Summary
Saruplase — a recombinant single-chain urokinase-type plasminogen activator was identified immunohistochemically in normal rat tissue after intravenous administration by means of a polyclonal antibody. For this purpose, rat tissues were fixed in various ways (liquid nitrogen, ethanol, formaldehyd solution). Saruplase could be detected by the PAP method, streptavidinbiotin system and indirect immunofluorescence in the kidney (proximal tubule), liver (hepatocytes, Kupffer cells) and spleen (reticular cells). Saruplase was not localized in the rat endothelium. It is discussed that the ratspecific receptors for urokinase-type plasminogen activator on endothelial cells cannot bind Saruplase due to the extreme species specificity.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Barnathan ES, Kuo A, Rosenfeld L, Kariko K, Leski M, Robbiati F, Nolli ML, Henkin J, Cines DB (1990) Interaction of single-chain urokinase-type plasminogen activator with human endothelial cells. J Biol Chem 265:2865–2872
Blasi F (1988) Surface receptors for urokinase plasminogen activator. Fibrinolysis 2:73–84
Coggi G, Dell'Orto P, Viale G (1986) Avidin-biotin methods. In: Polak JM, Van Norden S (eds) Immunocytochemistry, modern methods and applications. Wright & Sons, Bristol, pp 54–70
Collen D, Stump D, Van de Werf F, Jang IK, Nobuhara M, Lijnen HR (1985) Coronary thrombolysis in dogs with intravenously administered human pro-urokinase. Circulation 72:384–388
Coons AH, Creech HJ, Jones RN (1941) Immunological properties of an antibody containing a fluorescent group. Proc Soc Exp Biol Med 47:200–202
Flohé L, Frankus E, Friderichs E, Giertz H, Günzler WA, Hanbücken FW, Hennies HH, Henninger W, Kim SMA, Ötting F, Schneider J, Steffens GF (1988) Selective fibrinolysis produced by human pro-urokinase obtained from recombinant E.-coli bacteria. In: Breddin K, Groß D, Rilger H (Hrsg.) Angiologie und Hämostaseologie. Fischer, Stuttgart New York, S 267–270
Graham RC, Karnovsky MJ (1966) The early states of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique. J Histochem Cytochem 14:291–302
Grøndahl-Hansen J, Kirkeby LT, Ralfkiar E, Kristensen P, Lund LR, Danø K (1989) Urokinase-type plasminogen activator in endothelial cells during acute inflammation of the appendix. Am J Pathol 135:631–636
Hajjar KA, Hamel NM (1990) Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase. J Biol Chem 265:2908–2916
Hanbrücken FW, Schneider J, Günzler WA, Friderichs E, Giertz H, Flohé L (1987) Selective fibrinolytic activity of recombinant non-glycosylated human pro-urokinase (single-chain urokinase-type plasminogen activator) from bacteria. Drug Res 37:993–997
Hiramatsu R, Kasai S, Amatsuji Y, Kawai T, Hirose M, Morita M, Tanabe T, Kawabe H, Arimura H, Yokoyama K (1989) Effect of deletion of epidermal growth factor-like domain on plasma clearance of pro-urokinase. Fibrinolysis 3:147–151
Holmes WE, Pennica D, Blaber M, Rey MW, Günzler WA, Steffens GJ, Heyneker HL (1985) Cloning and expression of the gene for pro-urokinase in Escherichia coli. Biotechnology 3:923–929
Krause J (1988) Catabolism of tissue-type plasminogen activator (t-PA), its variants, mutants and hybrids. Fibrinolysis 2:133–142
Krause J, Seydel W, Heinzel G, Transwell P (1990) Different receptors mediate the hepatic catabolism of tissue-type plasminogen activator and urokinase. Biochem J 267:647–652
Kristensen P, Larsson LI, Nielsen LS, Grøndahl-Hansen J, Andreasen PA, Danø K (1984) Human endothelial cells contain one type of plasminogen activator. FEBS Lett 168:33–37
Kristensen P, Nielsen LS, Grøndahl-Hansen J, Andreasen PB, Larsson LI, Danø K (1985) Immunocytochemical demonstration of tissue-type plasminogen activator in endocrine cells of the rat pituitary gland. J Cell Biol 101:305–311
Kristensen P, Hougaard DM, Nielsen LS, Danø K (1986) Tissue-type plasminogen activator in rat adrenal medulla. Histochemistry 85:431–436
Kristensen P, Nielsen JH, Larsson LI, Danø K (1987) Tissue-type plasminogen activator in somatostatin cells of rat pancreas and hypothalamus. Endocrinology 121:2238–2244
Larsson LI, Skriver L, Nielsen LS, Grøndahl-Hansen J, Kristensen P, Danø K (1984) Distribution of urokinase-type plasminogen activator immunoreactivity in the mouse. J Cell Biol 98:894–903
Lijnen HR, Zammeran C, Blaber M, Winkler ME, Collen D (1986) Activation of plasminogen by pro-urokinase. I Mechanism. J Biol Chem 261:1253–1258
Miles LA, Levin EG, Plescia J, Collen D, Plow EF (1988) Plasminogen receptors, urokinase receptors, and their modulation on human endothelial cells. Blood 72:628–635
Sainte-Marie G (1962) A paraffin embedding technique for studies employing immunofluorescence. J Histochem Cytochem 10:250–256
Sternberger LA, Hardy PH, Cuculis JJ, Meyer HG (1970) The unlabeled antibody enzyme method of immunohistochemistry. Preparation and properties of soluble antigen-antibody complex (horseradish peroxidase-anti-horseradish peroxidase) and its use in the identification of spirochetes. J Histochem Cytochem 18:315–333
Vassalli JD, Baccino D, Belin D (1985) A cellular binding site for the 55,000 form of the human plasminogen activator, urokinase. J Cell Biol 100:86–92
Vihko KK, Kristensen P, Danø K, Parvinen M (1988) Immunohistochemical localization of urokinase-type plasminogen activation in Sertoli cells and tissue-type plasminogen activator in spermatogenic cells in the rat seminiferous epithelium. Dev Biol 126:150–155
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Wöhrmann, T., Matthiesen, T., Beier, H. et al. Immunohistological detection of Saruplase (recombinant single-chain urokinase-type plasminogen activator) in normal rat tissue. Histochemistry 96, 163–167 (1991). https://doi.org/10.1007/BF00315988
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00315988