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HUMAN FIBRONECTIN alpha-CHYMOTRYPTIC FRAGMENT 40kDa (heparin-binding) PURIFIED PROTEIN- 2952565
Document Type:

Certificate of Analysis
Lot Number:

2952565

Product Catalog Number:

F1903
Product Catalog Name:

Fibronectin 40 kDa α Chymotryptic Fragment (Heparin-binding region), Human purified
The fibronectin receptor alpha5 integrin subunit is upregulated by cell-cell adhesion via a cyclic AMP-dependent mechanism: implications for human trophoblast migration.
Cell adhesion molecules are implicated in the mechanisms regulating trophoblast migration during human embryo implantation and placentation. We investigated the expression and subcellular organization of the fibronectin receptor alpha5 integrin subunit during the differentiation of human trophoblasts in vitro, and the role of cyclic adenosine monophosphate (cAMP) in the process. Human trophoblasts isolated from chorionic villi expressed no alpha5 integrin, but the molecule was upregulated as cells aggregated in vitro. Low levels of expression of alpha5 integrin subunit and a diffuse cellular distribution pattern were seen in migrating mononuclear trophoblasts. Formation of cell aggregates was accompanied by increased expression of the alpha5 integrin, which translocated to the cytoskeleton-bound pool of proteins and clustered within focal adhesion plaques on the cell surface. This coincided with increased binding to fibronectin. In the absence of cell-cell adhesion, trophoblasts did not display an increase in alpha5 integrin messenger RNA or protein and there was no alpha5 integrin in focal adhesion plaques, suggesting that cell-cell contacts specifically trigger the upregulation of alpha5 integrin subunit and its subcellular translocation. Cyclic AMP is the second messenger mediating the aggregation-induced increase in alpha5 integrin: cAMP increased the de novo synthesis of alpha5 integrin protein, particularly in mononuclear cells, whereas the aggregation-induced increase in alpha5 integrin was strongly inhibited by the antagonist Rp-cAMP in aggregating cells. Our data provide evidence that the alpha5 integrin mediates binding of human trophoblasts to fibronectin and is implicated in the regulation of trophoblast migration. This integrin's expression is specifically triggered by cell-cell adhesion and regulated via cAMP-mediated pathway(s). It is hypothesized that these mechanisms may play an important role in the molecular events controlling human placentation.
Document Type:

Reference

Product Catalog Number:

AB1928
Product Catalog Name:

Anti-Integrin α5 Antibody, CT, Intracellular
HUMAN FIBRONECTIN alpha-CHYMOTRYPTIC FRAGMENT 40kDa (heparin-binding) PURIFIED PROTEIN - 2382066
Document Type:

Certificate of Analysis
Lot Number:

2382066

Product Catalog Number:

F1903
Product Catalog Name:

Fibronectin 40 kDa α Chymotryptic Fragment (Heparin-binding region), Human purified
HUMAN FIBRONECTIN alpha-CHYMOTRYPTIC FRAGMENT 40kDa (heparin-binding) PURIFIED PROTEIN - 3752737
Document Type:

Certificate of Analysis
Lot Number:

3752737

Product Catalog Number:

F1903
Product Catalog Name:

Fibronectin 40 kDa α Chymotryptic Fragment (Heparin-binding region), Human purified
HUMAN FIBRONECTIN alpha-CHYMOTRYPTIC FRAGMENT 40kDa (heparin-binding) PURIFIED PROTEIN -2488809
Document Type:

Certificate of Analysis
Lot Number:

2488809

Product Catalog Number:

F1903
Product Catalog Name:

Fibronectin 40 kDa α Chymotryptic Fragment (Heparin-binding region), Human purified
Fetal fibronectin signaling induces matrix metalloproteases and cyclooxygenase-2 (COX-2) in amnion cells and preterm birth in mice.
Fetal fibronectin (fFN) in cervical and vaginal secretions has been used as a predictor of preterm delivery. Here, we clarified the pathological function of fFN on cell type-specific matrix metalloproteinases (MMPs) and prostaglandin synthesis in fetal membranes. Treatment of amnion mesenchymal cells with fFN resulted in dramatic increases in MMP-1 and MMP-9 mRNA and enzymatic activity as well as COX-2 mRNA and prostaglandin E(2) synthesis, activating both NFκB and ERK1/2 signaling. Fetal FN-induced increases in MMPs and COX-2 were mediated through its extra domain A and Toll-like receptor 4 expressed in mesenchymal cells. Lipopolysaccharide and TNF-α increased the release of free FN in medium of amnion epithelial cells in culture. Finally, injection of fFN in pregnant mice resulted in preterm birth. Collectively, these results indicate that fFN is not only a marker of preterm delivery but also plays a significant role in the pathogenesis of preterm labor and premature rupture of fetal membranes.
Document Type:

Reference

Product Catalog Number:

AB1945
Fibronectin, human cellular - 21673
Document Type:

Certificate of Analysis
Lot Number:

21673
HUMAN FIBRONECTIN alpha-CHYMOTRYPTIC FRAGMENT 40kDa (heparin-binding) - 3934925
Document Type:

Certificate of Analysis
Lot Number:

3934925

Product Catalog Number:

F1903
Product Catalog Name:

Fibronectin 40 kDa α Chymotryptic Fragment (Heparin-binding region), Human purified
Fibronectin fragments and blocking antibodies to alpha2beta1 and alpha5beta1 integrins stimulate mitogen-activated protein kinase signaling and increase collagenase 3 (ma ...
OBJECTIVE: To determine if integrin-mediated signaling results in activation of chondrocyte mitogen-activated protein (MAP) kinases that lead to increased expression of matrix metalloproteinase 13 (MMP-13; collagenase 3), a potent mediator of cartilage matrix degradation. METHODS: Human articular chondrocytes isolated from normal ankle and knee cartilage obtained from tissue donors were cultured in monolayers. The cells were treated with a 120-kd fibronectin fragment (FN-f) that binds the alpha5beta1 integrin or with antibodies to specific integrin receptors. Activation of MAP kinases was determined by immunoblotting with phosphospecific antibodies. MMP production was measured by gelatin zymography, and MMP-13 production and activation were determined by immunoblotting and by a fluorogenic peptide assay. RESULTS: Human articular chondrocytes were found to respond to the 120-kd FN-f and to adhesion-blocking antibodies to the alpha2beta1 and alpha5beta1 integrins with increased phosphorylation of the extracellular signal-regulated kinase 1 (ERK1)/ERK2, c-Jun N-terminal kinase (JNK), and p38 MAP kinases. Intact FN and integrin-blocking antibodies to alpha1, alpha3, and alphaVbeta3 and a nonblocking alpha5 antibody had no effect. After MAP kinase activation, increased phosphorylation of c-Jun and the nuclear factor kappaB inhibitor was noted, followed by increased pro- and activated MMP-13 in the conditioned media. Inhibitors of mitogen-activated protein kinase kinase, p38, and JNK were each able to inhibit increased MMP-13 production, while the interleukin-1 receptor antagonist (IL-1Ra) protein did not. However, the IL-1Ra partially inhibited FN-f-induced activation of MMP-13. CONCLUSION: Integrin-mediated MAP kinase signaling stimulated by FN-f is associated with increased production and release of pro- and active MMP-13. Autocrine production of IL-1 appears to result in additional MMP-13 activation. These processes may play a key role in feedback loops responsible for progressive cartilage degradation in arthritis.
Document Type:

Reference

Product Catalog Number:

AB1999
Fibronectin: purification, immunochemical properties, and biological activities.
Document Type:

Reference

Product Catalog Number:

Multiple
Product Catalog Name:

Multiple