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GPA33  -  glycoprotein A33 (transmembrane)

Homo sapiens

Synonyms: A33, Cell surface A33 antigen, Glycoprotein A33
 
 
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Disease relevance of GPA33

  • Thus, A33 antigen has been explored as a potential therapeutic target for the treatment of colon cancers [1].
  • Here, we describe strategies for the purification and structural analysis of the A33 antigen from the human colorectal carcinoma cell lines LIM1215 and SW1222 [2].
  • The modest antitumor activity of 131I-mAb A33 in heavily pretreated patients is encouraging because of its lack of toxicity in the bowel, the only antigen-positive normal tissue [3].
  • Here, we determined the ability of a human melanoma-specific, cytotoxic T-cell line (CTL) in suppressing the growth of spontaneously metastasizing human melanoma cells M24 met (HLA-A11, A33) in scid mice [4].
  • A33, a monoclonal antibody that targets colon carcinomas, was labeled with (125)I or (131)I and the relative therapeutic efficacy of the 2 radiolabeled species was compared in a human colon cancer xenograft system [5].
 

High impact information on GPA33

  • We used mAb A33/22, which recognizes a nuclear protein on the loops of amphibian lampbrush chromosomes, to select cDNA clone PwA33 from an expression library of the newt Pleurodeles waltl [6].
  • The murine A33 mAb has been shown to target colon cancer in clinical trials, and the therapeutic potential of a humanized antibody is currently being evaluated [7].
  • The human A33 antigen is a transmembrane glycoprotein and a novel member of the immunoglobulin superfamily [7].
  • The mAb A33 detects a membrane antigen that is expressed in normal human colonic and small bowel epithelium and > 95% of human colon cancers [7].
  • Degenerate primers were used in PCRs to produce a probe to screen a LIM1215 cDNA library, yielding clones that enabled us to deduce the complete amino acid sequence of the A33 antigen and express the protein [7].
 

Chemical compound and disease context of GPA33

 

Biological context of GPA33

  • These data indicate that the A33 antigen is a novel cell surface receptor or cell adhesion molecule in the immunoglobulin superfamily [7].
  • Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium [12].
  • PURPOSE: A phase I/II study was designed to determine the maximum-tolerated dose (MTD) of iodine 131-labeled monoclonal antibody (mAb) A33 (131I-mAb A33) administered intravenously, its limiting organ toxicity, and its radioisotope retention in tumors, and to develop preliminary evidence of antitumor activity [3].
  • Serological analysis of human anti-human antibody responses in colon cancer patients treated with repeated doses of humanized monoclonal antibody A33 [8].
  • When tumor cells were targeted using antibody-antigen systems exhibiting slow rates of endocytosis (e.g., hP67 on HL-60 cells and hA33 on Colo 205 cells), little differences in cellular retention of radioactivity was observed, regardless of whether 125I, 111In, or 90Y was used [13].
 

Anatomical context of GPA33

 

Associations of GPA33 with chemical compounds

  • When long-term survival was used as an end point, 38% of the mice treated with 5-FU and 131I-mAb A33 were disease free at 276 days compared to none from any other group, suggesting a synergistic effect [14].
  • Additional, significant responses were observed in those patients treated with chemotherapy [carmustine [BCNU], vincristine, flourouracil, and streptozocin [BOF-Strep]) after completion of the 125I-mAb A33 study [9].
  • In assessing the reduction in tumor volumes over the first 28 days of the experiment, 5-FU treatment (with or without leucovorin) in combination with 131I-mAb A33 showed a statistically significant additive antitumor effect compared to 131I-mAb A33 alone or to chemotherapy alone [14].
  • The A33 protein was purified from Triton X-114 extracts of LIM1215 cells under nondenaturing conditions [17].
  • Enhancement of radiation dose to the nucleus by vesicular internalization of iodine-125-labeled A33 monoclonal antibody [16].
 

Regulatory relationships of GPA33

 

Other interactions of GPA33

 

Analytical, diagnostic and therapeutic context of GPA33

  • CONCLUSION: The A33 antigen appears to be a promising target for radioimmunotherapy of colon cancer [3].
  • Enhanced antitumor activity of combination radioimmunotherapy (131I-labeled monoclonal antibody A33) with chemotherapy (fluorouracil) [14].
  • PATIENTS AND METHODS: Patients (N = 21) with advanced chemotherapy-resistant colon cancer who had not received prior radiotherapy were treated with a single 125I-mAb A33 dose [9].
  • Here we use phage display technology to select and humanize antibodies from rabbits that were immunized with human A33 antigen which is a target antigen for the immunotherapy of colon cancer [19].
  • The purification was monitored by biosensor analysis using surface plasmon resonance detection with a F(ab')2 fragment of the humanized A33 monoclonal antibody immobilized on the sensor surface and Western blot analysis following SDS-polyacrylamide gel electrophoresis (PAGE) under nonreducing conditions using humanized A33 monoclonal antibody [17].

References

  1. Transcriptional regulation of A33 antigen expression by gut-enriched Krüppel-like factor. Mao, Z., Song, S., Zhu, Y., Yi, X., Zhang, H., Shang, Y., Tong, T. Oncogene (2003) [Pubmed]
  2. Micro-sequencing strategies for the human A33 antigen, a novel surface glycoprotein of human gastrointestinal epithelium. Moritz, R.L., Ritter, G., Catimel, B., Cohen, L.S., Welt, S., Old, L.J., Burgess, A.W., Nice, E.C., Simpson, R.J. Journal of chromatography. A. (1998) [Pubmed]
  3. Phase I/II study of iodine 131-labeled monoclonal antibody A33 in patients with advanced colon cancer. Welt, S., Divgi, C.R., Kemeny, N., Finn, R.D., Scott, A.M., Graham, M., Germain, J.S., Richards, E.C., Larson, S.M., Oettgen, H.F. J. Clin. Oncol. (1994) [Pubmed]
  4. Human cytotoxic T-cells suppress the growth of spontaneous melanoma metastases in SCID/hu mice. Sabzevari, H., Reisfeld, R.A. Cancer Res. (1993) [Pubmed]
  5. Relative therapeutic efficacy of (125)I- and (131)I-labeled monoclonal antibody A33 in a human colon cancer xenograft. Barendswaard, E.C., Humm, J.L., O'Donoghue, J.A., Sgouros, G., Finn, R.D., Scott, A.M., Larson, S.M., Welt, S. J. Nucl. Med. (2001) [Pubmed]
  6. A putative zinc-binding protein on lampbrush chromosome loops. Bellini, M., Lacroix, J.C., Gall, J.G. EMBO J. (1993) [Pubmed]
  7. The human A33 antigen is a transmembrane glycoprotein and a novel member of the immunoglobulin superfamily. Heath, J.K., White, S.J., Johnstone, C.N., Catimel, B., Simpson, R.J., Moritz, R.L., Tu, G.F., Ji, H., Whitehead, R.H., Groenen, L.C., Scott, A.M., Ritter, G., Cohen, L., Welt, S., Old, L.J., Nice, E.C., Burgess, A.W. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  8. Serological analysis of human anti-human antibody responses in colon cancer patients treated with repeated doses of humanized monoclonal antibody A33. Ritter, G., Cohen, L.S., Williams, C., Richards, E.C., Old, L.J., Welt, S. Cancer Res. (2001) [Pubmed]
  9. Phase I/II study of iodine 125-labeled monoclonal antibody A33 in patients with advanced colon cancer. Welt, S., Scott, A.M., Divgi, C.R., Kemeny, N.E., Finn, R.D., Daghighian, F., Germain, J.S., Richards, E.C., Larson, S.M., Old, L.J. J. Clin. Oncol. (1996) [Pubmed]
  10. A phase I trial of humanized monoclonal antibody A33 in patients with colorectal carcinoma: biodistribution, pharmacokinetics, and quantitative tumor uptake. Scott, A.M., Lee, F.T., Jones, R., Hopkins, W., MacGregor, D., Cebon, J.S., Hannah, A., Chong, G., U, P., Papenfuss, A., Rigopoulos, A., Sturrock, S., Murphy, R., Wirth, V., Murone, C., Smyth, F.E., Knight, S., Welt, S., Ritter, G., Richards, E., Nice, E.C., Burgess, A.W., Old, L.J. Clin. Cancer Res. (2005) [Pubmed]
  11. Pharmacokinetics and microdistribution of polyethylene glycol-modified humanized A33 antibody targeting colon cancer xenografts. Deckert, P.M., Jungbluth, A., Montalto, N., Clark, M.A., Finn, R.D., Williams, C., Richards, E.C., Panageas, K.S., Old, L.J., Welt, S. Int. J. Cancer (2000) [Pubmed]
  12. Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium. Ritter, G., Cohen, L.S., Nice, E.C., Catimel, B., Burgess, A.W., Moritz, R.L., Ji, H., Heath, J.K., White, S.J., Welt, S., Old, L.J., Simpson, R.J. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  13. Comparative metabolism and retention of iodine-125, yttrium-90, and indium-111 radioimmunoconjugates by cancer cells. Press, O.W., Shan, D., Howell-Clark, J., Eary, J., Appelbaum, F.R., Matthews, D., King, D.J., Haines, A.M., Hamann, P., Hinman, L., Shochat, D., Bernstein, I.D. Cancer Res. (1996) [Pubmed]
  14. Enhanced antitumor activity of combination radioimmunotherapy (131I-labeled monoclonal antibody A33) with chemotherapy (fluorouracil). Tschmelitsch, J., Barendswaard, E., Williams, C., Yao, T.J., Cohen, A.M., Old, L.J., Welt, S. Cancer Res. (1997) [Pubmed]
  15. Role of receptor-mediated endocytosis in the formation of vaccinia virus extracellular enveloped particles. Husain, M., Moss, B. J. Virol. (2005) [Pubmed]
  16. Enhancement of radiation dose to the nucleus by vesicular internalization of iodine-125-labeled A33 monoclonal antibody. Daghighian, F., Barendswaard, E., Welt, S., Humm, J., Scott, A., Willingham, M.C., McGuffie, E., Old, L.J., Larson, S.M. J. Nucl. Med. (1996) [Pubmed]
  17. Purification and characterization of a novel restricted antigen expressed by normal and transformed human colonic epithelium. Catimel, B., Ritter, G., Welt, S., Old, L.J., Cohen, L., Nerrie, M.A., White, S.J., Heath, J.K., Demediuk, B., Domagala, T., Lee, F.T., Scott, A.M., Tu, G.F., Ji, H., Moritz, R.L., Simpson, R.J., Burgess, A.W., Nice, E.C. J. Biol. Chem. (1996) [Pubmed]
  18. Glycoprotein A34, a novel target for antibody-based cancer immunotherapy. Scanlan, M.J., Ritter, G., Yin, B.W., Williams, C., Cohen, L.S., Coplan, K.A., Fortunato, S.R., Frosina, D., Lee, S.Y., Murray, A.E., Chua, R., Filonenko, V.V., Sato, E., Old, L.J., Jungbluth, A.A. Cancer Immun. (2006) [Pubmed]
  19. The rabbit antibody repertoire as a novel source for the generation of therapeutic human antibodies. Rader, C., Ritter, G., Nathan, S., Elia, M., Gout, I., Jungbluth, A.A., Cohen, L.S., Welt, S., Old, L.J., Barbas, C.F. J. Biol. Chem. (2000) [Pubmed]
 
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