Evidence map›Paper›PMID 28246172›Full record

ArticleThe Journal of biological chemistry2017

A mammalian homolog of the zebrafish transmembrane protein 2 (TMEM2) is the long-sought-after cell-surface hyaluronidase.

Hayato Yamamoto, Yuki Tobisawa, Toshihiro Inubushi, Fumitoshi Irie, Chikara Ohyama, Yu Yamaguchi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

83 citing papers in PubMed, 161 citations in OpenAlex.

  1. Naive CD4iScience · 2026
    Article
  2. Angiogenesis, Angiogenic Factors, and Interstitial Cystitis/Bladder Pain Syndrome (IC/BPS).International journal of urology : official journal of the Japanese Urological Association · 2026
    Review
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23 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Hayato YamamotoFrom the Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California 92037 and.
Yuki TobisawaFrom the Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California 92037 and.
Toshihiro InubushiFrom the Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California 92037 and.
Fumitoshi IrieFrom the Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California 92037 and.
Chikara Ohyamathe Department of Urology, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan.
Yu YamaguchiFrom the Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, California 92037 and yyamaguchi@sbpdiscovery.org.
Sanford Burnham Prebys Medical Discovery Institute · USHirosaki University · JP

Funding

Genetic dissection of the role of chondroitin sulfate in cartilageR01AR062692 · NIAMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI YAMAGUCHI, YU · 2012 to 2016
$2.2M
NIAMS NIH HHS R01 AR062692
6 · The paper itself

Abstract

Hyaluronan (HA) is an extremely large polysaccharide (glycosaminoglycan) involved in many cellular functions. HA catabolism is thought to involve the initial cleavage of extracellular high-molecular-weight (HMW) HA into intermediate-size HA by an extracellular or cell-surface hyaluronidase, internalization of intermediate-size HA, and complete degradation into monosaccharides in lysosomes. Despite considerable research, the identity of the hyaluronidase responsible for the initial HA cleavage in the extracellular space remains elusive. HYAL1 and HYAL2 have properties more consistent with lysosomal hyaluronidases, whereas CEMIP/KIAA1199, a recently identified HA-binding molecule that has HA-degrading activity, requires the participation of the clathrin-coated pit pathway of live cells for HA degradation. Here we show that transmembrane protein 2 (TMEM2), a mammalian homolog of a protein playing a role in zebrafish endocardial cushion development, is a cell-surface hyaluronidase. Live immunostaining and surface biotinylation assays confirmed that mouse TMEM2 is expressed on the cell surface in a type II transmembrane topology. TMEM2 degraded HMW-HA into ∼5-kDa fragments but did not cleave chondroitin sulfate or dermatan sulfate, indicating its specificity to HA. The hyaluronidase activity of TMEM2 was Ca

Indexed as

AnimalsCalciumCell LineCell MembraneGene Expression Regulation, EnzymologicHumansHyaluronic AcidHyaluronoglucosaminidaseHydrogen-Ion ConcentrationMembrane ProteinsMiceCalciumHyaluronic AcidHyaluronoglucosaminidaseMembrane ProteinsTmem2 protein, mousecell surfaceCEMIP/KIAA1199glycosaminoglycanhyaluronanhyaluronidasemembrane functionTMEM2

Identifiers

PMID28246172
PMCPMC5418033
OpenAlexW2592565933

What OpenQuestion holds

Textmetadata
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.