NDLI: Cytosolic Phospholipase A2-α Mediates Endothelial Cell Proliferation and Is Inactivated by Association with the Golgi Apparatus

Content Provider	PubMed Central
Author	Herbert, S. P. Ponnambalam, S. Walker, J. H.
Editor	Malhotra, Vivek
Copyright Year	2005
Abstract	Arachidonic acid and its metabolites are implicated in regulating endothelial cell proliferation. Cytosolic phospholipase A2-α (cPLA2α) is responsible for receptor-mediated arachidonic acid evolution. We tested the hypothesis that cPLA2α activity is linked to endothelial cell proliferation. The specific cPLA2α inhibitor, pyrrolidine-1, inhibited umbilical vein endothelial cell (HUVEC) proliferation in a dose-dependent manner. Exogenous arachidonic acid addition reversed this inhibitory effect. Inhibition of sPLA2 did not affect HUVEC proliferation. The levels of cPLA2α did not differ between subconfluent and confluent cultures of cells. However, using fluorescence microscopy we observed a novel, confluence-dependent redistribution of cPLA2α to the distal Golgi apparatus in HUVECs. Association of cPLA2α with the Golgi was linked to the proliferative status of HUVECs. When associated with the Golgi apparatus, cPLA2α activity was seen to be 87% inhibited. Relocation of cPLA2α to the cytoplasm and nucleus, and cPLA2α enzyme activity were required for cell cycle entry upon mechanical wounding of confluent monolayers. Thus, cPLA2α activity and function in controlling endothelial cell proliferation is regulated by reversible association with the Golgi apparatus.
Related Links	http://dx.doi.org/10.1091/mbc.e05-02-0164
Ending Page	3809
Page Count	10
Starting Page	3800
File Format	PDF
ISSN	10591524
Journal	Molecular Biology of the Cell
Issue Number	8
Volume Number	16
Language	English
Publisher	The American Society for Cell Biology
Publisher Date	2005-05-01
Access Restriction	Open
Rights Holder	The American Society for Cell Biology
Subject Keyword	Cell Biology Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Nuclear localisation of cytosolic phospholipase A2-α in the EA.hy.926 human endothelial cell line is proliferation dependent and modulated by phosphorylation

A VE-cadherin–PAR3–α-catenin complex regulates the Golgi localization and activity of cytosolic phospholipase A2α in endothelial cells

Activation of Cytosolic Phospholipase A2-α as a Novel Mechanism Regulating Endothelial Cell Cycle Progression and Angiogenesis*

The Confluence-dependent Interaction of Cytosolic Phospholipase A2-α with Annexin A1 Regulates Endothelial Cell Prostaglandin E2 Generation

Lung Krüppel-like factor (LKLF) is a transcriptional activator of the cytosolic phospholipase A2 α promoter

The Cytosolic Phospholipase A2 Catalytic Domain Modulates Association and Residence Time at Golgi Membranes

The Calcium Binding Loops of the Cytosolic Phospholipase A2 C2 Domain Specify Targeting to Golgi and ER in Live CellsV⃞

Membrane Tubule-mediated Reassembly and Maintenance of the Golgi Complex Is Disrupted by Phospholipase A2 Antagonists

Activation of Cytosolic Phospholipase A2 α in Resident Peritoneal Macrophages by Listeria monocytogenes Involves Listeriolysin O and TLR2 *

Cytosolic Phospholipase A2-α Mediates Endothelial Cell Proliferation and Is Inactivated by Association with the Golgi Apparatus

Similar Documents

Nuclear localisation of cytosolic phospholipase A2-α in the EA.hy.926 human endothelial cell line is proliferation dependent and modulated by phosphorylation

A VE-cadherin–PAR3–α-catenin complex regulates the Golgi localization and activity of cytosolic phospholipase A2α in endothelial cells

Activation of Cytosolic Phospholipase A2-α as a Novel Mechanism Regulating Endothelial Cell Cycle Progression and Angiogenesis*

The Confluence-dependent Interaction of Cytosolic Phospholipase A2-α with Annexin A1 Regulates Endothelial Cell Prostaglandin E2 Generation

Lung Krüppel-like factor (LKLF) is a transcriptional activator of the cytosolic phospholipase A2 α promoter

The Cytosolic Phospholipase A2 Catalytic Domain Modulates Association and Residence Time at Golgi Membranes

The Calcium Binding Loops of the Cytosolic Phospholipase A2 C2 Domain Specify Targeting to Golgi and ER in Live CellsV⃞

Membrane Tubule-mediated Reassembly and Maintenance of the Golgi Complex Is Disrupted by Phospholipase A2 Antagonists

Activation of Cytosolic Phospholipase A2 α in Resident Peritoneal Macrophages by Listeria monocytogenes Involves Listeriolysin O and TLR2 *

Cytosolic Phospholipase A2-α Mediates Endothelial Cell Proliferation and Is Inactivated by Association with the Golgi Apparatus