Evidence map›Paper›PMID 18180404›Full record

ArticleHypertension (Dallas, Tex. : 1979)2008

Novel role of protein kinase C-delta Tyr 311 phosphorylation in vascular smooth muscle cell hypertrophy by angiotensin II.

Hidekatsu Nakashima, Gerald D Frank, Heigoro Shirai, Akinari Hinoki, Sadaharu Higuchi, Haruhiko Ohtsu, Kunie Eguchi, Archana Sanjay, Mary E Reyland, Peter J Dempsey and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Hypertension (Dallas, Tex. : 1979), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 32 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

12 authors at 4 institutions in 1 country.

Hidekatsu NakashimaCardiovascular Research Center, Department of Physiology, Temple University School of Medicine, 3420 N Broad St, Philadelphia, PA 19140, USA.
Gerald D Frank
Heigoro Shirai
Akinari Hinoki
Sadaharu Higuchi
Haruhiko Ohtsu
Kunie Eguchi
Archana Sanjay
Mary E Reyland
Peter J Dempsey
Tadashi Inagami
Satoru Eguchi
Vanderbilt University · USUniversity of Colorado Health · USUniversity of Colorado Hospital · USUniversity of Colorado Denver · US

Funding

Regulation of Salivary Cell Apoptosis by Protein Kinase CR01DE015648 · NIDCR · UNIVERSITY OF COLORADO DENVER · PI REYLAND, MARY ELAINE · 2004 to 2019
$5.6M
ErbB Activation via a Metalloprotease by Angiotensin IIR01HL076770 · NHLBI · VANDERBILT UNIVERSITY · PI EGUCHI, SATORU · 2004 to 2012
$2.8M
Vascular Smooth Muscle PKC Delta: Signaling and FunctionK01HL076575 · NHLBI · VANDERBILT UNIVERSITY · PI FRANK, GERALD D · 2004 to 2008
$682k
NHLBI NIH HHS HL076575NHLBI NIH HHS HL076770NHLBI NIH HHS K01 HL076575NHLBI NIH HHS R01 HL076770NIDCR NIH HHS DE015648NIDCR NIH HHS R01 DE015648
6 · The paper itself

Abstract

We have shown previously that activation of protein kinase C-delta (PKC delta) is required for angiotensin II (Ang II)-induced migration of vascular smooth muscle cells (VSMCs). Here, we have hypothesized that PKC delta phosphorylation at Tyr(311) plays a critical role in VSMC hypertrophy induced by Ang II. Immunoblotting was used to monitor PKC delta phosphorylation at Tyr(311), and cell size and protein measurements were used to detect hypertrophy in VSMCs. PKC delta was rapidly (0.5 to 10.0 minutes) phosphorylated at Tyr(311) by Ang II. This phosphorylation was markedly blocked by an Src family kinase inhibitor and dominant-negative Src but not by an epidermal growth factor receptor kinase inhibitor. Ang II-induced Akt phosphorylation and hypertrophic responses were significantly enhanced in VSMCs expressing PKC delta wild-type compared with VSMCs expressing control vector, whereas the enhancements were markedly diminished in VSMCs expressing a PKC delta Y311F mutant. Also, these responses were significantly inhibited in VSMCs expressing kinase-inactive PKC delta K376A compared with VSMCs expressing control vector. From these data, we conclude that not only PKC delta kinase activation but also the Src-dependent Tyr(311) phosphorylation contributes to Akt activation and subsequent VSMC hypertrophy induced by Ang II, thus signifying a novel molecular mechanism for enhancement of cardiovascular diseases induced by Ang II.

Indexed as

Amino Acid SequenceAngiotensin IIAnimalsAortaCells, CulturedGTP-Binding Protein alpha Subunits, Gq-G11HypertrophyImmunoblottingMuscle, Smooth, VascularMyocytes, Smooth MusclePhosphorylationProtein Kinase C-deltaRatsReceptor, Angiotensin, Type 1src-Family KinasesTyrosineAngiotensin IIGTP-Binding Protein alpha Subunits, Gq-G11Protein Kinase C-deltaReceptor, Angiotensin, Type 1src-Family KinasesTyrosine

Identifiers

PMID18180404
PMCPMC2728048
OpenAlexW2117905385

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.