13 entries found for : it-38
Roles of the FGF-FGFR signaling system in cancer development and inflammation
Wiedlocha A, Haugsten EM, Zakrzewska M (2021) Roles of the FGF-FGFR signaling system in cancer development and inflammation. Cells 10(9):2231. doi: 10.3390/cells10092231Objective: To highlight the latest advances in understanding the role of the FGF-FGFR signaling system in the development of neoplastic diseases and in the induction and maintenance of inflammation and its sequelae.
Related Products: FGF-SAP (Cat. #IT-38)
Vikan AK, Kostas M, Haugsten EM, Selbo PK, Wesche J (2021) Efficacy and selectivity of FGF2-saporin cytosolically delivered by PCI in cells overexpressing FGFR1. Cells 10(6):1476. doi: 10.3390/cells10061476Summary: Fibroblast growth factor receptors (FGFRs) have become an attractive target in cancer research and therapy due to their implication in several cancers. The authors evaluated the efficacy and selectivity of PCI of FGF2-saporin (FGF-SAP) in cells overexpressing FGFR1. The authors conclude that to prevent off-target effects of FGF-based toxins, it will be necessary to circumvent binding to HSPGs, for example by mutating the binding site of FGF2 to HSPGs.
Related Products: FGF-SAP (Cat. #IT-38)
Glycosylation mutants of cultured mammalian cells
Esko JD, Stanley P (2017) Glycosylation mutants of cultured mammalian cells. (eds. Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Darvill AG, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger PH). In: Essentials of Glycobiology Chapter 49. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press doi: 10.1101/glycobiology.3e.049 Related Products: FGF-SAP (Cat. #IT-38)
Method for confirming cytoplaintratumoral anti-HuD immunotoxinsmic delivery of RNA aptamers.
Dickey D, Thomas G, Dassie J, Giangrande P (2016) Method for confirming cytoplaintratumoral anti-HuD immunotoxinsmic delivery of RNA aptamers. (eds. Shum K, Rossi J). In: SiRNA Delivery Methods. Methods in Molecular Biology. 1364:209-217. Humana Press, New York, NY. doi: 10.1007/978-1-4939-3112-5_17
Objective: To describe a functional assay (RIP assay) to confirm cellular uptake and subsequent cytoplasmic release of an RNA aptamer which binds to a cell surface receptor expressed on prostate cancer cells (PSMA).
Summary: This publication details an in vitro functional assay to confirm that the aptamer retains function following conjugation to saporin and describe a cellular assay to measure aptamer-mediated saporin-induced cytotoxicity.
Usage: The folded biotinylated aptamer was mixed at a 1:4 molar ratio of Streptavidin-ZAP, confirmed by agarose gel, a PSMA enzymatic activity (NAALADase) assay performed. FGF-SAP was used as a control.
Related Products: Streptavidin-ZAP (Cat. #IT-27), FGF-SAP (Cat. #IT-38)
Methods for evaluating cell-specific, cell-internalizing RNA aptamers.
Hernandez L, Flenker K, Hernandez F, Klingelhutz A, McNamara J, Giangrande P (2013) Methods for evaluating cell-specific, cell-internalizing RNA aptamers. Pharmaceuticals (Basel) 6:295-319. doi: 10.3390/ph6030295
Objective: Isolate aptamers that internalize upon binding to their cognate receptor on the cell surface
Summary: Among the methods used to characterize aptamers that internalize is a way to monitor for cytoplasmic delivery using the ribosome inactivating protein-based (RNA-RIP) assay. Biotin-labeled A9g was conjugated to streptavidin-modified saporin (streptavidin-ZAP). First, it was verified that conjugation of biotinylated aptamer to Streptavidin-ZAP (A9g-SAP) did not affect the inhibitory effect of the aptamer. Next, the effect was examined of A9g-SAP on PC3(PSMA+) and PC3(PSMA-) cells. Cells were treated with varying amounts of aptamer-saporin conjugate for 72 h at 37°C and then an assay was performed to determine potential cytotoxicity of the conjugate. Results confirm that A9g is internalized preferentially into target cells and that A9g is efficiently accessing the cytoplasm of target cells possibly through a mechanism of endosomal escape, resulting in inhibition of protein synthesis and ultimate cell-death. FGF-SAP was used as a control.
Related Products: Streptavidin-ZAP (Cat. #IT-27), FGF-SAP (Cat. #IT-38)
Vascular smooth cell proliferation in perfusion culture of porcine carotid arteries.
Liao D, Lin PH, Yao Q, Chen C (2008) Vascular smooth cell proliferation in perfusion culture of porcine carotid arteries. Biochem Biophys Res Commun 372(4):668-673. doi: 10.1016/j.bbrc.2008.05.117
Summary: Basic fibroblast growth factor is highly effective in stimulating smooth muscle cell (SMC) proliferation. The authors used FGF-SAP (Cat. #IT-38) to help characterize a model of vascular SMC proliferation with porcine carotid arteries. Arteries isolated from pigs were cultured under several different conditions, one of which included FGF-SAP at a concentration of 0.4 nM. In all cases the arteries maintained viability for up to 96 hours. SMC proliferation was drastically reduced in the arteries treated with FGF-SAP. [Note, FGF-SAP is not ATS.]
Related Products: FGF-SAP (Cat. #IT-38)
Davol P, Frackelton AR Jr (1996) The mitotoxin, basic fibroblast growth factor-saporin, effectively targets human prostatic carcinoma in an animal model. J Urol 156(3):1174-1179. doi: 10.1016/s0022-5347(01)65745-8
Related Products: FGF-SAP (Cat. #IT-38)
Davol P, Beitz JG, Mohler M, Ying W, Cook J, Lappi DA, Frackelton AR Jr (1995) Saporin toxins directed to basic fibroblast growth factor receptors effectively target human ovarian teratocarcinoma in an animal model. Cancer 76(1):79-85. doi: 10.1002/1097-0142(19950701)76:1<79::aid-cncr2820760111>3.0.co;2-g
Related Products: FGF-SAP (Cat. #IT-38)
David T, Tassin J, Lappi DA, Baird A, Courtois Y (1992) Biphasic effect of the mitotoxin bFGF-saporin on bovine lens epithelial cell growth: effect of cell density and extracellular matrix. J Cell Physiol 153:483-490. doi: 10.1002/jcp.1041530307
Related Products: FGF-SAP (Cat. #IT-38)
Antitumor activity of basic fibroblast growth factor-saporin mitotoxin in vitro and in vivo.
Beitz JG, Davol P, Clark JW, Kato J, Medina M, Frackelton AR Jr, Lappi DA, Baird A, Calabresi P (1992) Antitumor activity of basic fibroblast growth factor-saporin mitotoxin in vitro and in vivo. Cancer Res 52:227-230.
Related Products: FGF-SAP (Cat. #IT-38)
Gonzalez AM, Lappi DA, Buscaglia ML, Carman LS, Gage FH, Baird A (1991) Basic FGF-SAP mitotoxin in the hippocampus. Specific lethal effect on cells expressing the basic FGF receptor. Ann N Y Acad Sci 638:442-444. doi: 10.1111/j.1749-6632.1991.tb49064.x
Related Products: FGF-SAP (Cat. #IT-38)
Role of basic fibroblast growth factor in vascular lesion formation.
Lindner V, Lappi DA, Baird A, Majack RA, Reidy MA (1991) Role of basic fibroblast growth factor in vascular lesion formation. Circ Res 68:106-113. doi: 10.1161/01.res.68.1.106
Related Products: FGF-SAP (Cat. #IT-38)
Beattie GM, Lappi DA, Baird A, Hayek A (1990) Selective elimination of fibroblasts from pancreatic islet monolayers by basic fibroblast growth factor-saporin mitotoxin. Diabetes 39:1002-1005. doi: 10.2337/diab.39.8.1002
Related Products: FGF-SAP (Cat. #IT-38)