Evidence map›Paper›PMID 19923420›Full record

ArticleAmerican journal of physiology. Cell physiology2010

Abnormalities in focal adhesion complex formation, regulation, and function in human autosomal recessive polycystic kidney disease epithelial cells.

Sharon Israeli, Kurt Amsler, Nadezhda Zheleznova, Patricia D Wilson

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 44 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

4 authors at 2 institutions in 1 country.

Sharon IsraeliDepartment of Medicine, Division of Nephrology, Mount Sinai School of Medicine, New York, New York, USA.
Kurt Amsler
Nadezhda Zheleznova
Patricia D Wilson
Icahn School of Medicine at Mount Sinai · USMedical College of Wisconsin · US

Funding

Viral Vector, Cell Line, Tissue & Mouse Model Production, Validation & ProcessingP01DK062345 · NIDDK · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI WILSON, PATRICIA D. · 2003 to 2007
$6.7M
NIDDK NIH HHS P01 DK062345NIDDK NIH HHS P01DK62345
6 · The paper itself

Abstract

Integrin-associated focal adhesion complex formation and turnover plays an essential role in directing interactions between epithelial cells and the extracellular matrix during organogenesis, leading to appropriate cell spreading, cell-matrix adhesion, and migration. Autosomal recessive polycystic kidney disease (ARPKD) is associated with loss of function of PKHD1-encoded protein fibrocystin-1 and is characterized by cystic dilation of renal collecting tubules (CT) in utero and loss of renal function in patients if they survive the perinatal period. Normal polycystin-1 (PC-1)/focal adhesion complex function is required for control of CT diameter during renal development, and abnormalities in these complexes have been demonstrated in human PC-1 mutant cystic cells. To determine whether loss of fibrocystin-1 was associated with focal adhesion abnormalities, ARPKD cells or normal age-matched human fetal (HF)CT cells in which fibrocystin-1 had been decreased by 85% by small interfering RNA inhibition were compared with normal HFCT. Accelerated attachment and spreading on collagen matrix and decreased motility of fibrocystin-1-deficient cells were associated with longer paxillin-containing focal adhesions, more complex actin-cytoskeletal rearrangements, and increased levels of total beta(1)-integrin, c-Src, and paxillin. Immunoblot analysis of adhesive cells using site-specific phospho-antibodies demonstrated ARPKD-associated loss of activation of focal adhesion kinase (FAK) by phosphorylation at its autophosphorylation site (Y397); accelerated FAK inhibition by phosphorylation at Y407, S843, and S910; as well as increased activation of c-Src at pY418. Paxillin coimmunoprecipitation analyses suggested that fibrocystin-1 was a component of the normal focal adhesion complex and that actin and fibrocystin-1 were lost from ARPKD complexes.

Indexed as

ActinsAnimalsCell AdhesionCell MovementCells, CulturedEpithelial CellsFocal Adhesion Protein-Tyrosine KinasesFocal AdhesionsHumansKidney Tubules, CollectingMicePaxillinPolycystic Kidney, Autosomal RecessiveReceptors, Cell SurfaceRNA, Small InterferingTRPP Cation ChannelsActinsFocal Adhesion Protein-Tyrosine KinasesPaxillinPKHD1 protein, humanReceptors, Cell SurfaceRNA, Small InterferingTRPP Cation Channels

Identifiers

PMID19923420
PMCPMC2853216
OpenAlexW2030692297

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.