Evidence map›Paper›PMID 27687691›Full record

ArticleScientific reports2016

Expression of B4GALNT1, an essential glycosyltransferase for the synthesis of complex gangliosides, suppresses BACE1 degradation and modulates APP processing.

Tokiaki Yamaguchi, Yoshio Yamauchi, Keiko Furukawa, Yuhsuke Ohmi, Yuki Ohkawa, Qing Zhang, Tetsuya Okajima, Koichi Furukawa

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

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  5. Downregulation ofZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2024
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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

8 authors at 2 institutions in 1 country.

Tokiaki YamaguchiDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
Yoshio YamauchiDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
Keiko FurukawaDepartment of Biomedical Sciences, Chubu University College of Life and Health Science, Kasugai 487-8501, Japan.
Yuhsuke OhmiDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
Yuki OhkawaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
Qing ZhangDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
Tetsuya OkajimaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
Koichi FurukawaDepartment of Biochemistry II, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
Nagoya University · JPChubu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is the most prevalent form of dementia characterized by the extracellular accumulation of amyloid β (Aβ) peptides, which are produced by proteolytic cleavages of amyloid precursor protein (APP). Gangliosides are involved in AD pathophysiology including Aβ deposition and APP processing, yet the detailed mechanisms are not fully understood. Here we examined how changes in the carbohydrate moiety of gangliosides alter APP processing in human melanoma cells, neuroectoderm-derived cells. We showed that forced expression of GD2, GM2 or GM1 (by introducing B4GALNT1 cDNA into cells not expressing this glycosyltransferase) results in increases of α- and β-site cleavages of APP with a prominent increase in β-cleavage. We also showed that β-site APP cleaving enzyme 1 (BACE1) protein is highly protected from the degradation in cells expressing these gangliosides, thereby increasing the expression of this protein. Unexpectedly, adding gangliosides exogenously altered neither BACE1 levels nor β-site cleavage. The stabilisation of BACE1 protein led to the increase of this protein in lipid rafts, where BACE1 processes APP. Based on the current results, we propose a hitherto undisclosed link between ganglioside expression and AD; the expression of B4GALNT1 positively regulates the β-site cleavage by mainly inhibiting the lysosomal degradation of BACE1 protein.

Identifiers

PMID27687691
PMCPMC5043288
OpenAlexW2526855527

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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.