Evidence map›Paper›PMID 26713442›Full record

ArticlePloS one2015

Biochemical Characterization of Medaka (Oryzias latipes) Transglutaminases, OlTGK1 and OlTGK2, as Orthologues of Human Keratinocyte-Type Transglutaminase.

Ayaka Kikuta, Eri Furukawa, Ryota Ogawa, Natsuki Suganuma, Mai Saitoh, Toshiyuki Nishimaki, Takafumi Katsumura, Hiroki Oota, Tadafumi Kawamoto, Hideki Tatsukawa and 2 more

Abstract read
In one paragraph

Article in PloS one, 2015. 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
–field-weighted citation impact
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.

  1. Article
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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

12 authors.

Ayaka KikutaGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601 Japan.
Eri FurukawaGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601 Japan.
Ryota OgawaGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601 Japan.
Natsuki SuganumaGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601 Japan.
Mai SaitohGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601 Japan.
Toshiyuki NishimakiKitasato University School of Medicine, Sagamihara, 252-0734 Japan.
Takafumi KatsumuraKitasato University School of Medicine, Sagamihara, 252-0734 Japan.
Hiroki OotaKitasato University School of Medicine, Sagamihara, 252-0734 Japan.
Tadafumi KawamotoRadioisotope Research Institute, School of Dental Medicine, Tsurumi University, Tsurumi, Yokohama, 230-8501 Japan.
Hideki TatsukawaGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601 Japan.
Hisashi HashimotoBioscience and Biotechnology Center, Nagoya University, Nagoya, 464-8601 Japan.
Kiyotaka HitomiGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, 464-8601 Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium-dependent transglutaminases (TGs) are a family of enzymes that catalyze protein cross-linking and/or attachment of primary amines in a variety of organisms. Mammalian TGs are implicated in multiple biological events such as skin formation, blood coagulation, and extracellular matrix stabilization. Medaka (Oryzias latipes) has been used as a model fish to investigate the physiological functions of mammalian proteins. By analysis of the medaka genome, we found seven TGs orthologues, some of which apparently corresponded to the mammalian TG isozymes, TG1, TG2, and Factor XIII. All orthologues had preserved amino acid residues essential for enzymatic activity in their deduced primary structures. In this study, we analyzed biochemical properties of two orthologues (OlTGK1 and OlTGK2) of mammalian epithelium-specific TG (TG1) that are significantly expressed at the transcriptional level. Using purified recombinant proteins for OlTGK1 and OlTGK2, we characterized their catalytic reactions. Furthermore, immunohistochemical analyses of fish sections revealed higher expression in the pancreas (OTGK1), intervertebral disk (OlTGK2) and pharyngeal teeth (OlTGK2) as well as in the skin epidermis.

Indexed as

Amino Acid SequenceAnimalsEpidermisFish ProteinsHumansKineticsMolecular Sequence DataOryziasPhylogenyTransglutaminasesFish ProteinsTransglutaminases

Identifiers

PMID26713442
PMCPMC4694659

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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.