Rat submandibular glands secrete nanovesicles with NTPDase and 5′-nucleotidase activities
Autor: | Martín M. Barbieri van Haaster, Claude Hattab, Patricia Egido, Débora A. González, Noelia B. Balcarcel, Julie Pelletier, Jean Sévigny, Mariano A. Ostuni |
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Jazyk: | angličtina |
Rok vydání: | 2014 |
Předmět: |
Adenosine Triphosphatases
Nucleotidase activity medicine.diagnostic_test Secretory Vesicles Purinergic receptor Submandibular Gland Biological Transport Cell Biology Biology Submandibular gland 5'-nucleotidase Rats Cellular and Molecular Neuroscience medicine.anatomical_structure Biochemistry Western blot Nucleotidase Extracellular medicine Animals Secretion Original Article Rats Wistar Molecular Biology 5'-Nucleotidase |
Popis: | Extracellular nucleotides modulate a wide number of biological processes such as neurotransmission, platelet aggregation, muscle contraction, and epithelial secretion acting by the purinergic pathway. Nucleotidases as NTPDases and ecto-5′-nucleotidase are membrane-anchored proteins that regulate extracellular nucleotide concentrations. In a previous work, we have partially characterized an NTPDase-like activity expressed by rat submandibular gland microsomes, giving rise to the hypothesis that membrane NTPDases could be released into salivary ducts to regulate luminal nucleotide concentrations as was previously proposed for ovarian, prostatic, and pancreatic secretions. Present results show that rat submandibular glands incubated in vitro release membrane-associated NTPDase and ecto-5′-nucleotidase activities. Electron microscopy images show that released membranes presenting nucleotidase activity correspond to exosome-like vesicles which are also present at microsomal fraction. Both exosome release and nucleotidase activities are raised by adrenergic stimulation. Nucleotidase activities present the same kinetic characteristics than microsomal nucleotidase activity, corresponding mainly to the action of NTPDase2 and NTPDase3 isoforms as well as 5′-nucleotidase. This is consistent with Western blot analysis revealing the presence of these enzymes in the microsomal fraction. Electronic supplementary material The online version of this article (doi:10.1007/s11302-014-9437-0) contains supplementary material, which is available to authorized users. |
Databáze: | OpenAIRE |
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