scholarly journals Role of extracellular matrix, growth factors and proto-oncogenes in metanephric development

1997 ◽  
Vol 52 (3) ◽  
pp. 589-606 ◽  
Author(s):  
Yashpal S. Kanwar ◽  
Frank A. Carone ◽  
Anil Kumar ◽  
Jun Wada ◽  
Kosuke Ota ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Growth Factors

Role of fibrinolysis and α2-macroglobulin in growth of primary adenocarcinoma and rectal polyps.

2017 ◽  
Vol 35 (15_suppl) ◽  
pp. e15093-e15093
Author(s):  
Evgeniy N. Kolesnikov ◽  
Elena Alekseevna Nikipelova ◽  
Elena Mikhaylovna Frantsiyants ◽  
Larisa Kozlova ◽  
Irina V. Kaplieva ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Growth Factors ◽  
Protective Effect ◽  
Tumor Angiogenesis ◽  
Active Form ◽  
Primary Adenocarcinoma ◽  
Α2 Macroglobulin ◽  
Rectal Polyps ◽  
Resection Line

e15093 Background: An important role in tumor angiogenesis induction is played by hydrolytic systems, in particular plasmin one which provides degradation of the extracellular matrix, activates growth factors and metalloproteinases. Our purpose was to analyze the tissue fibrinolytic system and α2-macroglobulin (α2M) in primary adenocarcinoma (PA) and polyps (P) of the rectum (R). Methods: Tissues of tumors (РА, G2, T2-3N0M0, 42-73 years) and their perifocal zone (PZ) in R (n = 24) and Р (n = 27) were studied by ELISA; the result was calculated per 1 mg of tissue. Results: Resection line (RL) tissues contained levels of tРА antigen and its active form (tРА-Ag and tРА-act) 6.7 and 33.8 times higher than prourokinase and urokinase levels (uPA-Ag and uPA-act). RL tissues in P did not differ significantly from R tissues at PA resection. uPA-act in PA was higher than in RL by 3.2 times, uPA-Ag - 8 times higher, tРА-act - 2.3 times lower; tPA-Ag was similar to RL tissue values. Plasmin-α2-antiplasmin complex (PAP) in PA was 1.4 times higher than in RL. Plasminogen (PG) in PA was 1.5 times lower than in RL (p < 0.01). Activity of α2M in PA and RL did not differ. PAP and α2М in PA PZ were similar to RL, and PG did not differ from PA. Other indices were between tumor and RL levels. P tissue did not show changes in uPA; tPA-act activity was 1.3 times lower than in RL, and tPA-Ag 1.3 times higher (p < 0.01). PAP in tissues of 88.2% P was 1.5 times higher than in RL and 1.7 times lower than in PA. PG and α2М were similar in P and RL. PAP in PZ of P was 2.3 times higher than in RL and 1.5 times higher than in PA PZ. PG in P PZ was 1.4 times lower than in RL (p < 0.01). α2М activity in P PZ was higher than in RL and P by 5.4 times on average. uPA in P PZ did not differ from RL; tРА-Ag and tРА-act were higher than in RL by 1.5 and 1.9 times and exceeded P by 2.1 and 1.5 times (p < 0.01). Prevalence of uPA, activation of PG in PA and its PZ indicated degradation of the extracellular matrix compared with the corresponding P tissues. Conclusions: The role of R tumor PZ as a "metabolic" tumor field in neoplasm progression was confirmed. Activation of fibrinolysis in PA and its PZ with a deficiency of inhibitors stimulates the migration and proliferation of cells. Increasing tРА, РАР and α2М in PZ of polyps has a protective effect.

scholarly journals The Role of Glypicans in Cancer Progression and Therapy

2020 ◽  
Vol 68 (12) ◽  
pp. 841-862 ◽  
Author(s):  
Nan Li ◽  
Madeline R. Spetz ◽  
Mitchell Ho
Keyword(s):  
Extracellular Matrix ◽  
Cell Proliferation ◽  
Growth Factors ◽  
Heparan Sulfate ◽  
Cancer Progression ◽  
Core Protein ◽  
Heparan Sulfate Proteoglycans ◽  
Glycosylphosphatidylinositol Anchor ◽  
Multiple Ligands

Glypicans are a family of heparan sulfate proteoglycans that are attached to the cell membrane via a glycosylphosphatidylinositol anchor. Glypicans interact with multiple ligands, including morphogens, growth factors, chemokines, ligands, receptors, and components of the extracellular matrix through their heparan sulfate chains and core protein. Therefore, glypicans can function as coreceptors to regulate cell proliferation, cell motility, and morphogenesis. In addition, some glypicans are abnormally expressed in cancers, possibly involved in tumorigenesis, and have the potential to be cancer-specific biomarkers. Here, we provide a brief review focusing on the expression of glypicans in various cancers and their potential to be targets for cancer therapy.

The role of growth factors and extracellular matrix in wound healing following laryngotracheal reconstruction

1997 ◽  
Vol 117 (2) ◽  
pp. P82-P82
Author(s):  
D WALNER ◽  
S HEFFELFINGER ◽  
M ABRAMS ◽  
M MILLER ◽  
R COTTON ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Wound Healing ◽  
Growth Factors ◽  
Laryngotracheal Reconstruction

scholarly journals αv-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation

2020 ◽  
Vol 219 (12) ◽  
Author(s):  
María Benito-Jardón ◽  
Nico Strohmeyer ◽  
Sheila Ortega-Sanchís ◽  
Mitasha Bharadwaj ◽  
Markus Moser ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Growth Factors ◽  
Binding Sites ◽  
Mouse Genetics ◽  
Dependent Manner ◽  
Rgd Motif ◽  
Cell Force ◽  
Deficient Mice

Fibronectin (FN) is an essential glycoprotein of the extracellular matrix; binds integrins, syndecans, collagens, and growth factors; and is assembled by cells into complex fibrillar networks. The RGD motif in FN facilitates cell binding­ and fibrillogenesis through binding to α5β1 and αv-class integrins. However, whether RGD is the sole binding site for αv-class integrins is unclear. Most notably, substituting aspartate with glutamate (RGE) was shown to eliminate integrin binding in vitro, while mouse genetics revealed that FNRGE preserves αv-class integrin binding and fibrillogenesis. To address this conflict, we employed single-cell force spectroscopy, engineered cells, and RGD motif–deficient mice (Fn1ΔRGD/ΔRGD) to search for additional αv-class integrin–binding sites. Our results demonstrate that α5β1 and αv-class integrins solely recognize the FN-RGD motif and that αv-class, but not α5β1, integrins retain FN-RGE binding. Furthermore, Fn1ΔRGD/ΔRGD tissues and cells assemble abnormal and dysfunctional FNΔRGD fibrils in a syndecan-dependent manner. Our data highlight the central role of FN-RGD and the functionality of FN-RGE for αv-class integrins.

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