GPCR/endocytosis/ERK signaling/S2R is involved in the regulation of the internalization, mitochondria-targeting and -activating properties of human salivary histatin 1.


Journal

International journal of oral science
ISSN: 2049-3169
Titre abrégé: Int J Oral Sci
Pays: India
ID NLM: 101504351

Informations de publication

Date de publication:
15 08 2022
Historique:
received: 27 12 2021
accepted: 10 05 2022
revised: 14 04 2022
entrez: 15 8 2022
pubmed: 16 8 2022
medline: 18 8 2022
Statut: epublish

Résumé

Human salivary histatin 1 (Hst1) exhibits a series of cell-activating properties, such as promoting cell spreading, migration, and metabolic activity. We recently have shown that fluorescently labeled Hst1 (F-Hst1) targets and activates mitochondria, presenting an important molecular mechanism. However, its regulating signaling pathways remain to be elucidated. We investigated the influence of specific inhibitors of G protein-coupled receptors (GPCR), endocytosis pathways, extracellular signal-regulated kinases 1/2 (ERK1/2) signaling, p38 signaling, mitochondrial respiration and Na+/K+-ATPase activity on the uptake, mitochondria-targeting and -activating properties of F-Hst1. We performed a siRNA knockdown (KD) to assess the effect of Sigma-2 receptor (S2R) /Transmembrane Protein 97 (TMEM97)-a recently identified target protein of Hst1. We also adopted live cell imaging to monitor the whole intracellular trafficking process of F-Hst1. Our results showed that the inhibition of cellular respiration hindered the internalization of F-Hst1. The inhibitors of GPCR, ERK1/2, phagocytosis, and clathrin-mediated endocytosis (CME) as well as siRNA KD of S2R/TMEM97 significantly reduced the uptake, which was accompanied by the nullification of the promoting effect of F-Hst1 on cell metabolic activity. Only the inhibitor of CME and KD of S2R/TMEM97 significantly compromised the mitochondria-targeting of Hst1. We further showed the intracellular trafficking and targeting process of F-Hst1, in which early endosome plays an important role. Overall, phagocytosis, CME, GPCR, ERK signaling, and S2R/TMEM97 are involved in the internalization of Hst1, while only CME and S2R/TMEM97 are critical for its subcellular targeting. The inhibition of either internalization or mitochondria-targeting of Hst1 could significantly compromise its mitochondria-activating property.

Identifiants

pubmed: 35970844
doi: 10.1038/s41368-022-00181-5
pii: 10.1038/s41368-022-00181-5
pmc: PMC9378733
doi:

Substances chimiques

Histatins 0
Membrane Proteins 0
RNA, Small Interfering 0
Receptors, G-Protein-Coupled 0
Receptors, sigma 0
TMEM97 protein, human 0
sigma-2 receptor 0
HTN1 protein, human 101056-53-5

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

42

Informations de copyright

© 2022. The Author(s).

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Auteurs

Dandan Ma (D)

Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands.
School of Stomatology, Zhejiang Chinese Medical University, Hangzhou, China.
Laboratory for Myology, Department of Human Movement Sciences, Faculty of Behavioral and Movement Sciences, Amsterdam Movement Sciences, Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Wei Sun (W)

Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Cuicui Fu (C)

Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Kamran Nazmi (K)

Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Enno C I Veerman (ECI)

Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Richard T Jaspers (RT)

Laboratory for Myology, Department of Human Movement Sciences, Faculty of Behavioral and Movement Sciences, Amsterdam Movement Sciences, Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Jan G M Bolscher (JGM)

Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Floris J Bikker (FJ)

Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands.

Gang Wu (G)

Department of Oral Cell Biology, Academic Centre for Dentistry Amsterdam(ACTA), University of Amsterdam and Vrije Universiteit Amsterdam, Amsterdam, Netherlands. g.wu@acta.nl.
Department of Oral and Maxillofacial Surgery/Pathology, Amsterdam UMC and Academic Center for Dentistry Amsterdam (ACTA), Vrije Universiteit Amsterdam, Amsterdam Movement Science, Amsterdam, Netherlands. g.wu@acta.nl.

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