Autocrine saturation of pro-urokinase receptors on human A431 cells - PubMed (original) (raw)
Autocrine saturation of pro-urokinase receptors on human A431 cells
M P Stoppelli et al. Cell. 1986.
Abstract
Single-chain pro-urokinase (pro-uPA) is present both in the medium and lysate of the A431 epidermoid carcinoma cell line. Most of the cell-associated pro-uPA is on the cell surface, as shown by indirect immunofluorescence and by surface iodination. Pro-uPA is not an integral membrane protein but is bound to a specific surface receptor that is completely saturated. A mild acid treatment uncovers the surface receptors by dissociating pro-uPA. Resaturation of uncovered receptors has been studied by reincubating cells in normal medium; within 40 min, 50% of the free sites are reoccupied. Excess uPA-specific antibodies prevent rebinding of ligand to the receptors. Thus, A431 cells first secrete uPA, which then binds to the surface receptor. We propose that the synthesis of uPA and uPA receptor by the same cell may provide a pathway for the activation of the metastatic potential of malignant cells.
Similar articles
- Regulation of human squamous cell carcinoma plasma membrane associated urokinase plasminogen activator by epidermal growth factor.
Niedbala MJ, Bajetta S, Carbone R, Sartorelli AC. Niedbala MJ, et al. Cancer Commun. 1990;2(9):317-24. Cancer Commun. 1990. PMID: 2169831 - Characterization of the cellular binding site for the urokinase-type plasminogen activator.
Estreicher A, Wohlwend A, Belin D, Schleuning WD, Vassalli JD. Estreicher A, et al. J Biol Chem. 1989 Jan 15;264(2):1180-9. J Biol Chem. 1989. PMID: 2536017 - The receptor for urokinase-plasminogen activator.
Blasi F, Stoppelli MP, Cubellis MV. Blasi F, et al. J Cell Biochem. 1986;32(3):179-86. doi: 10.1002/jcb.240320303. J Cell Biochem. 1986. PMID: 3023408 Review. - Urokinase/urokinase receptor system: internalization/degradation of urokinase-serpin complexes: mechanism and regulation.
Conese M, Blasi F. Conese M, et al. Biol Chem Hoppe Seyler. 1995 Mar;376(3):143-55. Biol Chem Hoppe Seyler. 1995. PMID: 7612191 Review.
Cited by
- Activation of pro-urokinase and plasminogen on human sarcoma cells: a proteolytic system with surface-bound reactants.
Stephens RW, Pöllänen J, Tapiovaara H, Leung KC, Sim PS, Salonen EM, Rønne E, Behrendt N, Danø K, Vaheri A. Stephens RW, et al. J Cell Biol. 1989 May;108(5):1987-95. doi: 10.1083/jcb.108.5.1987. J Cell Biol. 1989. PMID: 2523891 Free PMC article. - Increased cell-surface urokinase in advanced ovarian cancer.
Kobayashi H, Moniwa N, Sugimura M, Shinohara H, Ohi H, Terao T. Kobayashi H, et al. Jpn J Cancer Res. 1993 Jun;84(6):633-40. doi: 10.1111/j.1349-7006.1993.tb02023.x. Jpn J Cancer Res. 1993. PMID: 8340251 Free PMC article. - Urokinase (uPA) and its inhibitor PAI-1 are strong and independent prognostic factors in node-negative breast cancer.
Jänicke F, Schmitt M, Pache L, Ulm K, Harbeck N, Höfler H, Graeff H. Jänicke F, et al. Breast Cancer Res Treat. 1993;24(3):195-208. doi: 10.1007/BF01833260. Breast Cancer Res Treat. 1993. PMID: 8435475 - Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect.
Resnati M, Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F. Resnati M, et al. EMBO J. 1996 Apr 1;15(7):1572-82. EMBO J. 1996. PMID: 8612581 Free PMC article. - Urokinase receptor-dependent and -independent p56/59(hck) activation state is a molecular switch between myelomonocytic cell motility and adherence.
Chiaradonna F, Fontana L, Iavarone C, Carriero MV, Scholz G, Barone MV, Stoppelli MP. Chiaradonna F, et al. EMBO J. 1999 Jun 1;18(11):3013-23. doi: 10.1093/emboj/18.11.3013. EMBO J. 1999. PMID: 10357814 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous