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Antithrombin is incorporated into exosomes produced by antithrombin non-expressing cells
Ginés Luengo-Gil1, Antonio Bernardino García-Andreo1, Carmen Ortega-Sabater1
1Servicio de Hematología y Oncología Médica, Hospital Universitario Morales Meseguer, Centro Regional de Hemodonación, Universidad de Murcia, IMIB-Arrixaca, U-765, Center for Biomedical Research on Rare Diseases, Murcia, Spain.
Biochimie
|August 25, 2019
Summary
Madin-Darby canine kidney (MDCK) cells release exosomes containing antithrombin (AT), a key coagulation inhibitor. This exosomal AT forms complexes with high temperature requirement A1 (HTRA1), suggesting a novel biological interaction.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Medicine
Background:
- Antithrombin (AT) is a critical serine protease inhibitor regulating hemostasis.
- AT also influences inflammation and cancer progression.
- Exosomes are key mediators of intercellular communication.
Purpose of the Study:
- To investigate the presence and potential function of antithrombin within exosomes.
- To explore the interaction between exosomal antithrombin and other proteins.
Main Methods:
- Madin-Darby canine kidney (MDCK) cells were cultured in the presence of heparin.
- Exosomes were isolated from cell culture supernatant.
- Proteomic analysis was performed to identify proteins within exosomes, including antithrombin and HTRA1.
Main Results:
- Exosomes released by MDCK cells incorporate antithrombin from the serum.
- Exosomal antithrombin was found to be complexed with the serine protease high temperature requirement A1 (HTRA1).
- Cellular HTRA1 levels increased under serum deprivation, the condition used for exosome collection.
Conclusions:
- MDCK cell-derived exosomes can carry antithrombin, potentially sequestered from the serum.
- A functional interplay between antithrombin and HTRA1 within exosomes is suggested.
- Further research is needed to elucidate the biological significance of exosomal antithrombin and its complex with HTRA1.
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