Aspartic proteinase members secreted by the ruminant placenta: Specificity of three radioimmunoassay systems for the measurement of pregnancy-associated glycoproteins
[en] Pregnancy-associated glycoproteins (PAGs) isolated from the placenta of various ruminant species are enzymatically inactive members of the aspartic proteinase family. The measurement of these proteins in the maternal blood can be a good indicator of the presence of a live embryo. As certain aspartic proteinases are present in biological fluids in physiological and pathological conditions at various concentrations, it was necessary to determine the specificity of three radioimmunoassay (RIA) systems currently used for the detection of PAG molecules. Commercially available members of the aspartic proteinase family like pepsinogen, pepsin, chymosin, rennet, cathepsin D and renin were tested in a wide concentration range (10 ng/ml - 1 mg/ml). Pepsinogen cross-reacted in RIA 1, RIA 2 and RIA 3 over 1 mg/ml, 50 microg/ml and 500 microg/ml concentrations, respectively. In the presence of pepsin, cross-reaction was observed in RIA 1, RIA 2 and RIA 3 over 1 mg/ml, 500 microg/ml and 1 mg/ml concentrations, respectively. Chymosin and rennet could cross-react in RIA 2 and RIA 3, while renin and cathepsin D did not decrease the binding of the tracer to antisera more, than that of the minimal detection limit. As the plasma/serum concentrations of the examined aspartic proteinases reported in the literature were outside the concentration range where cross-reaction was observed, it can be concluded that these RIA systems were specific for the detection of PAGs in biological fluids.
Disciplines :
Veterinary medicine & animal health
Author, co-author :
Perenyi, Z. S.; Université de Liège - ULiège
Szenci, O.
Drion, Pierre ; Université de Liège - ULiège > Services généraux de l'Université
Banga-Mboko, H.; Université de Liège - ULiège
Melo de Sousa, Noelita ; Université de Liège - ULiège > Département de sciences fonctionnelles > Physiologie de la reproduction
El Amiri, Bouchra; Université de Liège - ULiège
Beckers, Jean-François ; Université de Liège - ULiège > Département de sciences fonctionnelles > Physiologie de la reproduction
Language :
English
Title :
Aspartic proteinase members secreted by the ruminant placenta: Specificity of three radioimmunoassay systems for the measurement of pregnancy-associated glycoproteins
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Bibliography
Barrett AJ, 1977: Cathepsin D and other carboxyl proteinases. In: Barrett, AJ (ed.) Proteinases in Mammalian Cells and Tissues. Elsevier, Amsterdam, pp. 209-248.
Beckers JF, Drion PV, Garbayo JM, Perényi ZS, Zarrouk A, Sulon J, Remy B, Szenci O, 1999: Pregnancy associated glycoproteins in ruminants: inactive members of the aspartic proteinase family. Acta Vet Hung 47, 461-469.
Blum J, Fiani M, Stahl P, 1992: Localization of cathepsin D in endosomes: characterization and biological importance. In: Dunn, B (ed.), Structure and Function of the Aspartic Proteinases. Genetics, Structure, and Mechanisms. Plenum Press, New York, London, pp. 281-287.
Deinum J, Derkx FH, Danser AH, Schalekamp MA, 1990: Identification and quantification of renin and prorenin in the bovine eye. Endocrinology 126, 1673-1682.
Ernstrom CA, 1965: Rennin and other enzyme actions. In: Webb, BH, Johnson, AH (eds), Fundamentals of Dairy Chemistry. The AVI Publishing Company, Inc., Westport, CO, pp. 590-600.
Foltmann B, Pedersen VB, Kauffman D, Wybrandt G, 1979: The primary structure of calf chymosin. J Biol Chem 254, 8447-8456.
Garbayo JM, Green J, Beckers JF, Roberts RM, 1999: Cloning and expression of pregnancy-associated glycoproteins (PAGs) from the caprine placenta. Biol Reprod 60 (Suppl 1), pp. 493.
González F, Sulon J, Calero P, Batista M, Gracia A, Beckers JF, 2001: Pregnancy-associated glycoproteins (PAG) detection in milk samples for pregnancy diagnosis in dairy goats. Theriogenology 56 (4), 671-676.
Green J, Xie S, Gan X, Roberts RM, 1998: An aspartic proteinase expressed in the equine placenta. In: James, MNG (eds), Aspartic Proteinases. Plenum Press, New York, pp. 163-167.
Green JA, Xie S, Quan X, Bao B, Gan X, Mathialagan N, Beckers JF, Roberts RM, 2000: Pregnancy-associated bovine and ovine glycoproteins exhibit spatially and temporally distinct expression patterns during pregnancy. Biol Reprod 62, 1624-1631.
Greenwood FC, Hunter WM, Glover JS, 1963: The preparation of 131-I labelled human growth hormone of high specific radioactivity. Biochem J 89, 114-123.
Guruprasad K, Blundell TL, Xie S, Green J, Szafranska B, Nagel RJ, McDowell K, Baker CB, Roberts RM, 1996: Comparative modelling and analysis of amino acid substitutions suggests that the family of pregnancy-associated glycoproteins includes both active and inactive aspartic proteinases. Protein Engineering 9, 849-856.
Harboe M, Andersen PM, Foltmann B, 1974: The activation of bovine pepsinogen. Sequence of the peptides released, identification of a pepsin inhibitor. J Biol Chem 249, 4487-4494.
Harvey-White JD, Smith JP, Parbuoni E, Allen EH, 1983: Reference serum pepsinogen concentrations in dairy cattle. Am J Vet Res 44, 115-117.
Inagami T, Misono K, Chang JJ, Takii Y, Dykes C, 1985: Renin and general aspartyl proteases: Differences and similarities in structure and function. In: Kostka, V (ed.), Aspartic Proteinases and their Inhibitors. Walter de Gruyter, Berlin, New York, pp. 319-337.
Larsen LB, Petersen TE, 1995: Identification of five molecular forms of cathepsin D in bovine milk. Adv Exp Med Biol 362, 279-283.
Larsen LB, Boisen A, Petersen TE, 1993: Procathepsin D cannot autoactivate to cathepsin D at acid pH. FEBS Lett 319, 54-58.
Larsen LB, Benfeldt C, Rasmussen LK, Petersen, TE, 1996: Bovine milk procathepsin D and cathepsin D: coagulation and milk protein degradation. J Dairy Res 63, 119-130.
Marciniszyn J, Hartsuck JA, Tang J, 1976: Mode of inhibition of acid proteases by pepstatin. J Biol Chem 251, 7088-7094.
Mukhopadhyay AK, Holstein K, Szkudlinski M, Brunswig-Spickenheier B, Leidenberger FA, 1991: The relationship between prorenin levels in follicular fluid and follicular atresia in bovine ovaries. Endocrinology 129, 2367-2375.
Nielsen AH, Gotfredsen P, Nielsen PB, Hyttel P, Poulsen K, 1991: Measurement of renin and prorenin in cattle, hog and horse. Comp Biochem Physiol A 100, 127-131.
Pedersen VB, Foltmann B, 1975: Amino-acid sequence of the peptide segment liberated during activation of prochymosin (prorennin). Eur J Biochem 55, 95-103.
Rajagopalan TG, Stein WH, Moore S, 1966: The inactivation of pepsin by diazoacetylnorleucine methyl ester. J Biol Chem 241, 4295-4297.
Rothe GA, Axelsen NH, Johnk P, Foltmann B, 1976: Immunochemical, chromatographic, and milk-clotting activity measurements for quantification of milk-clotting enzymes in bovine rennets. J Dairy Res 43, 85-95.
Schauser KH, Nielsen AH, Winther H, Dantzer V, Poulsen K, 1999: Dominance of type 1 angiotensin II receptor in the nonpregnant and pregnant bovine uterus. J Reprod Fertil 116, 403-413.
Selman IE, Armour J, Jennings FW, Reid JFS, 1977: Interpretation of the plasma pepsinogen test. Vet Rec 100, 249-250.
Stepanov VM, Baratova LA, Pugacheva IB, Belyanova LP, Revina LP, Timokhina EA, 1973: N-terminal sequence of swine pepsinogen and pepsin. The site of pepsinogen activation. Biochem Biophys Res Commun 54, 1164-1170.
Takahashi T, Tang J, 1981: Cathepsin D from porcine and bovine spleen. Methods Enzymol 80, 565-581.
Tang J, 1971: Specific and irreversible inactivation of pepsin by substrate-like epoxides. J Biol Chem 246, 4510-4517.
Umezawa H, Aoyagi T, Morishima H, Matsuzaki M, Hamada M, Takeuchi T, 1979: Pepstatin, a new pepsin inhibitor produced by actinomycetes. J Antibiot 23, 259-262.
Vaitukaitis J, Robbins JB, Nieschlag E, Ross GT, 1971: A method for producing specific antisera with small doses of immunogen. J Clin Endocrinol Metab 33, 988-991.
Vörös K, Meyer C, Stöber M, 1984: Pepsinogenaktivität von Serum und Harn sowie Pepsinaktivität des Labmagensaftes labmagengesunder und nicht-parasitär labmagenk ranker Rinder. Zbl Vet Med A 31, 182-192.
Xie S, Cow B, Zoli PA, Beckers JF, Roberts RM, 1991: Molecular cloning of pregnancy-associated glycoproteins from cattle and sheep: identity with the aspartate protease family. In: Biology of Reproduction, Annual Meeting, University of British Columbia, Vancouver, July 29-31, 1991. 44 (Suppl. 1), 101.
Xie S, Low BG, Nagel RJ, Beckers JF, Roberts RM, 1994: A novel glycoprotein of the aspartic proteinase gene family expressed in bovine placental trophectoderm. Biol Reprod 51, 1145-1153.
Xie S, Green J, Beckers JF, Roberts RM, 1995: The gene encoding bovine pregnancy-associated glycoprotein-1, an inactive member of the aspartic proteinase family. Gene 159, 193-197.
Xie S, Green J, Bixby JB, Szafranska B, Demartini JC, Hecht S, Roberts RM, 1997: The diversity and evolutionary relationships of the pregnancy-associated glycoproteins, an aspartic proteinase subfamily, consisting of many trophoblast-expressed genes. Proc Natl Acad Sci 94, 12809-12816.
Zarrouk A, Engeland I, Sulon J, Beckers JF, 1999a: Determination of pregnancy-associated glycoprotein concentrations in goats (Capra hircus) with unsuccessful pregnancies: a retrospective study. Theriogenology 51, 1221-1231.
Zarrouk A, Engeland I, Sulon J, Beckers JF, 1999b: Pregnancy-associated glycoprotein levels in pregnant goats inoculated with Toxoplasma gondii or Listeria monocytogenes: a retrospective study. Theriogenology 52, 1095-1104.
Zoli AP, Beckers JF, Wouters-Ballman P, Closset J, Falmagne P, Ectors F, 1991: Purification and characterization of a bovine pregnancy-associated glycoprotein. Biol Reprod 45, 1-10.
Zoli AP, Guibault LA, Delahaut P, Benitez Ortiz W, Beckers JF, 1992: Radioimmunoassay of a bovine pregnancy-associated glycoprotein in serum: its application for pregnancy diagnosis. Biol Reprod 46, 83-92.
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