Evidence map›Paper›PMID 31795436›Full record

ArticleBiomedicines2019

Intracellular Localization in Zebrafish Muscle and Conserved Sequence Features Suggest Roles for Gelatinase A Moonlighting in Sarcomere Maintenance.

Amina M Fallata, Rachael A Wyatt, Julie M Levesque, Antoine Dufour, Christopher M Overall, Bryan D Crawford

Open access · goldAbstract read
In one paragraph

Article in Biomedicines, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

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  4. Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.International journal of molecular sciences · 2022
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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

6 authors at 2 institutions in 1 country.

Amina M FallataDepartment of Biology, University of New Brunswick, Fredericton, NB E3B 5A3, Canada.
Rachael A WyattDepartment of Biology, University of New Brunswick, Fredericton, NB E3B 5A3, Canada.
Julie M LevesqueDepartment of Biology, University of New Brunswick, Fredericton, NB E3B 5A3, Canada.
Antoine DufourDepartment of Physiology & Pharmacology, University of Calgary, Calgary, AB T2N 4N1, Canada.
Christopher M OverallDepartment of Oral Biological and Medical Sciences and Centre for Blood Research, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.
Bryan D CrawfordDepartment of Biology, University of New Brunswick, Fredericton, NB E3B 5A3, Canada.
University of New Brunswick · CAUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gelatinase A (Mmp2 in zebrafish) is a well-characterized effector of extracellular matrix remodeling, extracellular signaling, and along with other matrix metalloproteinases (MMPs) and extracellular proteases, it plays important roles in the establishment and maintenance of tissue architecture. Gelatinase A is also found moonlighting inside mammalian striated muscle cells, where it has been implicated in the pathology of ischemia-reperfusion injury. Gelatinase A has no known physiological function in muscle cells, and its localization within mammalian cells appears to be due to inefficient recognition of its N-terminal secretory signal. Here we show that Mmp2 is abundant within the skeletal muscle cells of zebrafish, where it localizes to the M-line of sarcomeres and degrades muscle myosin. The N-terminal secretory signal of zebrafish Mmp2 is also challenging to identify, and this is a conserved characteristic of gelatinase A orthologues, suggesting a selective pressure acting to prevent the efficient secretion of this protease. Furthermore, there are several strongly conserved phosphorylation sites within the catalytic domain of gelatinase A orthologues, some of which are phosphorylated in vivo, and which are known to regulate the activity of this protease. We conclude that gelatinase A likely participates in uncharacterized physiological functions within the striated muscle, possibly in the maintenance of sarcomere proteostasis, that are likely regulated by kinases and phosphatases present in the sarcomere.

Indexed as

Gelatinase AMmp2myosinphosphorylationproteostasissarcomeresecretionTAILSzebrafish

Identifiers

PMID31795436
PMCPMC6966518
OpenAlexW2990975437

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.