Fluid shear stress induces a shift from glycolytic to amino acid pathway in human trophoblasts.

Fluidic shear stress Placenta development Trophoblast metabolism

Journal

Cell & bioscience
ISSN: 2045-3701
Titre abrégé: Cell Biosci
Pays: England
ID NLM: 101561195

Informations de publication

Date de publication:
08 Sep 2023
Historique:
received: 16 01 2023
accepted: 28 08 2023
medline: 9 9 2023
pubmed: 9 9 2023
entrez: 8 9 2023
Statut: epublish

Résumé

The human placenta, a tissue with a lifespan limited to the period of pregnancy, is exposed to varying shear rates by maternal blood perfusion depending on the stage of development. In this study, we aimed to investigate the effects of fluidic shear stress on the human trophoblast transcriptome and metabolism. Based on a trophoblast cell line cultured in a fluidic flow system, changes caused by shear stress were analyzed and compared to static conditions. RNA sequencing and bioinformatics analysis revealed an altered transcriptome and enriched gene ontology terms associated with amino acid and mitochondrial metabolism. A decreased GLUT1 expression and reduced glucose uptake, together with downregulated expression of key glycolytic rate-limiting enzymes, hexokinase 2 and phosphofructokinase 1 was observed. Altered mitochondrial ATP levels and mass spectrometry data, suggested a shift in energy production from glycolysis towards mitochondrial oxidative phosphorylation. This shift in energy production could be supported by increased expression of glutamic-oxaloacetic transaminase variants in response to shear stress as well as under low glucose availability or after silencing of GLUT1. The shift towards amino acid metabolic pathways could be supported by significantly altered amino acid levels, like glutamic acid, cysteine and serine. Downregulation of GLUT1 and glycolytic rate-limiting enzymes, with concomitant upregulation of glutamic-oxaloacetic transaminase 2 was confirmed in first trimester placental explants cultured under fluidic flow. In contrast, high fluid shear stress decreased glutamic-oxaloacetic transaminase 2 expression in term placental explants when compared to low flow rates. Placental tissue from pregnancies with intrauterine growth restriction are exposed to high shear rates and showed also decreased glutamic-oxaloacetic transaminase 2, while GLUT1 was unchanged and glycolytic rate-limiting enzymes showed a trend to be upregulated. The results were generated by using qPCR, immunoblots, quantification of immunofluorescent pictures, padlock probe hybridization, mass spectrometry and FRET-based measurement. Our study suggests that onset of uteroplacental blood flow is accompanied by a shift from a predominant glycolytic- to an alternative amino acid converting metabolism in the villous trophoblast. Rheological changes with excessive fluidic shear stress at the placental surface, may disrupt this alternative amino acid pathway in the syncytiotrophoblast and could contribute to intrauterine growth restriction.

Sections du résumé

BACKGROUND BACKGROUND
The human placenta, a tissue with a lifespan limited to the period of pregnancy, is exposed to varying shear rates by maternal blood perfusion depending on the stage of development. In this study, we aimed to investigate the effects of fluidic shear stress on the human trophoblast transcriptome and metabolism.
RESULTS RESULTS
Based on a trophoblast cell line cultured in a fluidic flow system, changes caused by shear stress were analyzed and compared to static conditions. RNA sequencing and bioinformatics analysis revealed an altered transcriptome and enriched gene ontology terms associated with amino acid and mitochondrial metabolism. A decreased GLUT1 expression and reduced glucose uptake, together with downregulated expression of key glycolytic rate-limiting enzymes, hexokinase 2 and phosphofructokinase 1 was observed. Altered mitochondrial ATP levels and mass spectrometry data, suggested a shift in energy production from glycolysis towards mitochondrial oxidative phosphorylation. This shift in energy production could be supported by increased expression of glutamic-oxaloacetic transaminase variants in response to shear stress as well as under low glucose availability or after silencing of GLUT1. The shift towards amino acid metabolic pathways could be supported by significantly altered amino acid levels, like glutamic acid, cysteine and serine. Downregulation of GLUT1 and glycolytic rate-limiting enzymes, with concomitant upregulation of glutamic-oxaloacetic transaminase 2 was confirmed in first trimester placental explants cultured under fluidic flow. In contrast, high fluid shear stress decreased glutamic-oxaloacetic transaminase 2 expression in term placental explants when compared to low flow rates. Placental tissue from pregnancies with intrauterine growth restriction are exposed to high shear rates and showed also decreased glutamic-oxaloacetic transaminase 2, while GLUT1 was unchanged and glycolytic rate-limiting enzymes showed a trend to be upregulated. The results were generated by using qPCR, immunoblots, quantification of immunofluorescent pictures, padlock probe hybridization, mass spectrometry and FRET-based measurement.
CONCLUSION CONCLUSIONS
Our study suggests that onset of uteroplacental blood flow is accompanied by a shift from a predominant glycolytic- to an alternative amino acid converting metabolism in the villous trophoblast. Rheological changes with excessive fluidic shear stress at the placental surface, may disrupt this alternative amino acid pathway in the syncytiotrophoblast and could contribute to intrauterine growth restriction.

Identifiants

pubmed: 37684702
doi: 10.1186/s13578-023-01114-3
pii: 10.1186/s13578-023-01114-3
pmc: PMC10492287
doi:

Types de publication

Journal Article

Langues

eng

Pagination

163

Subventions

Organisme : Oesterreichische Nationalbank
ID : 18175
Organisme : Austrian Science Fund
ID : P 33554
Organisme : Austrian Science Fund
ID : I 3304
Organisme : Austrian Science Fund
ID : P 35118
Organisme : Austrian Science Fund
ID : Doc 31-B26

Informations de copyright

© 2023. Society of Chinese Bioscientists in America (SCBA).

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Auteurs

Beatrice Anna Brugger (BA)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Lena Neuper (L)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Jacqueline Guettler (J)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Désirée Forstner (D)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Stefan Wernitznig (S)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Daniel Kummer (D)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Freya Lyssy (F)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Julia Feichtinger (J)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Julian Krappinger (J)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Amin El-Heliebi (A)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.
Center for Biomarker Research in Medicine (CBmed), Graz, Austria.

Lilli Bonstingl (L)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.
Center for Biomarker Research in Medicine (CBmed), Graz, Austria.

Gerit Moser (G)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Giovanny Rodriguez-Blanco (G)

Clinical Institute for Medical and Chemical Laboratory Diagnosis, Medical University of Graz, Graz, Austria.

Olaf A Bachkönig (OA)

Division of Molecular Biology and Biochemistry, Gottfried Schatz Research Center, Medical University of Graz, Graz, Austria.

Benjamin Gottschalk (B)

Division of Molecular Biology and Biochemistry, Gottfried Schatz Research Center, Medical University of Graz, Graz, Austria.

Michael Gruber (M)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.

Olivia Nonn (O)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria.
Experimental and Clinical Research Center, a cooperation between the Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association and the Charité-Universitätsmedizin Berlin, Berlin, Germany.
Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany.

Florian Herse (F)

Experimental and Clinical Research Center, a cooperation between the Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association and the Charité-Universitätsmedizin Berlin, Berlin, Germany.
Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.
Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany.

Stefan Verlohren (S)

Department of Obstetrics and Gynaecology, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany.
Clinic for Obstetrics, Charité Berlin, Berlin, Germany.

Hans-Georg Frank (HG)

Department of Anatomy II, LMU Munich, Munich, Germany.

Nirav Barapatre (N)

Department of Anatomy II, LMU Munich, Munich, Germany.

Cornelia Kampfer (C)

Department of Anatomy II, LMU Munich, Munich, Germany.

Herbert Fluhr (H)

Department of Obstetrics and Gynaecology, Medical University of Graz, Graz, Austria.

Gernot Desoye (G)

Department of Obstetrics and Gynaecology, Medical University of Graz, Graz, Austria.

Martin Gauster (M)

Division of Cell Biology, Histology and Embryology, Gottfried Schatz Research Center, Medical University of Graz, Neue Stiftingtalstraße 6, OST V, 8010, Graz, Austria. martin.gauster@medunigraz.at.

Classifications MeSH