and recently the physiological importance of aquaporins as glycerol channels have been demonstrated. The aquaglyceroporins (AQP3, AQP7, AQP9 and AQP10) represent key glycerol channels, enabling glycerol flux across the membranes of cells. Adipocytes are the major source of glycerol and during lipolysis, glycerol is released to be metabolized by other tissues through a well-orchestrated process. Here we show that both AQP3 and AQP7 bind to the lipid droplet protein perilipin 1 (PLIN1), suggesting that PLIN1 is involved in the coordination of the subcellular translocation of aquaglyceroporins in human adipocytes. Moreover, in addition to aquaglyceroporins, we discovered by transcriptome sequencing that AQP1 is expressed in human primary adipocytes. AQP1 is mainly a water channel and thus is thought to be involved in the response to hyper-osmotic stress by efflux of water during hyperglycemia. Thus, this data suggests a contribution of both orthodox aquaporin and aquaglyceroporin in human adipocytes to maintain the homeostasis of glycerol and water during fasting and feeding.
Department/s
- EXODIAB: Excellence of Diabetes Research in Sweden
- Medical Structural Biology
- Genetic chaos in aggressive cancer
- Division of Clinical Genetics
- The pathogenetic mechanisms behind MLL-rearranged acute leukemia in infancy
- Protein Phosphorylation
- Membrane Protein Structural Biology
Publishing year
2022-02-01
Language
English
Publication/Series
Biochimica et Biophysica Acta - Biomembranes
Volume
1864
Issue
1
Document type
Journal article
Publisher
Elsevier
Topic
- Biochemistry and Molecular Biology
Keywords
- AQP
- Aquaglyceroporins
- Human adipocytes
- Orthodox aquaporins
- Perilipin 1
Status
Published
Research group
- Medical Structural Biology
- Genetic chaos in aggressive cancer
- The pathogenetic mechanisms behind MLL-rearranged acute leukemia in infancy
- Protein Phosphorylation
- Membrane Protein Structural Biology
ISBN/ISSN/Other
- ISSN: 0005-2736