Batch-to-batch consistency of human-derived gonadotrophin preparations compared with recombinant preparations

Different gonadotrophin preparations derived from human urine or manufactured by recombinant technology are currently used in clinical practice for the treatment of infertility. It has been widely assumed that gonadotrophin products manufactured by recombinant technology have better batch-to-batch c...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autor principal: Wolfenson, C.
Otros Autores: Groisman, J., Couto, A.S, Hedenfalk, M., Cortvrindt, R.G, Smitz, J.E.J, Jespersen, S.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Reproductive Healthcare Ltd 2005
Materias:
Acceso en línea:Registro en Scopus
DOI
Handle
Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
LEADER 14399caa a22012377a 4500
001 PAPER-22224
003 AR-BaUEN
005 20230518205346.0
008 190411s2005 xx ||||fo|||| 00| 0 eng|d
024 7 |2 scopus  |a 2-s2.0-16844368185 
024 7 |2 cas  |a chorionic gonadotropin, 9002-61-3; human menopausal gonadotropin, 61489-71-2; recombinant follitropin, 1219693-73-8, 146479-72-3, 1359819-75-2; urofollitropin, 97048-13-0 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a RBOEA 
100 1 |a Wolfenson, C. 
245 1 0 |a Batch-to-batch consistency of human-derived gonadotrophin preparations compared with recombinant preparations 
260 |b Reproductive Healthcare Ltd  |c 2005 
270 1 0 |m Jespersen, S.; Ferring Pharmaceuticals A/S, Kay Fiskers Plads 11, 2300 Copenhagen S, Denmark; email: sonja.jespersen@ferring.com 
506 |2 openaire  |e Política editorial 
504 |a Adriaens, I., Cortvrindt, R., Smitz, J., Differential FSH exposure in preantral follicle culture has marked effects on folliculogenesis and oocyte developmental competence (2004) Human Reproduction, 19, pp. 398-408 
504 |a Akar, A.H., Gervasi, G., Blacker, C., Human chronionic gonadotrophin-like and beta-core like materials in postmenopausal urine (1990) Journal of Endocrinology, 125, pp. 477-485 
504 |a Alfthan, H., Haglund, C., Dabek, J., Concentration of human choriogonadotropin, its beta-subunit, and the core fragment of the beta-subunit in serum and urine of men and non-pregnant women (1992) Clinical Chemistry, 38, pp. 1981-1987 
504 |a Andersen, C.Y., Effect of FSH and its different isoforms on maturation of oocytes from pre-ovulatory follicles (2002) Reproductive BioMedicine Online, 5, pp. 232-239 
504 |a Andersen, C.Y., Westergaard, L.G., Wely, M.V., FSH isoform composition of commercial gonadotrophin preparations: A neglected aspect? (2004) Reproductive BioMedicine Online, 9, pp. 231-236 
504 |a Armstrong, E.G., Ehrlich, P.H., Birken, S., Use of a highly sensitive and a specific immunoradiometric assay for the detection of human chorionic gonadotropin in urine of normal, non-pregnant, and pregnant individuals (1984) Journal of Clinical Endocrinology and Metabolism, 59, pp. 867-874 
504 |a Babu, P.S., Krishnamurthy, H., Chedrese, P.J., Activation of extracellular-regulated kinase pathways in ovarian granulosa cells by the novel growth factor type 1 follicle-stimulating hormone receptor. Role in hormone signaling and cell proliferation (2000) Journal of Biological Chemistry, 275, pp. 27615-27626 
504 |a Baenziger, J.U., Green, E.D., Pituitary glycoprotein hormone oligosaccharides: Structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin (1988) Biochimica Et Biophysica Acta, 947, pp. 287-306 
504 |a Balasch, J., Fábregues, F., Peñarrubia, J., Outcome from consecutive assisted reproduction cycles in patients treated with recombinant follitropin alfa filled-by-bioassay and those treated with recombinant follitropin alfa filled-by-mass (2004) Reproductive BioMedicine Online, 8, pp. 408-413 
504 |a Barrios-de-Timossi, J., Timossi, C., Merchant, H., Assessment of the in vitro and in vivo biological activities of the human follicle-stimulating isohormones (2002) Molecular and Cellular Endocrinology, 186, pp. 189-198 
504 |a Bishop, L., Nguyen, T., Schofield, P., Both of the beta-subunit carbohydrate residues of follicle-stimulating hormone determine the metabolic clearance rate and in vivo potency (1995) Endocrinology, 136, pp. 2635-2640 
504 |a Burgon, P., Stanton, P., Robertson, D., In vivo bioactivities and clearance patterns of highly purified human luteinizing hormone isoforms (1996) Endocrinology, 137, pp. 4827-4836 
504 |a Cortvrindt, R.G., Smitz, J.E.J., Follicle culture in reproductive toxicology: A tool for in-vitro testing of ovarian function? (2002) Human Reproduction Update, 8, pp. 243-254 
504 |a Cortvrindt, R.G., Hu, Y., Liu, J., Timed analysis of the nuclear maturation of oocytes in early preantral mouse follicle culture supplemented with recombinant gonadotropin (1998) Fertility and Sterility, 70, pp. 1114-1125 
504 |a Dahl, K.D., Bicsak, T.A., Hsueh, A.J.W., Naturally occurring antihormones: Secretion of FSH antagonists by women treated with a GnRH analog (1988) Science, 239, pp. 72-74 
504 |a Driebergen, R., Baer, G., Quantification of follicle stimulating hormone (follitropin alfa): Is in vivo bioassay still relevant in the recombinant age? (2003) Current Medical Research and Opinion, 19, pp. 41-46 
504 |a Efficacy and safety of highly purified menotropin versus recombinant follicle-stimulating hormone in in vitro fertilization/intracytoplasmic sperm injection cycles: A randomized, comparative trial (2002) Fertility and Sterility, 78, pp. 520-528. , EISG 
504 |a Gad, S.C., Weil, C.S., Statistics for toxicologists (1989) Principle and Methods of Toxicology, pp. 435-483. , Hayes AW (ed.) 2nd edn. Raven Press, New York 
504 |a Galway, A., Hsueh, A., Keene, J., In vitro and in vivo bioactivity of recombinant human follicle-stimulating hormone and partially deglycosylated variants secreted by transfected eukaryotic cell lines (1990) Endocrinology, 127, pp. 93-100 
504 |a Gervais, A., Hammel, Y.-A., Pelloux, S., Glycosylation of human gonatrophins: Characterization and batch-to-batch consistency (2003) Glycobiology, 13, pp. 179-189 
504 |a Green, E., Baenziger, J., Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. I. Structural elucidation of the sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones (1988) Journal of Biological Chemistry, 263, pp. 25-35 
504 |a Green, E., Baenziger, J., Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. II. Distributions of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones (1988) Journal of Biological Chemistry, 263, pp. 36-44 
504 |a Horsman, G., Talbot, J.A., McLoughlin, J.D., A biological, immunological and physico-chemical comparison of the current clinical batches of the recombinant FSH preparations GONAL-f and Puregon (2000) Human Reproduction, 15, pp. 1898-1902 
504 |a Lambert, A., Rodgers, M., Mitchell, R., In-vitro biopotency and glycoform distribution of recombinant human follicle stimulating hormone (Org 32489), Metrodin and Metrodin-HP (1995) Molecular Human Reproduction, 10, pp. 1928-1935 
504 |a McFarland, K., Sprengel, R., Phillips, H., Lutropin-choriogonadotropin receptor: An unusual member of the G protein-coupled receptor family (1989) Science, 245, pp. 494-499 
504 |a Mulders, J.W.M., Derksen, M., Swolfs, A., Prediction of the in vivo biological activity of human recombinant follicle stimulating hormone using quantitative isoelectric focusing (1997) Biologicals, 25, pp. 269-281 
504 |a Recombinant follicle stimulating hormone: Development of the first biotechnology product for the treatment of infertility (1998) Human Reproduction Update, 4, pp. 862-881. , Recombinant Human FSH Product Development Group 
504 |a Richards, J., Estradiol receptor content in rat granulosa cells during follicular development: Modification by estradiol and gonadotropins (1975) Endocrinology, 97, pp. 1174-1184 
504 |a Rose, M.P., Das, R.E.G., Balen, A.H., Definition and measurement of follicle stimulating hormone (2000) Endocrine Reviews, 21, pp. 5-22 
504 |a Sairam, M.R., Jiang, L.G., Yarney, T.A., Alternative splicing converts the G-protein coupled follitropin receptor gene into a growth factor type I receptor: Implications for pleiotropic actions of the hormone (1997) Molecular Reproduction and Development, 48, pp. 471-479 
504 |a Sasano, H., Okamoto, M., Mason, J., Immunolocalization of aromatase, 17 alpha-hydroxylase and side-chain-cleavage cytochromes P-450 in the human ovary (1989) Journal of Reproduction and Fertility, 85, pp. 163-169 
504 |a Steelman, S.L., Pohley, F.M., Assay of the follicle stimulating hormone based on the augmentation with human chorionic gonadotrophin (1953) Endocrinology, 53, pp. 604-614 
504 |a Tamura, T., Kitawaki, J., Yamamoto, T., Imunohistochemical localization of 17 alpha-hydroxylase/C17-20 lyase and aromatase cytochrome P450 in the human ovary during the menstrual cycle (1992) Journal of Endocrinology, 135, pp. 589-595 
504 |a Timossi, C., Dámian-Matsumura, P., Dominguez-González, R., A less acidic human follicle-stimulating hormone preparation induce tissue-type plasminogen activator enzyme activity earlier than a predominantly acidic analogue in phenobarbital-blocked pro-oestrous rats (1998) Molecular Human Reproduction, 4, pp. 1032-1038 
504 |a Timossi, C.M., Tomasib, J.B.D., Zambranob, E., A naturally occurring basically charged human follicle-stimulating hormone (FSH) variant inhibits FSH-induced androgen aromatization and tissue-type plasminogen activator enzyme activity in vitro (1998) Neuroendocrinology, 67, pp. 153-163 
504 |a Timossi, C.M., Barrios-de-Timossi, J., González-Suárez, R., Differential effect of the charge variants of human follicle-stimulating hormone (2000) Journal of Endocrinology, 165, pp. 193-205 
504 |a Vitt, U.A., Nayudu, P.L., Rose, U.M., Embryonic development after follicle culture is influenced by follicle-stimulating hormone isoelectric point range (2001) Biology of Reproduction, 65, pp. 1542-1547 
504 |a Westergaard, L.G., Erb, K., Laursen, S.B., Human menopausal gonadotropin versus recombinant follicle-stimulating hormone in normogonadotropic women down-regulated with a gonadotropin-releasing hormone agonist who were undergoing in vitro fertilization and intracytoplasmic sperm injection: A prospective randomized study (2001) Fertility and Sterility, 76, pp. 543-549 
504 |a Wide, L., The regulation of metabolic clearance rate of human FSH in mice by variation of the molecular structure of the hormone (1986) Acta Endocrinologica, 112, pp. 336-344 
504 |a Wide, L., Hobson, B., Influence of the assay method used on the selection of the most active forms of FSH from the human pituitary (1986) Acta Endocrinologica, 113, pp. 17-22 
520 3 |a Different gonadotrophin preparations derived from human urine or manufactured by recombinant technology are currently used in clinical practice for the treatment of infertility. It has been widely assumed that gonadotrophin products manufactured by recombinant technology have better batch-to-batch consistency compared with human-derived preparations and that this potentially will be shown to provide a more constant clinical response, but there is little evidence for either statement. This study compared the batch-to-batch consistency between urinary-derived and recombinant manufactured gonadotrophin preparations using standard analytical techniques, as well as a novel in-vitro follicle bioassay to evaluate the consistency of the biological response at the target organ. Oligosaccharide isoform profiling, immunoassay testing, size exclusion chromatography analysis and in-vitro bioassay testing of urinary derived gonadotrophin preparations (MENOPUR® and BRAVELLE®) confirm that these products display a high degree of batch-to-batch consistency, similar to recombinant FSH (GONAL-f®) either filled by mass or bioassay. The data also suggest that the batch-to-batch variation is independent of the manufacturing procedure (filled-by-bioassay of filled-by-mass) for the recombinant preparation (Gonal-f), but that the total FSH bioactivity delivered from a single dose preparation after reconstitution differs between the two manufacturing procedures.  |l eng 
593 |a Instituto Massone S.A. Arias 4431, 1430 Buenos Aires, Argentina 
593 |a CIHIDECAR, Faculty of Exact and Natural Science, University of Buenos Aires, Buenos Aires, Argentina 
593 |a Ferring Pharmaceuticals A/S, Kay Fiskers Plads 11, 2300 Copenhagen S, Denmark 
593 |a EggCentris NV, Kranenberg 6, 1731 Brussels, Belgium 
690 1 0 |a BATCH-TO-BATCH CONSISTENCY 
690 1 0 |a GONADOTROPHIN 
690 1 0 |a HUMAN-DERIVED 
690 1 0 |a IN-VITRO FOLLICLE BIOASSAY 
690 1 0 |a RECOMBINANT FSH 
690 1 0 |a CHORIONIC GONADOTROPIN 
690 1 0 |a HUMAN MENOPAUSAL GONADOTROPIN 
690 1 0 |a ISOPROTEIN 
690 1 0 |a OLIGOSACCHARIDE 
690 1 0 |a RECOMBINANT FOLLITROPIN 
690 1 0 |a UROFOLLITROPIN 
690 1 0 |a ANALYTIC METHOD 
690 1 0 |a ARTICLE 
690 1 0 |a CLINICAL PRACTICE 
690 1 0 |a DRUG DESIGN 
690 1 0 |a DRUG DETERMINATION 
690 1 0 |a DRUG DOSAGE FORM 
690 1 0 |a DRUG MANUFACTURE 
690 1 0 |a DRUG POTENTIATION 
690 1 0 |a DRUG QUALITY 
690 1 0 |a EVIDENCE BASED MEDICINE 
690 1 0 |a HUMAN 
690 1 0 |a IMMUNOASSAY 
690 1 0 |a IN VITRO STUDY 
690 1 0 |a INFERTILITY 
690 1 0 |a OVARY FOLLICLE MATURATION 
690 1 0 |a TARGET ORGAN 
690 1 0 |a URINE 
653 0 0 |a bravelle, Ferring, United Kingdom; gonal f; humegon, Organon, Netherlands Antilles; menopur, Ferring, United Kingdom; pergonal, Serono, Switzerland 
700 1 |a Groisman, J. 
700 1 |a Couto, A.S. 
700 1 |a Hedenfalk, M. 
700 1 |a Cortvrindt, R.G. 
700 1 |a Smitz, J.E.J. 
700 1 |a Jespersen, S. 
773 0 |d Reproductive Healthcare Ltd, 2005  |g v. 10  |h pp. 442-454  |k n. 4  |p Reprod. BioMed. Online  |x 14726483  |w (AR-BaUEN)CENRE-6658  |t Reproductive BioMedicine Online 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-16844368185&doi=10.1016%2fS1472-6483%2810%2960819-X&partnerID=40&md5=dac695034f6cd2f0850135d24638b4d1  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1016/S1472-6483(10)60819-X  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_14726483_v10_n4_p442_Wolfenson  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14726483_v10_n4_p442_Wolfenson  |y Registro en la Biblioteca Digital 
961 |a paper_14726483_v10_n4_p442_Wolfenson  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 83177