Evidence map›Paper›PMID 18647959›Full record

ArticleBlood2008

Functional analysis of the cytoplasmic domain of the integrin {alpha}1 subunit in endothelial cells.

Tristin D Abair, Nada Bulus, Corina Borza, Munirathinam Sundaramoorthy, Roy Zent, Ambra Pozzi

Open access · greenAbstract read
In one paragraph

Article in Blood, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

25 citing papers in PubMed, 39 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

6 authors at 3 institutions in 2 countries.

Tristin D AbairDepartment of Medicine, Division of Nephrology, Vanderbilt University, Nashville, TN, USA.
Nada Bulus
Corina Borza
Munirathinam Sundaramoorthy
Roy Zent
Ambra Pozzi
Centre for Cancer Biology · AUVanderbilt University · USVeterans Health Administration · US

Funding

TYPE IV COLLAGEN, LAMININS, AND INTEGRINS IN NORMAL AND DISEASED GLOMERULIP01DK065123 · NIDDK · VANDERBILT UNIVERSITY · PI HUDSON, BILLY GERALD · 2003 to 2012
$12.9M
MULTIDISCIPLINARY BASIC RESEARCH TRAINING IN CANCERT32CA009592 · NCI · VANDERBILT UNIVERSITY · PI Justin M Balko, Julie A Rhoades (Sterling) · 1987 to 2026
$10.4M
The Laminin Receptors in Kidney FibrosisR01DK069921 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI ROY ZENT · 2005 to 2026
$9.5M
Betal Integrin and Renal TubulogenesisR01DK075594 · NIDDK · VANDERBILT UNIVERSITY · PI ZENT, ROY · 2008 to 2015
$2.6M
Control of Tumor Growth by the MMP/Angiostatin PathwayR01CA094849 · NCI · VANDERBILT UNIVERSITY · PI POZZI, AMBRA · 2003 to 2007
$1.9M
NCI NIH HHS R01 CA094849NCI NIH HHS R01-CA94849NCI NIH HHS T32 CA009592NIDDK NIH HHS P01 DK065123NIDDK NIH HHS P01 DK65123NIDDK NIH HHS R01 DK075594NIDDK NIH HHS R01-DK 075594NIDDK NIH HHS R01-DK 69 921
6 · The paper itself

Abstract

Integrin alpha1beta1, the major collagen type IV receptor, is expressed by endothelial cells and plays a role in both physiologic and pathologic angiogenesis. Because the molecular mechanisms whereby this collagen IV receptor mediates endothelial cell functions are poorly understood, truncation and point mutants of the integrin alpha1 subunit cytoplasmic tail (amino acids 1137-1151) were generated and expressed into alpha1-null endothelial cells. We show that alpha1-null endothelial cells expressing the alpha1 subunit, which lacks the entire cytoplasmic tail (mutant alpha1-1136) or expresses all the amino acids up to the highly conserved GFFKR motif (mutant alpha1-1143), have a similar phenotype to parental alpha1-null cells. Pro(1144) and Leu(1145) were shown to be necessary for alpha1beta1-mediated endothelial cell proliferation; Lys(1146) for adhesion, migration, and tubulogenesis and Lys(1147) for tubulogenesis. Integrin alpha1beta1-dependent endothelial cell proliferation is primarily mediated by ERK activation, whereas migration and tubulogenesis require both p38 MAPK and PI3K/Akt activation. Thus, distinct amino acids distal to the GFFKR motif of the alpha1 integrin cytoplasmic tail mediate activation of selective downstream signaling pathways and specific endothelial cell functions.

Indexed as

Amino Acid MotifsCell AdhesionCell MovementCell ProliferationCytoplasmEndothelial CellsHumansIntegrin alpha1MutationNeovascularization, PathologicPhenotypePhosphatidylinositol 3-KinasesPoint MutationProtein Structure, TertiarySignal TransductionIntegrin alpha1Phosphatidylinositol 3-Kinases

Identifiers

PMID18647959
PMCPMC2569176
OpenAlexW2147961424

What OpenQuestion holds

Textmetadata
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.