Evidence map›Paper›PMID 25963142›Full record

ReviewMatrix biology : journal of the International Society for Matrix Biology2015

The microfibril-associated glycoproteins (MAGPs) and the microfibrillar niche.

Robert P Mecham, Mark A Gibson

Open access · hybridAbstract readReview
In one paragraph

Review in Matrix biology : journal of the International Society for Matrix Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2025
    Article
  4. Loss of MFAP5 and Its Effect on Skin Homeostasis and Wound Healing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  5. Article
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  11. Review
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  19. Article
  20. Article

2 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

2 authors at 2 institutions in 2 countries.

Robert P MechamDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA. Electronic address: bmecham@wustl.edu.
Mark A GibsonSchool of Medical Sciences, University of Adelaide, Adelaide, South Australia 5005, Australia.
University of Adelaide · AUWashington University in St. Louis · US

Funding

The Role of the Osteoblast Secretome in Bone FormationP30AR057235 · NIAMS · WASHINGTON UNIVERSITY · PI SILVA, MATTHEW J · 2009 to 2018
$5.7M
ASSEMBLY OF LUNG ELASTINR37HL053325 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P. · 2000 to 2009
$4.1M
ASSEMBLY OF LUNG ELASTINR01HL053325 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P. · 1995 to 2019
$3.6M
VESSEL STIFFENING, HYPERTENSION, AND VASCULAR EXTRACELLULAR MATRIXR01HL105314 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P., WAGENSEIL, JESSICA · 2010 to 2018
$3.2M
ELASTIN IN VESSEL DEVELOPMENT & VASCULAR DISEASESR01HL074138 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P. · 2004 to 2012
$3.0M
NHLBI NIH HHS HL105314NHLBI NIH HHS HL53325NHLBI NIH HHS HL74138NHLBI NIH HHS R01 HL053325NHLBI NIH HHS R01 HL074138NHLBI NIH HHS R01 HL105314NHLBI NIH HHS R37 HL053325NIAMS NIH HHS P30 AR057235
6 · The paper itself

Abstract

The microfibril-associated glycoproteins MAGP-1 and MAGP-2 are extracellular matrix proteins that interact with fibrillin to influence microfibril function. The two proteins are related through a 60 amino acid matrix-binding domain but their sequences differ outside of this region. A distinguishing feature of both proteins is their ability to interact with TGFβ family growth factors, Notch and Notch ligands, and multiple elastic fiber proteins. MAGP-2 can also interact with αvβ3 integrins via a RGD sequence that is not found in MAGP-1. Morpholino knockdown of MAGP-1 expression in zebrafish resulted in abnormal vessel wall architecture and altered vascular network formation. In the mouse, MAGP-1 deficiency had little effect on elastic fibers in blood vessels and lung but resulted in numerous unexpected phenotypes including bone abnormalities, hematopoietic changes, increased fat deposition, diabetes, impaired wound repair, and a bleeding diathesis. Inactivation of the gene for MAGP-2 in mice produced a neutropenia yet had minimal effects on bone or adipose homeostasis. Double knockouts had phenotypes characteristic of each individual knockout as well as several additional traits only seen when both genes are inactivated. A common mechanism underlying all of the traits associated with the knockout phenotypes is altered TGFβ signaling. This review summarizes our current understanding of the function of the MAGPs and discusses ideas related to their role in growth factor regulation.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsBone DevelopmentContractile ProteinsExtracellular Matrix ProteinsFibrillinsGene ExpressionGlycoproteinsHematopoiesisHumansMicrofibrilsMicrofilament ProteinsMolecular Sequence DataProtein Processing, Post-TranslationalRNA Splicing FactorsContractile ProteinsExtracellular Matrix ProteinsFibrillinsGlycoproteinsmicrofibrillar proteinMicrofilament ProteinsRNA Splicing FactorsDiabetesfibrilinMAGPMicrofibrilMicrofibril-associated glycoproteinObesityOsteoporosisTGFβ

Identifiers

PMID25963142
PMCPMC5154765
OpenAlexW272428685

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.