Loading Pathway...
Error: Pathway image not found.
Hide
Pathway Description
Gallium Nitrate Action Pathway
Homo sapiens
Drug Action Pathway
Created: 2023-08-17
Last Updated: 2023-11-27
Gallium nitrate also known as Ganite, is a nitrate salt of gallium cation used to treat cancer-related hypercalcemia. It is commonly administered intravenously and produces a hypocalcemic effect. Gallium nitrate is transported into the cell by transferrin complexes and once it accumulates within the cell it acts to inhibit ribonucleoside diphosphate reductase and v-type proton ATPase. By inhibiting ribonucleoside diphosphate reductase it halts the proliferation of cancer cells causing hypercalcemic effects. Through inhibition of v-type proton ATPase it alters some properties of the bone matrix causing more crystallization and decreasing acid secretion of osteoclasts reducing bone resorption.
References
Gallium Nitrate Pathway References
Bockman RS, Guidon PT Jr, Pan LC, Salvatori R, Kawaguchi A: Gallium nitrate increases type I collagen and fibronectin mRNA and collagen protein levels in bone and fibroblast cells. J Cell Biochem. 1993 Aug;52(4):396-403. doi: 10.1002/jcb.240520404.
Pubmed: 8227174
Bockman R: The effects of gallium nitrate on bone resorption. Semin Oncol. 2003 Apr;30(2 Suppl 5):5-12. doi: 10.1016/s0093-7754(03)00170-2.
Pubmed: 12776254
Chitambar CR: Apoptotic mechanisms of gallium nitrate: basic and clinical investigations. Oncology (Williston Park). 2004 Nov;18(13 Suppl 10):39-44.
Pubmed: 15651176
Kurten RC, Cadena DL, Gill GN: Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science. 1996 May 17;272(5264):1008-10. doi: 10.1126/science.272.5264.1008.
Pubmed: 8638121
Carlton J, Bujny M, Peter BJ, Oorschot VM, Rutherford A, Mellor H, Klumperman J, McMahon HT, Cullen PJ: Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides. Curr Biol. 2004 Oct 26;14(20):1791-800. doi: 10.1016/j.cub.2004.09.077.
Pubmed: 15498486
Rojas R, Kametaka S, Haft CR, Bonifacino JS: Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. Mol Cell Biol. 2007 Feb;27(3):1112-24. doi: 10.1128/MCB.00156-06. Epub 2006 Nov 13.
Pubmed: 17101778
Fuchs U, Rehkamp G, Haas OA, Slany R, Konig M, Bojesen S, Bohle RM, Damm-Welk C, Ludwig WD, Harbott J, Borkhardt A: The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8756-61. doi: 10.1073/pnas.121433898. Epub 2001 Jul 3.
Pubmed: 11438682
Carlton JG, Bujny MV, Peter BJ, Oorschot VM, Rutherford A, Arkell RS, Klumperman J, McMahon HT, Cullen PJ: Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport. J Cell Sci. 2005 Oct 1;118(Pt 19):4527-39. doi: 10.1242/jcs.02568.
Pubmed: 16179610
Haft CR, de la Luz Sierra M, Barr VA, Haft DH, Taylor SI: Identification of a family of sorting nexin molecules and characterization of their association with receptors. Mol Cell Biol. 1998 Dec;18(12):7278-87. doi: 10.1128/mcb.18.12.7278.
Pubmed: 9819414
Traer CJ, Rutherford AC, Palmer KJ, Wassmer T, Oakley J, Attar N, Carlton JG, Kremerskothen J, Stephens DJ, Cullen PJ: SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment. Nat Cell Biol. 2007 Dec;9(12):1370-80. doi: 10.1038/ncb1656. Epub 2007 Nov 11.
Pubmed: 17994011
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. doi: 10.1038/ng1285. Epub 2003 Dec 21.
Pubmed: 14702039
Schneider C, Owen MJ, Banville D, Williams JG: Primary structure of human transferrin receptor deduced from the mRNA sequence. Nature. 1984 Oct 18-24;311(5987):675-8. doi: 10.1038/311675b0.
Pubmed: 6090955
McClelland A, Kuhn LC, Ruddle FH: The human transferrin receptor gene: genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence. Cell. 1984 Dec;39(2 Pt 1):267-74. doi: 10.1016/0092-8674(84)90004-7.
Pubmed: 6094009
Evans P, Kemp J: Exon/intron structure of the human transferrin receptor gene. Gene. 1997 Oct 15;199(1-2):123-31. doi: 10.1016/s0378-1119(97)00356-9.
Pubmed: 9358047
Highlighted elements will appear in red.
Highlight Compounds
Highlight Proteins
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
Visualize Protein Data
Settings