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#8497852   1993/06/21 Save this To Up

Role of urokinase type plasminogen activator (u-PA) in corneal epithelial migration.

The role of plasminogen activator (PA) in the migration of corneal reepithelialization was studied. Rabbit corneal blocks were cultured, and both the extent of epithelial migration over the exposed corneal stroma and the activity of PA released into the culture media were measured. A significant, direct correlation between epithelial migration and PA activity in the medium was observed, even when the migration was stimulated by fibronectin or EGF, or was inhibited by cytochalasin B or cycloheximide. Zymography confirmed that the PA released into the culture medium was of the urokinase type (u-PA). Immunohistochemical studies showed that u-PA and plasmin(ogen) were present at the leading edge of the migrating epithelium. Studies of corneal cell cultures indicated that epithelial cells rather than endothelial cells or fibroblasts were the source of the u-PA. The addition of antihuman u-PA IgG or protease inhibitors retarded the migration of the corneal epithelium in a dose-dependent manner, indicating that u-PA activity is essential for the migration of the corneal epithelium. These findings suggest that the migration of corneal epithelial cells requires not only cell attachment to the extracellular matrix through the fibronectin but also degradation of the fibronectin by the release of cellular u-PA.

1319 related Products with: Role of urokinase type plasminogen activator (u-PA) in corneal epithelial migration.

Rat monoclonal anti mouse Mouse anti-Tissue type Pl Rat monoclonal anti mouse Rat monoclonal anti mouse Human Migration Inhibitor Interferon-a Receptor Typ Native Parainfluenza Viru Native Parainfluenza Viru Native Parainfluenza Viru Native Parainfluenza Viru Native Parainfluenza Viru Native Parainfluenza Viru

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#2452081   1988/05/31 Save this To Up

Drosophila fibronectin: a protein that shares properties similar to those of its mammalian homologue.

This is the first report on the existence in Drosophila of a protein with properties similar to those of vertebrate fibronectin that we shall refer to as Drosophila fibronectin. Rabbit antibodies against human plasma fibronectin have allowed the detection of this molecule in Drosophila haemolymph; common epitopes are shared by the two proteins. Drosophila fibronectin with a subunit mol. wt of approximately 230 kd is a glycoprotein which binds to denatured mammalian collagen. It is present throughout development and is as abundant in embryos as in larvae and adult flies. Drosophila fibronectin is differentially expressed during embryogenesis, a small amount being present before the blastoderm stage. Its concentration increases at gastrulation and reaches a steady-state value at the end of organogenesis. Drosophila fibronectin is predominantly detected by immunofluorescence on frozen sections of 16 h embryos in the extracellular spaces lying between the different tissues and organs. In mature third instar larvae, most of the staining is concentrated in fat body and imaginal discs, and the pattern strongly supports an extracellular localization of the protein. In addition, it is shown that Drosophila embryonic cells can functionally utilize vertebrate fibronectin for their spreading and differentiation. Finally, injection of antihuman plasma fibronectin antibodies in early embryos leads to the same phenotype as injection of Arg-Gly-Asp-containing peptides. This result suggests that one of the Arg-Gly-Asp-bearing protein(s) involved in gastrulation might be fibronectin.

2250 related Products with: Drosophila fibronectin: a protein that shares properties similar to those of its mammalian homologue.

TOM1-like protein 2 antib Recombinant Human IFN-alp Recombinant Human IFN-alp Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H MarkerGene™ Total Prote Rabbit Anti-Human Toll In

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#6363568   1984/03/15 Save this To Up

Fibronectin in basal cell epithelioma: sources and significance.

Nodular basal cell epitheliomas (BCE) contain fibronectin both within tumor nodules and at the nodule-stroma interface (basement membrane zone). Fibronectin within or at the periphery of tumor nodules could be derived from the tumor cells, from entrapped stroma, or from plasma. The present study was designed to elucidate the source(s) of fibronectin within BCE nodules. If stromal entrapment occurred to any great extent, von Willebrand factor VIII:Ag-stained blood vessels within tumor nodules should be evident by immunofluorescence techniques. Likewise, if plasma proteins were deposited in BCE, the tumor nodules should stain with fluorescein-conjugated antifibrinogen antibodies. Therefore, 6 basal cell epitheliomas were double labeled with rhodamine-conjugated antihuman fibronectin and fluorescein-conjugated antihuman factor VIII:Ag or fluorescein-labeled antihuman fibrinogen. Fibronectin was present in a linear disposition along the margin of tumor lobules and as a fine filamentous deposit in the central portions of tumor tissue. There was no evidence of fibrinogen or factor VIII:Ag in any of the tumor lobules. Factor VIII:Ag was present in a granular pattern within blood vessel walls that coursed between tumor nests. An indirect immunoperoxidase technique using rabbit antihuman fibronectin and peroxidase-labeled goat antirabbit IgG demonstrated that fibronectin within the central portion of the tumor lobules was closely associated with the tumor cells. The absence of fibrinogen and factor VIII:Ag within the tumor tissue indicates that the fibronectin is probably not plasma- or stroma-derived while immunoperoxidase data suggest that fibronectin may be a product of BCE cells.

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