Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 175

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Prometastatic Effect ofN-Acetylglucosaminyltransferase V Is Due to Modification and Stabilization of Active Matriptase by Adding β1–6 GlcNAc Branching

Open access
Ihara, Shinji, Miyoshi, Eiji, Ko, Jeong Heon, Murata, Kohei, Nakahara, Susumu, Honke, Koichi, Dickson, Robert B., Lin, Chen-Yong, Taniguchi, Naoyuki·2002·Journal of Biological Chemistry

Abstract

Oligosaccharide moieties of glycoproteins are structurally altered during development, carcinogenesis, and malignant transformations. It is well known that beta1-6 GlcNAc branching, a product of UDP-GlcNAc alpha-mannoside beta1-6-N-acetylglucosaminyltransferase (GnT-V), is associated with malignant transformation as the results of such alterations. However, the mechanism by which beta1-6 GlcNAc branching is linked to metastasis remains unclear, because the identification of specific glycoprotein(s) that are glycosylated by GnT-V and its biological function have not been examined. We herein report that matriptase, which activates both urokinase-type plasminogen activator and hepatocyte growth factor, is a target protein for GnT-V. The overexpression of GnT-V in gastric cancer cells leads to severe peritoneal dissemination in athymic mice, which can be attributed to the increased expression of matriptase. This increase was due to the acquired resistance of matriptase to degradation, since it is glycosylated by GnT-V and a corresponding increase in the active form. These results indicate that this process is a key element in malignant transformation, as the direct result of oligosaccharide modification.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.m200673200

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 3 references

Cited by

See all 175

Metadata

Authors
Ihara, S., Miyoshi, E., Ko, J. H., Murata, K., Nakahara, S., Honke, K., Dickson, R. B., Lin, C.-Y., & Taniguchi, N.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-05
Volume
277
Issue
19
Pages
16960-16967
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2115504260
Cited by
175
References
3
FWCI
4.10
Type
journal article
Language
en
Open access
hybrid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Prometastatic Effect ofN-Acetylglucosaminyltransferase V Is Due to Modification and Stabilization of Active Matriptase by Adding β1–6 GlcNAc Branching. https://app.cochat.ai/papers/10.1074/jbc.m200673200
The paper
Ihara, S., Miyoshi, E., Ko, J. H., Murata, K., Nakahara, S., Honke, K., Dickson, R. B., Lin, C.-Y., & Taniguchi, N. (2002). Prometastatic Effect ofN-Acetylglucosaminyltransferase V Is Due to Modification and Stabilization of Active Matriptase by Adding β1–6 GlcNAc Branching. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m200673200

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.