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An EGP-2/Ep-CAM-expressing transgenic rat model to evaluate antibody-mediated immunotherapy (1999)

McLaughlin, Pamela M. J. ; Kroesen, Bart-Jan ; Dokter, Wim H. A. ; [et al.]

Springer

Cancer immunology immunotherapy 48 (1999), S. 303-311

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ISSN: 1432-0851

Keywords: Key words Transgenic ; Rat ; EGP-2 ; GA733-2 ; Immunotherapy

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract The human pancarcinoma-associated epithelial glycoprotein-2 (EGP-2), also known as 17-1A or Ep-CAM, is a 38-kDa transmembrane antigen, commonly used for targeted immunotherapy of carcinomas. Although strongly expressed by most carcinomas, EGP-2 is also expressed in most simple epithelia. To evaluate treatment-associated effects and side-effects on tumor and normal tissue respectively, we generated an EGP-2-expressing transgenic Wistar rat. To express the cDNA of the EGP-2 in an epithelium-specific manner, the 5′ and 3′ distal flanking regions of the human keratin 18 (K18) gene were used. EGP-2 protein expression was observed in the liver and pancreas, whereas EGP-2 mRNA could also be detected in lung, intestine, stomach and kidney tissues. In this rat, EGP-2-positive tumors can be induced by injecting a rat-derived carcinoma cell line transfected with the GA733-2 cDNA encoding EGP-2. Transgenic rats were used to study specific in vivo localization of an i.v. anti-EGP-2 monoclonal antibody, MOC31, applied i.v. Immunohistochemical analyses showed the specific localization of MOC31 in s.c. induced EGP-2-positive tumors, as well as in the liver. In contrast, in EGP-2-transgenic rats, MOC31 did not bind to EGP-2-negative tumors, the pancreas, or other normal tissues in vivo. In conclusion, an EGP-2-transgenic rat model has been generated that serves as a model to evaluate the efficacy and safety of a variety of anti-EGP-2-based immunotherapeutic modalities.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002620050579

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Fucosylation of glycoproteins in rat spermatocytes and spermatids (1982)

Grootegoed, J. Anton ; Krüger-Sewnarain, Bea C. ; Jutte, Nicolet H. P. M. ; [et al.]

New York, NY : Wiley-Blackwell

Gamete Research 5 (1982), S. 303-315

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ISSN: 0148-7280

Keywords: spermatocytes ; spermatids ; glycoproteins ; fucose ; acrosome ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: Glycoprotein synthesis in pachytene spermatocytes and round spermatids, isolated from rat testes, was studied by analysis of the incorporation of (3H)-fucose. The isolated germ cells were capable of incorporating (3H)-fucose into cell-bound, acid-precipitable components for an incubation period of at least 23 hours (at 32°C). In young spermatids, engaged in the formation of the acrosome, (3H)-fucose was incorporated into more than 16 different glycoproteins within the molecular weight range of 20.000-100,000. A qualitatively similar set of glycoproteins was found to be labeled in spermatocytes. Radioautography showed that after 4 hr most of the incorporated radioactivity was present at one pole in the perinuclear zone of spermatocytes and spermatids, which could reflect incorporation of fucose in the Golgi apparatus. The newly fucosylated glycoproteins were associated with a particulate subcellular fraction (membrane fraction). Trypsin treatment of whole cells after 25 hours of incubation with (3H)-fucose, however, did not cause significant lysis of tritiated glycoproteins.From the results it was concluded that the majority of the newly fucosylated glycoproteins in spermatocytes and spermatids remained associated with an intracellular membrane system, presumably the Golgi apparatus and the vesicles that arise from this structure, to be deposited subsequently in proacrosomic granules and the acrosome. The results also suggest that initiation of the synthesis of spermatidal glycoproteins occurs during the prophase of meiosis in spermatocytes.

Additional Material: 6 Ill.