Evidence map›Paper›PMID 37108200›Full record

ArticleInternational journal of molecular sciences2023

Vesicular Integral-Membrane Protein 36 Is Involved in the Selective Secretion of Fucosylated Proteins into Bile Duct-like Structures in HepG2 Cells.

Mizuki Muranaka, Shinji Takamatsu, Tsunenori Ouchida, Yuri Kanazawa, Jumpei Kondo, Tsutomu Nakagawa, Yuriko Egashira, Koji Fukagawa, Jianguo Gu, Toru Okamoto and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
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

12 authors at 4 institutions in 1 country.

Mizuki MuranakaDepartment of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, 1-7 Yamada-oka, Suita 565-0871, Osaka, Japan.
Shinji TakamatsuDepartment of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, 1-7 Yamada-oka, Suita 565-0871, Osaka, Japan.ORCID 0000-0003-1996-7740
Tsunenori OuchidaDepartment of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, 1-7 Yamada-oka, Suita 565-0871, Osaka, Japan.
Yuri KanazawaDepartment of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, 1-7 Yamada-oka, Suita 565-0871, Osaka, Japan.
Jumpei KondoDepartment of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, 1-7 Yamada-oka, Suita 565-0871, Osaka, Japan.
Tsutomu NakagawaDepartment of Pharmaceutics, School of Pharmaceutical Sciences, Health Sciences University of Hokkaido, 1757 Kanazawa, Toubetsu-cho, Ishikari-gun 061-0293, Hokkaido, Japan.
Yuriko EgashiraBio-Diagnostic Reagent Technology Center, Sysmex Corporation, 4-3-2 Takatsukadai, Nishi-ku, Kobe 651-2271, Hyogo, Japan.
Koji FukagawaBio-Diagnostic Reagent Technology Center, Sysmex Corporation, 4-3-2 Takatsukadai, Nishi-ku, Kobe 651-2271, Hyogo, Japan.
Jianguo GuDivision of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aobaku, Sendai 981-8558, Miyagi, Japan.ORCID 0000-0003-0241-8788
Toru OkamotoInstitute for Advanced Co-Creation Studies, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita 565-0871, Osaka, Japan.
Yoshihiro KamadaDepartment of Advanced Metabolic Hepatology, 1-7 Yamada-oka, Suita 565-0871, Osaka, Japan.
Eiji MiyoshiDepartment of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, 1-7 Yamada-oka, Suita 565-0871, Osaka, Japan.ORCID 0000-0002-9430-2362
The University of Osaka · JPSysmex (Japan) · JPHealth Sciences University of Hokkaido · JPTohoku Medical and Pharmaceutical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fucosylated proteins are widely used as biomarkers of cancer and inflammation. Fucosylated alpha-fetoprotein (AFP-L3) is a specific biomarker for hepatocellular carcinoma. We previously showed that increases in serum AFP-L3 levels depend on increased expression of fucosylation-regulatory genes and abnormal transport of fucosylated proteins in cancer cells. In normal hepatocytes, fucosylated proteins are selectively secreted in the bile duct but not blood. In cases of cancer cells without cellular polarity, this selective secretion system is destroyed. Here, we aimed to identify cargo proteins involved in the selective secretion of fucosylated proteins, such as AFP-L3, into bile duct-like structures in HepG2 hepatoma cells, which have cellular polarity like, in part, normal hepatocytes. α1-6 Fucosyltransferase (FUT8) is a key enzyme to synthesize core fucose and produce AFP-L3. Firstly, we knocked out the

Indexed as

Carcinoma, HepatocellularLiver Neoplasmsalpha-FetoproteinsBile DuctsBiomarkersFucoseHep G2 CellsHumansMembrane ProteinsProteomicsalpha-FetoproteinsBiomarkersFucoseMembrane ProteinsAFPcargo proteinfucosylationHepG2lectin

Identifiers

PMID37108200
PMCPMC10138374
OpenAlexW4364381611

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.