Literature DB >> 7589250

Participation of the NG2 proteoglycan in rat aortic smooth muscle cell responses to platelet-derived growth factor.

K A Grako1, W B Stallcup.   

Abstract

Through immunohistochemical studies we have identified the cell-surface proteoglycan, NG2, on blood vessels throughout the rat embryo. The particular cell type expressing this chondroitin sulfate proteoglycan, however, is dependent upon tissue location. Microvessels within the rat CNS express NG2 on endothelial cells, while in blood vessels outside the CNS, NG2 is found on smooth muscle cells. To analyze what role NG2 might play in these blood vessels, an enzymatic dissociation protocol was used to establish primary cultures of vascular smooth muscle cells from Postnatal Day 3 rat aorta. In this study we demonstrate the involvement of NG2 in the mitogenic and chemoattractant responses of smooth muscle cells to PDGF. In assays measuring either DNA synthesis or cell migration, treatment of smooth muscle cells with anti-NG2 immunoglobulins decreased their responses to PDGF-AA but had no effect upon their ability to react to PDGF-BB. These results support a role for NG2 in potentiating signaling through the alpha PDGF receptor in vascular smooth muscle cells. The presence of the proteoglycan on a large subpopulation of these cells could provide an enhanced response to the growth factor in times of active normal growth or in pathological conditions, such as arterial injury or atherosclerosis.

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Year:  1995        PMID: 7589250     DOI: 10.1006/excr.1995.1371

Source DB:  PubMed          Journal:  Exp Cell Res        ISSN: 0014-4827            Impact factor:   3.905


  31 in total

1.  The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the membrane-spanning proteoglycan NG2.

Authors:  D S Barritt; M T Pearn; A H Zisch; S S Lee; R T Javier; E B Pasquale; W B Stallcup
Journal:  J Cell Biochem       Date:  2000-08-02       Impact factor: 4.429

Review 2.  CSPG4, a potential therapeutic target, facilitates malignant progression of melanoma.

Authors:  Matthew A Price; Leah E Colvin Wanshura; Jianbo Yang; Jennifer Carlson; Bo Xiang; Guiyuan Li; Soldano Ferrone; Arkadiusz Z Dudek; Eva A Turley; James B McCarthy
Journal:  Pigment Cell Melanoma Res       Date:  2011-12       Impact factor: 4.693

3.  Pathological angiogenesis is reduced by targeting pericytes via the NG2 proteoglycan.

Authors:  Ugur Ozerdem; William B Stallcup
Journal:  Angiogenesis       Date:  2004       Impact factor: 9.596

4.  NG2 proteoglycan expression in mouse skin: altered postnatal skin development in the NG2 null mouse.

Authors:  Kuniko Kadoya; Jun-Ichi Fukushi; Yoshihiro Matsumoto; Yu Yamaguchi; William B Stallcup
Journal:  J Histochem Cytochem       Date:  2007-11-26       Impact factor: 2.479

5.  NG2 proteoglycan and the actin-binding protein fascin define separate populations of actin-containing filopodia and lamellipodia during cell spreading and migration.

Authors:  X H Lin; K A Grako; M A Burg; W B Stallcup
Journal:  Mol Biol Cell       Date:  1996-12       Impact factor: 4.138

Review 6.  Roles of NG2-glia in ischemic stroke.

Authors:  Fei-Er Song; Jia-Lv Huang; Si-Han Lin; Shuo Wang; Guo-Fen Ma; Xiao-Ping Tong
Journal:  CNS Neurosci Ther       Date:  2017-03-19       Impact factor: 5.243

7.  Pericyte deficiencies lead to aberrant tumor vascularizaton in the brain of the NG2 null mouse.

Authors:  Feng-Ju Huang; Weon-Kyoo You; Paolo Bonaldo; Thomas N Seyfried; Elena B Pasquale; William B Stallcup
Journal:  Dev Biol       Date:  2010-06-27       Impact factor: 3.582

8.  Adventitial pericyte progenitor/mesenchymal stem cells participate in the restenotic response to arterial injury.

Authors:  Ulrich Tigges; Masanobu Komatsu; William B Stallcup
Journal:  J Vasc Res       Date:  2012-12-18       Impact factor: 1.934

9.  Differences in tendon graft healing between the intra-articular and extra-articular ends of a bone tunnel.

Authors:  Asheesh Bedi; Sumito Kawamura; Liang Ying; Scott A Rodeo
Journal:  HSS J       Date:  2008-12-04

10.  PDGF-B-driven gliomagenesis can occur in the absence of the proteoglycan NG2.

Authors:  Marta Terrile; Irene Appolloni; Filippo Calzolari; Roberto Perris; Evelina Tutucci; Paolo Malatesta
Journal:  BMC Cancer       Date:  2010-10-12       Impact factor: 4.430

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