Occurrence, biochemical profile of vascular endothelial growth factor (VEGF) isoforms and their functions in endochondral ossification

2012 ◽  
Vol 227 (4) ◽  
pp. 1298-1308 ◽  
Author(s):  
A.S. Patil ◽  
R.B. Sable ◽  
R.M. Kothari
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Endochondral Ossification ◽  
Vascular Endothelial ◽  
Biochemical Profile ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms

scholarly journals Expression of Vascular Endothelial Growth Factor (VEGF) Isoforms VEGFxxxb in Normal Human Renal Development

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Heather Samantha Bevan ◽  
Nynke N.M.S van den Akker ◽  
Japke A.E Polman ◽  
Steve J Harper ◽  
Adriana C Gittenberger‐de Groot ◽  
...  
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Renal Development ◽  
Vascular Endothelial ◽  
Normal Human ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms

scholarly journals The vascular endothelial growth factor (VEGF) isoforms: differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF.

1993 ◽  
Vol 4 (12) ◽  
pp. 1317-1326 ◽  
Author(s):  
J E Park ◽  
G A Keller ◽  
N Ferrara
Keyword(s):  
Extracellular Matrix ◽  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Vascular Endothelial ◽  
Vegf Mrna ◽  
Angiogenic Potential ◽  
Molecular Masses ◽  
Matrix Bound ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms

Vascular endothelial growth factor (VEGF)mRNA undergoes alternative splicing events that generate four different homodimeric isoforms, VEGF121, VEGF165, VEGF189, or VEGF206. VEGF121 is a nonheparin-binding acidic protein, which is freely diffusible. The longer forms, VEGF189 or VEGF206, are highly basic proteins tightly bound to extracellular heparin-containing proteoglycans. VEGF165 has intermediate properties. To determine the localization of VEGF isoforms, transfected human embryonic kidney CEN4 cells expressing VEGF165, VEGF189, or VEGF206 were stained by immunofluorescence with a specific monoclonal antibody. The staining was found in patches and streaks suggestive of extracellular matrix (ECM). VEGF165 was observed largely in Golgi apparatus-like structures. Immunogold labeling of cells expressing VEGF189 or VEGF206 revealed that the staining was localized to the subepithelial ECM. VEGF associated with the ECM was bioactive, because endothelial cells cultured on ECM derived from cells expressing VEGF189 or VEGF206 were markedly stimulated to proliferate. In addition, ECM-bound VEGF can be released into a soluble and bioactive form by heparin or plasmin. ECM-bound VEGF189 and VEGF206 have molecular masses consistent with the intact polypeptides. The ECM may represent an important source of VEGF and angiogenic potential.

Cell migration and growth induced by photo-immobilised vascular endothelial growth factor (VEGF) isoforms

2019 ◽  
Vol 7 (27) ◽  
pp. 4272-4279 ◽  
Author(s):  
Xueli Ren ◽  
Jun Akimoto ◽  
Hideyuki Miyatake ◽  
Seiichi Tada ◽  
Liping Zhu ◽  
...  
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Cell Migration ◽  
Growth Factor ◽  
Vascular Endothelial ◽  
Cell Migration And Proliferation ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms

VEGF isoforms immobilised by photo-reactive gelatin (AzPhe-gelatin) enhance cell migration and proliferation.

Effect of Tibolone and its metabolites on vascular endothelial growth factor (VEGF) isoforms 121 and 165 in ishikawa cells

2002 ◽  
Vol 78 ◽  
pp. S159-S160
Author(s):  
Sebastian Mirkin ◽  
Susan Leslie ◽  
Michelle Billeter ◽  
Mary C Mahony ◽  
David F Archer
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Vascular Endothelial ◽  
Ishikawa Cells ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms

Addition of a c-myc epitope tag within the VEGF protein does not affect in vitro biological activity

2001 ◽  
Vol 79 (1) ◽  
pp. 107-112 ◽  
Author(s):  
Olivier Chavand ◽  
Katrina Spilsbury ◽  
Piroska E Rakoczy
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Retinal Pigment ◽  
Retinal Pigment Epithelial Cells ◽  
Endothelial Cell Proliferation ◽  
Vascular Endothelial ◽  
Heparin Binding ◽  
Epitope Tag ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms

The overexpression of vascular endothelial growth factor (VEGF) has been strongly implicated in diseases involving neovascularization. VEGF exists in as many as six different isoforms, each showing a unique pattern of tissue distribution and activity. To investigate the effect of individual VEGF isoform overexpression in neovascular disease models, we inserted c-myc epitope tags into the three VEGF isoforms expressed in retinal pigment epithelial cells, VEGF121, VEGF165, and VEGF189. We found that the 12-amino acid insertion between the receptor binding and heparin binding domains did not affect VEGF transcription, translation, or secretion. In addition, VEGF isoforms containing the c-myc epitope tag were able to stimulate endothelial cell proliferation as efficiently as non-tagged VEGF isoforms and they could be individually identified by Western blotting and immunocytochemistry using the c-myc epitope specific monoclonal antibody 9E10.Key words: Vascular endothelial growth factor, VEGF, c-myc epitope tag, immunocytochemistry.

Effects of Vascular Endothelial Growth Factor (VEGF) Isoforms on Rat Testis Composition and Germ Cell Numbers.

2009 ◽  
Vol 81 (Suppl_1) ◽  
pp. 20-20
Author(s):  
Ningxia Lu ◽  
Shantille Kruse ◽  
Racheal Slattery ◽  
Debra Clopton ◽  
Andrea S. Cupp
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Germ Cell ◽  
Vascular Endothelial ◽  
Cell Numbers ◽  
Rat Testis ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms

Decreased cardiac expression of vascular endothelial growth factor and redox imbalance in murine diabetic cardiomyopathy

2009 ◽  
Vol 297 (2) ◽  
pp. H829-H835 ◽  
Author(s):  
Bing Han ◽  
Reshma Baliga ◽  
Hong Huang ◽  
Peter J. Giannone ◽  
John Anthony Bauer
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Type 1 Diabetes ◽  
Growth Factor ◽  
Vascular Endothelial ◽  
Redox Imbalance ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms ◽  
Fractional Shortening ◽  
Microvascular Rarefaction

Type 1 diabetes is associated with a unique form of cardiomyopathy that is present without atherosclerosis. Redox imbalance and/or changes in vascular endothelial growth factor (VEGF) expression have been associated with diabetes-related cardiomyopathy. However, the mechanisms of these changes and their interrelationships remain unclear. Using a murine type 1 diabetes model, we tested the hypothesis that alterations in cardiac performance are associated with decreased cardiac microvascular prevalence, as well as downregulation of VEGF isoforms. We also investigated oxidative stress as a contributor to regulate individual VEGF isoforms and microvascular rarefaction. Significant and rapid hyperglycemia was observed at 1 wk post-streptozotocin (STZ) and persisted throughout the 5-wk study. Left ventricular (LV) fractional shortening was reduced at week 1 and 5 post-STZ insult relative to age-matched controls. We also observed the early reduction in E/A ratio at 1 wk. Immunostaining for CD31 and digital image analysis demonstrated a 35% reduction in microvessels/myocardial area, indicative of rarefaction, which was highly correlated with fractional shortening. Furthermore, a significant increase in the prevalence of protein 3-nitrotyrosine was observed in the diabetic cardiac tissue, which was inversely associated with microvascular rarefaction. The expressions of three VEGF isoforms were significantly reduced to different extents. The reduction of VEGF164 was associated with GSSG accumulation. These data demonstrate that the mouse model of STZ-induced diabetes has hallmark features observed in humans with respect to nonischemic systolic and diastolic performance and microvascular rarefaction, which are associated with changes in VEGF isoform expression and redox imbalance in the myocardium.

scholarly journals VEGF: an Essential Mediator of Both Angiogenesis and Endochondral Ossification

2007 ◽  
Vol 86 (10) ◽  
pp. 937-950 ◽  
Author(s):  
J. Dai ◽  
A.B.M. Rabie
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Heparan Sulfate ◽  
Endochondral Ossification ◽  
Transforming Growth Factor ◽  
Heparan Sulfate Proteoglycans ◽  
Vascular Endothelial ◽  
Biological Functions ◽  
Placenta Growth Factor ◽  
Endothelial Growth Factor

During bone growth, development, and remodeling, angiogenesis as well as osteogenesis are closely associated processes, sharing some essential mediators. Vascular endothelial growth factor (VEGF) was initially recognized as the best-characterized endothelial-specific growth factor, which increased vascular permeability and angiogenesis, and it is now apparent that this cytokine regulates multiple biological functions in the endochondral ossification of mandibular condylar growth, as well as long bone formation. The complexity of VEGF biology is paralleled by the emerging complexity of interactions between VEGF ligands and their receptors. This narrative review summarizes the family of VEGF-related molecules, including 7 mammalian members, namely, VEGF, placenta growth factor (PLGF), and VEGF-B, -C, -D, -E, and -F. The biological functions of VEGF are mediated by at least 3 corresponding receptors: VEGFR-1/Flt-1, VEGFR-2/Flk-1, VEGFR-3/Flt-4 and 2 co-receptors of neuropilin (NRP) and heparan sulfate proteoglycans (HSPGs). Current findings on endochondral ossification are also discussed, with emphasis on VEGF-A action in osteoblasts, chondroblasts, and chondroclasts/osteoclasts and regulatory mechanisms involving oxygen tension, and some growth factors and hormones. Furthermore, the therapeutic implications of recombinant VEGF-A protein therapy and VEGF-A gene therapy are evaluated. Abbreviations used: VEGF, Vascular endothelial growth factor; PLGF, placenta growth factor; NRP, neuropilin; HSPGs, heparan sulfate proteoglycans; FGF, fibroblast growth factor; TGF, transforming growth factor; HGF, hepatocyte growth factor; TNF, tumor necrosis factor; ECM, extracellular matrix; RTKs, receptor tyrosine kinases; ERK, extracellular signal kinases; HIF, hypoxia-inducible factor

Effect of the luteinising hormone surge on regulation of vascular endothelial growth factor and extracellular matrix-degrading proteinases and their inhibitors in bovine follicles

2008 ◽  
Vol 20 (2) ◽  
pp. 258 ◽  
Author(s):  
Bajram Berisha ◽  
Martin Steffl ◽  
Harald Welter ◽  
Heike Kliem ◽  
Heinrich H. D. Meyer ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Plasminogen Activator ◽  
Luteinising Hormone ◽  
Experimental Period ◽  
Vascular Endothelial ◽  
Endothelial Growth Factor ◽  
Vegf Isoforms ◽  
Pai 1

The aim of the present study was to evaluate the pattern of regulation of vascular endothelial growth factor (VEGF)-A (isoforms 121, 165, 189), VEGF receptor tyrosine kinases (VEGF-R1 and VEGF-R2), matrix metalloproteinase (MMP)-1, MMP-2, MMP-14, MMP-19, tissue-specific inhibitor of metalloproteinases (TIMP)-1, TIMP-2, tissue plasminogen activator (tPA), urokinase plasminogen activator (uPA), urokinase plasminogen activator receptor (uPAR) and plasminogen activator inhibitor-1 (PAI-1) in time-defined follicle classes before (0 h) and after the application of gonadotrophin-releasing hormone (GnRH). Bovine ovaries containing periovulatory follicles or new corpora lutea (CL; Days 1–2) were collected 0, 4, 10, 20 and 25 h (follicles) or 60 h (CL) after the injection of GnRH. Transcripts of VEGF isoforms (VEGF121, VEGF165, VEGF189) were upregulated 4 h after GnRH injection (during the luteinising hormone (LH) surge) and decreased thereafter to lowest levels around ovulation. All VEGF isoforms and their receptors were upregulated again after ovulation. The VEGF peptide concentration in follicular fluid decreased 20 h after GnRH injection, followed by an increase in follicles 25 h after GnRH. Expression of MMP-1 mRNA increased rapidly 4 h after GnRH injection and remained high during the entire experimental period. In contrast, MMP-19 mRNA increased significantly only after ovulation. Expression of TIMP-1 mRNA increased 4 h after GnRH and again after ovulation. Expression of tPA mRNA increased 4 h after GnRH and remained high during the entire experimental period, whereas expression of uPA transcripts increased significantly only after ovulation. Both uPAR and PAI-1 mRNA levels increased in follicles 4 h after GnRH and again after ovulation. The amount of MMP-1 protein (immunolocalisation) increased in follicles 10 h after GnRH: additional staining was observed in the granulosa cell layer. In conclusion, the temporal and spatial pattern of regulation of VEGF and extracellular matrix-degrading proteinases during periovulation suggests they are important mediators of the LH-dependent rupture of bovine follicles and for early CL formation (angiogenesis).

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