NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin (Q24561606)

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English	NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin	scientific article

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instance of

scholarly article

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title

NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin (English)

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main subject

cell biology

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angiogenesis

1 reference

based on heuristic

inferred from title

author name string

Jun-ichi Fukushi

series ordinal

1

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Irwan T Makagiansar

series ordinal

2

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William B Stallcup

series ordinal

3

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language of work or name

English

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publication date

August 2004

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published in

Molecular Biology of the Cell

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volume

15

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issue

8

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page(s)

3580-90

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cites work

Complex interactions between the laminin alpha 4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo

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

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Integrin alphavbeta3 requirement for sustained mitogen-activated protein kinase activity during angiogenesis

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The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein

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NG2 proteoglycan is expressed exclusively by mural cells during vascular morphogenesis

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Signaling through focal adhesion kinase

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Binding of the NG2 proteoglycan to type VI collagen and other extracellular matrix molecules

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Cell contact-dependent activation of alpha3beta1 integrin modulates endothelial cell responses to thrombospondin-1

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Galectins as modulators of cell adhesion

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Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena

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The generation and characterization of a cell line derived from a sporadic renal angiomyolipoma: use of telomerase to obtain stable populations of cells from benign neoplasms

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Involvement of alpha3 integrin/tetraspanin complexes in the angiogenic response induced by angiotensin II.

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PDGF (alpha)-receptor is unresponsive to PDGF-AA in aortic smooth muscle cells from the NG2 knockout mouse

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Expression of the NG2 proteoglycan enhances the growth and metastatic properties of melanoma cells

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Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with alpha3 beta1 integrin localized at endothelial lateral junctions

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Basic fibroblast growth factor-induced angiogenic phenotype in mouse endothelium. A study of aortic and microvascular endothelial cell lines.

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27 September 2017

Aminopeptidase a is a constituent of activated pericytes in angiogenesis

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27 September 2017

Generation of truncated forms of the NG2 proteoglycan by cell surface proteolysis

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27 September 2017

A monoclonal antibody against an activation epitope on mouse integrin chain beta 1 blocks adhesion of lymphocytes to the endothelial integrin alpha 6 beta 1

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27 September 2017

The primary structure of NG2, a novel membrane-spanning proteoglycan

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Expression of the high molecular weight melanoma-associated antigen by pericytes during angiogenesis in tumors and in healing wounds.

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27 September 2017

Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain

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Vascular development: cellular and molecular regulation.

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Binding of the NG2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen).

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High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan

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NG2 is a major chondroitin sulfate proteoglycan produced after spinal cord injury and is expressed by macrophages and oligodendrocyte progenitors.

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NG2 proteoglycan promotes angiogenesis-dependent tumor growth in CNS by sequestering angiostatin.

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NG2 proteoglycan expression by pericytes in pathological microvasculature.

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Regulation of cellular adhesion to extracellular matrix proteins by galectin-3.

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Osteopontin (Eta-1) and Fibroblast Growth Factor-2 Cross-Talk in Angiogenesis

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Pericyte involvement in capillary sprouting during angiogenesis in situ

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Identifiers

DOI

10.1091/MBC.E04-03-0236

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2109831

Fatcat ID

release_ofxs2awwgbbtllkvbddmvwhnem

0 references

OpenCitations bibliographic resource ID

2109831

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2109831

PMC publication ID

491820

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2109831

PubMed publication ID

15181153

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2109831

 

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