Evidence map›Paper›PMID 7514608›Full record

ArticleThe Journal of cell biology1994

SPARC is a source of copper-binding peptides that stimulate angiogenesis.

T F Lane, M L Iruela-Arispe, R S Johnson, E H Sage

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

69 citing papers in PubMed, 251 citations in OpenAlex.

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  20. Ternary Cu(II) Complex with GHK Peptide andInternational journal of molecular sciences · 2020
    Article

9 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

4 authors at 1 institution in 1 country.

T F LaneDepartment of Biological Structure, University of Washington School of Medicine, Seattle 98195.
M L Iruela-Arispe
R S Johnson
E H Sage
University of Washington · US

Funding

EXPERIMENTAL PATHOLOGY OF CARDIOVASCULAR DISEASET32HL007312 · NHLBI · UNIVERSITY OF WASHINGTON · PI MAJESKY, MARK W., SCHWARTZ, STEPHEN MARK · 1985 to 2019
$11.8M
EXTRACELLULAR PROTEINS AS SIGNALS IN ENDOTHELIAL GROWTHR01GM040711 · NIGMS · UNIVERSITY OF WASHINGTON · PI SAGE, EMILY HELENE · 1988 to 2009
$2.7M
NHLBI NIH HHS HL-03174NHLBI NIH HHS HL-07312NIGMS NIH HHS GM-40711
6 · The paper itself

Abstract

SPARC is a transiently expressed extracellular matrix-binding protein that alters cell shape and regulates endothelial cell proliferation in vitro. In this study, we show that SPARC mRNA and protein are synthesized by endothelial cells during angiogenesis in vivo. SPARC and peptides derived from a cationic region of the protein (amino acids 113-130) stimulated the formation of endothelial cords in vitro; moreover, these peptides stimulated angiogenesis in vivo. Mapping of the active domain demonstrated that the sequence KGHK was responsible for most of the angiogenic activity; substitution of the His residue decreased the effect. We found that proteolysis of SPARC provided a source of KGHK, GHK, and longer peptides that contained these sequences. Although the Cu(2+)-GHK complex had been identified as a mitogen/morphogen in normal human plasma, we found KGHK and longer peptides to be potent stimulators of angiogenesis. SPARC113-130 and KGHK were shown to bind Cu2+ with high affinity; however, previous incubation with Cu2+ was not required for the stimulatory activity. Since a peptide from a second cationic region of SPARC (SPARC54-73) also bound Cu2+ but had no effect on angiogenesis, the angiogenic activity appeared to be sequence specific and independent of bound Cu2+. Thus, specific degradation of SPARC, a matrix-associated protein expressed by endothelial cells during vascular remodeling, releases a bioactive peptide or peptides, containing the sequence (K)GHK, that could regulate angiogenesis in vivo.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCarrier ProteinsCattleCells, CulturedCopperEndopeptidasesEndothelium, VascularExtracellular SpaceFemaleFibrinolysinMaleMiceMolecular Sequence DataNeovascularization, PathologicCarrier ProteinsCoppercopper-binding proteinEndopeptidasesFibrinolysinOsteonectinPeptide FragmentsTrypsin

Identifiers

PMID7514608
PMCPMC2120067
OpenAlexW2095724936

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.