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The homeostasis of the plasma phosphate level is essential for many biological processes including skeletal 2265. The reabsorption of phosphate in the kidney is a major determinant of the plasma levels of phosphate. Phosphatonin is a hormone-like factor that specifically inhibits phosphate uptake in renal proximal epithelial cells.
Recent studies on tumor-induced osteomalacia suggested that phosphatonin was potentially identical to fibroblast growth factor FGF However, as purified recombinant FGF could not inhibit 282265 uptake in renal proximal epithelial cells, the iec of action of FGF remains to be elucidated. Therefore, we examined the mechanism of action of FGF in cultured renal proximal epithelial cells, opossum kidney cells.
FGF was found to require heparin-like molecules for its inhibitory activity on phosphate uptake. FGF binds to the FGF receptor 3c, which is mainly expressed in opossum kidney cells, with high affinity. Phosphate is a nutrient essential for many biological processes including skeletal mineralization and energy metabolism 1. The homeostasis of the plasma phosphate level is essential for these processes. The reabsorption of phosphate in the kidney is a major determinant of the plasma phosphate level.
PTH and 1,25 OH 2 D decrease and increase the reabsorption of phosphate in renal proximal tubules, respectively 1.
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Tumor-induced osteomalacia oce a renal phosphate-wasting disorder resulting in low serum phosphorus concentration and osteomalacia. Removal of the tumors responsible for tumor-induced osteomalacia normalizes phosphate metabolism. Recent studies on tumor-induced osteomalacia revealed that phosphatonin was potentially identical to fibroblast growth factor FGFwhich is a new member of the FGF family 235.
Autosomal dominant hypophosphataemic rickets is also a renal phosphate-wasting disorder resulting in low serum phosphorus concentration, rickets, and osteomalacia. However, as purified recombinant FGF could not inhibit phosphate uptake in renal proximal epithelial cells 3the mechanism of action of FGF on the phosphate uptake in renal proximal epithelial cells remains ic be elucidated.
Therefore, we examined the mechanism of action of FGF on phosphate transport in the cultured renal proximal epithelial cell line, opossum kidney OK cells, using purified recombinant FGF The results reported here revealed a novel mechanism of phosphate reabsorption regulated by activation of the mitogen-activated protein kinase pathway mediated by FGF signaling.
The phosphate uptake in OK cells was determined essentially according to the method described previously 6. The cultured ic were quickly washed with uptake solution containing m m Uce, 5. Phosphate uptake was initiated by addition of uptake solution supplemented with 0.
Phosphate uptake was terminated by quickly removing the uptake solution and washing three times with ice-cold stop solution containing m m NaCl and 14 m m HEPES pH 7. The nucleotide sequences of the clones were determined. Thereafter, the gel was stained with ethidium bromide. High Five insect cells infected with the recombinant baculovirus efficiently secreted recombinant FGF as described previously 5. Purified recombinant FGF was analyzed by SDS-polyacrylamide gel electrophoresis followed by both protein staining and Western blotting analysis with anti-E tag antibodies.
The observed molecular mass was essentially consistent with the calculated molecular mass of recombinant FGF 28, Da. Purified FGF was shown not to inhibit sodium-dependent phosphate uptake in the cultured renal proximal epithelial cell line, OK cells 3.
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As heparan sulfate or heparin was reported to modulate the activity of several FGFs 1216we examined the inhibitory activity of FGF in the presence of heparin.
We also examined the inhibitory activity of FGF-2 in the presence of heparin. However, FGF-2 could not inhibit phosphate uptake data not shown. OK cells were treated with different concentrations of FGF for 3 h in the presence or absence of heparin.
After treatment, phosphate uptake in OK cells was examined for 5 min.
Aafter treatment, the phosphate uptake in OK cells was examined for 5 min. Renal proximal epithelial cells were shown to preferentially express FGFR-3 Two different amino acid sequences were predicted from their nucleotide sequences.
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The sequences of major and minor clones were highly similar to those of mouse FGFR-3c and -3b 9respectively Fig. To confirm this, the amplified DNA was digested with Msp I followed by polyacrylamide gel electrophoresis.
Asterisks indicate amino acid residues identical among the sequences. The numbers indicated by arrows show the sizes of DNA fragments. In contrast to bovine serum albumin as a control data not shownthe typical binding and dissociation curves of FGF were observed, indicating that the binding was highly specific Fig.
The equilibrium dissociation was also determined. FGF was found to bind to the extracellular domain with high affinity Fig. FGF was fixed on the carboxymethyl sensor tip.
Different concentrations of the extracellular domain were used.
SU is an inhibitor specific for protein kinases of FGFR but not for those of other receptors, platelet-derived growth factor receptor, insulin receptor, and epidermal growth factor receptor 282655 After treatment, the phosphate uptake in OK cells was examined for 5 min. Administration of FGF decreased serum phosphate level in mice 3.
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These results indicated that FGF lowers serum phosphorus concentration by inhibition of phosphate reabsorption in renal epithelial cells. Therefore, these results indicated that FGF might require other molecule s for the activity or further processing to the biologically active form.
We prepared purified recombinant FGF produced by the baculovirus expression system and examined the activity of FGF However, FGF with heparin was found to significantly inhibit phosphate uptake, indicating that heparin-like molecules are essential for the activity of FGF PTH is a hormone that regulates the plasma levels of phosphate by inhibition of the reabsorption of phosphate in renal proximal tubules.
PTH also rapidly inhibited phosphate uptake in OK cells. The occupied receptors interact with guanyl nucleotide-regulated membrane-bound proteins that in turn activate membrane-bound adenylyl cyclase to convert ATP to cyclic adenosine monophosphate cAMP.
However, the mechanism of action remains to be elucidated. However, FGF could inhibit phosphate uptake in the presence of heparin but not in the absence of heparin.
FGFRs are receptor tyrosine kinases that have intrinsic protein tyrosine kinase activity and elicit tyrosine autophosphorylation of the receptors The ERK pathway generally plays roles in cell proliferation and differentiation, while the p38 pathway plays roles in cellular stress, inflammation, apoptosis, and differentiation. FGFs are local signaling molecules.
Therefore, FGF might be a hormone-like-signaling molecule. Although a variety of benign mesenchymal tumors were shown to abundantly express FGF, FGF was barely detectable in normal tissues 345. Therefore, the physiological significance of FGF remains to be elucidated. The costs of publication of this article were defrayed in part by the payment of page charges. Section solely to indicate this fact. You’ll be in good company. Journal of Lipid Research. Previous Section Next Section.
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