Evidence map›Paper›PMID 26888252›Full record

ArticleImmunology and cell biology2016

A naturally occurring transcript variant of MARCO reveals the SRCR domain is critical for function.

Kyle E Novakowski, Angela Huynh, SeongJun Han, Michael G Dorrington, Charles Yin, Zhongyuan Tu, Peter Pelka, Peter Whyte, Alba Guarné, Kaori Sakamoto and 1 more

Open access · greenAbstract read
In one paragraph

Article in Immunology and cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

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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

11 authors at 3 institutions in 2 countries.

Kyle E NovakowskiDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
Angela HuynhDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
SeongJun HanDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
Michael G DorringtonDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
Charles YinDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
Zhongyuan TuDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
Peter PelkaDepartment of Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada.
Peter WhyteDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
Alba GuarnéDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Kaori SakamotoDepartment of Pathology, College of Veterinary Medicine, University of Georgia, Athens, GA, USA.
Dawn M E BowdishDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
McMaster University · CAUniversity of Georgia · USUniversity of Manitoba · CA

Funding

Role of MARCO in susceptibility and resistance to tuberculosisR15AI094436 · NIAID · UNIVERSITY OF GEORGIA · PI SAKAMOTO, KAORI · 2012 to 2012
$405k
CIHRNIAID NIH HHS R15 AI094436
6 · The paper itself

Abstract

Macrophage receptor with collagenous structure (MARCO) is a class A scavenger receptor (cA-SR) that recognizes and phagocytoses a wide variety of pathogens. Most cA-SRs that contain a C-terminal scavenger receptor cysteine-rich (SRCR) domain use the proximal collagenous domain to bind ligands. In contrast, the role of the SRCR domain of MARCO in phagocytosis, adhesion and pro-inflammatory signaling is less clear. The discovery of a naturally occurring transcript variant lacking the SRCR domain, MARCOII, provided the opportunity to study the role of the SRCR domain of MARCO. We tested whether the SRCR domain is required for ligand binding, promoting downstream signaling and enhancing cellular adhesion. Unlike cells expressing full-length MARCO, ligand binding was abolished in MARCOII-expressing cells. Furthermore, co-expression of MARCO and MARCOII impaired phagocytic function, indicating that MARCOII acts as a dominant-negative variant. Unlike MARCO, expression of MARCOII did not enhance Toll-like receptor 2 (TLR2)-mediated pro-inflammatory signaling in response to bacterial stimulation. MARCO-expressing cells were more adherent and exhibited a dendritic-like phenotype, whereas MARCOII-expressing cells were less adherent and did not exhibit changes in morphology. These data suggest the SRCR domain of MARCO is the key domain in modulating ligand binding, enhancing downstream pro-inflammatory signaling and MARCO-mediated cellular adhesion.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsCell AdhesionCell ShapeCloning, MolecularEndocytosisHEK293 CellsHumansLigandsLipopolysaccharide ReceptorsMice, Inbred C57BLNF-kappa BProtein DomainsReceptors, ImmunologicRNA, MessengerLigandsLipopolysaccharide ReceptorsMARCO protein, humanNF-kappa BReceptors, ImmunologicRNA, MessengerToll-Like Receptor 2

Identifiers

PMID26888252
PMCPMC4980223
OpenAlexW2293030617

What OpenQuestion holds

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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.