Evidence map›Paper›PMID 30982221›Full record

ArticleJournal of cellular and molecular medicine2019

Anti-human CD9 antibody Fab fragment impairs the internalization of extracellular vesicles and the nuclear transfer of their cargo proteins.

Mark F Santos, Germana Rappa, Jana Karbanová, Cheryl Vanier, Chikao Morimoto, Denis Corbeil, Aurelio Lorico

Open access · goldAbstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 31 citations in OpenAlex.

  1. Rethinking Extracellular Vesicle Signaling.Advanced materials (Deerfield Beach, Fla.) · 2026
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  18. Silencing ofFrontiers in cellular and infection microbiology · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Mark F SantosCollege of Medicine, Touro University Nevada, Henderson, Nevada.
Germana RappaCollege of Medicine, Touro University Nevada, Henderson, Nevada.
Jana KarbanováBiotechnology Center and Center for Molecular and Cellular Bioengineering, Technische Universität Dresden, Dresden, Germany.
Cheryl VanierCollege of Medicine, Touro University Nevada, Henderson, Nevada.
Chikao MorimotoDepartment of Therapy Development and Innovation for Immune Disorders and Cancers, Graduate School of Medicine, Juntendo University, Bunkyo-ku, Tokyo, Japan.
Denis CorbeilBiotechnology Center and Center for Molecular and Cellular Bioengineering, Technische Universität Dresden, Dresden, Germany.ORCID 0000-0003-1181-3659
Aurelio LoricoCollege of Medicine, Touro University Nevada, Henderson, Nevada.ORCID 0000-0003-0644-7375
Touro University Nevada · USTechnische Universität Dresden · DEJuntendo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intercellular communication mediated by extracellular vesicles (EVs) has gained international interest during the last decade. Interfering with the mechanisms regulating this cellular process might find application particularly in oncology where cancer cell-derived EVs play a role in tumour microenvironment transformation. Although several mechanisms were ascribed to explain the internalization of EVs, little is our knowledge about the fate of their cargos, which are crucial to mediate their function. We recently demonstrated a new intracellular pathway in which a fraction of endocytosed EV-associated proteins is transported into the nucleoplasm of the host cell via a subpopulation of late endosomes penetrating into the nucleoplasmic reticulum. Silencing tetraspanin CD9 both in EVs and recipient cells strongly decreased the endocytosis of EVs and abolished the nuclear transfer of their cargos. Here, we investigated whether monovalent Fab fragments derived from 5H9 anti-CD9 monoclonal antibody (referred hereafter as CD9 Fab) interfered with these cellular processes. To monitor the intracellular transport of proteins, we used fluorescent EVs containing CD9-green fluorescent protein fusion protein and various melanoma cell lines and bone marrow-derived mesenchymal stromal cells as recipient cells. Interestingly, CD9 Fab considerably reduced EV uptake and the nuclear transfer of their proteins in all examined cells. In contrast, the divalent CD9 antibody stimulated both events. By impeding intercellular communication in the tumour microenvironment, CD9 Fab-mediated inhibition of EV uptake, combined with direct targeting of cancerous cells could lead to the development of novel anti-melanoma therapeutic strategies.

Indexed as

Active Transport, Cell NucleusCell CommunicationCells, CulturedEndocytosisExtracellular VesiclesHumansImmunoglobulin Fab FragmentsIntracellular Signaling Peptides and ProteinsMelanomaMesenchymal Stem CellsNeoplasm ProteinsTetraspanin 29Immunoglobulin Fab FragmentsIntracellular Signaling Peptides and ProteinsNeoplasm ProteinsTetraspanin 29cancerCD9endocytosisextracellular vesicleFab fragmentnucleoplasm

Identifiers

PMID30982221
PMCPMC6533511
OpenAlexW2940308113

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.