Evidence map›Paper›PMID 26150355›Full record

ArticleBiochemical and biophysical research communications2015

LMAN1 (ERGIC-53) is a potential carrier protein for matrix metalloproteinase-9 glycoprotein secretion.

Tyler Duellman, John Burnett, Alice Shin, Jay Yang

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

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  17. LMAN1 (ERGIC-53) promotes trafficking of neuroreceptors.Biochemical and biophysical research communications · 2019
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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

4 authors at 1 institution in 1 country.

Tyler DuellmanDepartment of Anesthesiology, University of Wisconsin School of Medicine and Public Health, Madison, WI 53705, USA.
John BurnettDepartment of Anesthesiology, University of Wisconsin School of Medicine and Public Health, Madison, WI 53705, USA.
Alice ShinDepartment of Anesthesiology, University of Wisconsin School of Medicine and Public Health, Madison, WI 53705, USA.
Jay YangDepartment of Anesthesiology, University of Wisconsin School of Medicine and Public Health, Madison, WI 53705, USA. Electronic address: Jyang75@wisc.edu.
University of Wisconsin–Madison · US

Funding

Training Program in Translational Cardiovascular Science (TPTCS)T32HL007936 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Lee Lochbaum Eckhardt, Gail A Robertson · 2001 to 2026
$11.6M
Treatment for neuropathic pain targeting selective inhibition of MEKR01GM105665 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI YANG, JAY · 2014 to 2017
$1.1M
Sigma 1 receptor as a master regulator of pronociceptive protein trafficking in tR01GM107054 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RUOHO, ARNOLD EINO, YANG, JAY · 2013 to 2016
$1.1M
NHLBI NIH HHS T32 HL007936NHLBI NIH HHS T32 HL07936-12NIGMS NIH HHS GM105665NIGMS NIH HHS R01 GM105665NIGMS NIH HHS R01 GM107054
6 · The paper itself

Abstract

Matrix metalloproteinase-9 (MMP-9) is a secreted glycoprotein with a major role in shaping the extracellular matrix and a detailed understanding of the secretory mechanism could help identify methods to correct diseases resulting from dysregulation of secretion. MMP-9 appears to follow a canonical secretory pathway through a quality control cycle in the endoplasmic reticulum (ER) before transport of the properly folded protein to the Golgi apparatus and beyond for secretion. Through a complementation assay, we determined that LMAN1, a well-studied lectin-carrier protein, interacts with a secretion-competent N-glycosylated MMP-9 in the ER while N-glycosylation-deficient secretion-compromised MMP-9 does not. In contrast, co-immunoprecipitation demonstrated protein interaction between LMAN1 and secretion-compromised N-glycosylation-deficient MMP-9. MMP-9 secretion was reduced in the LMAN1 knockout cell line compared to control cells confirming the functional role of LMAN1. These observations support the role of LMAN1 as a lectin-carrier protein mediating efficient MMP-9 secretion.

Indexed as

Amino Acid SubstitutionBacterial ProteinsChloroquineClustered Regularly Interspaced Short Palindromic RepeatsEndoplasmic ReticulumGene Knockout TechniquesGenetic Complementation TestGlycosylationHEK293 CellsHumansLuminescent ProteinsMannose-Binding LectinsMatrix Metalloproteinase 9Membrane ProteinsMutagenesis, Site-DirectedProtein Interaction Domains and MotifsBacterial ProteinsChloroquineLMAN1 protein, humanLuminescent ProteinsMannose-Binding LectinsMatrix Metalloproteinase 9Membrane ProteinsMMP9 protein, humanRecombinant Fusion Proteinsyellow fluorescent protein, BacteriaGlycoproteinLectin-carrier proteinMatrix metalloproteinase-9Secretion

Identifiers

PMID26150355
PMCPMC4697752
OpenAlexW794091443

What OpenQuestion holds

Textmetadata
LicenceTDM
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.