Clinical screening of monoclonal antibodies 323/A3, cSF-25 and K928 for suitability of targetting tumours in the upper aerodigestive and respiratory tract

Bree, Remco de; Jc, Roos; Quak, Jasper J.; Hollander, W. den; Snow, G. B.; Dongen, Guus A.M.S. van

doi:10.1097/00006231-199408000-00006

Cited by 31 publications

(29 citation statements)

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“…In 70% of these tumours, the antigen was expressed by the majority of the cells within these tumours. A similar reactivity pattern was observed in 31 tumour-infiltrated lymph nodes from neck dissection specimens (De Bree et al, 1994a Before and up to 7 days after administration of the radioimmunoconjugates, urine and blood were obtained for analysis as described previously (De Bree et al, 1994b). Vital signs were recorded before and up to 3 h after injection.…”

Section: Monoclonal Antibodiesmentioning

confidence: 70%

“…British Journal of Cancer (1997) 75(7) (De Bree et al, 1994a); all data are now available for the selection of one of these MAbs for adjuvant RIT and to estimate the feasibility of this therapeutic approach.…”

Section: British Journal Of Cancermentioning

confidence: 99%

“…Two of these MAbs, designated E48 and U36, are selectively reactive with normal and malignant squamous and transitional epithelia (Quak et al, 1990;Schrijvers et al, 1993). While MAb E48 shows a homogeneous reactivity with 70% of HNSCC, for MAb U36 this approaches 96% reactivity (De Bree et al, 1994a). The biodistribution of 99mTc-labelled mE48 IgG and mU36 IgG has been evaluated by radioimmunoscintigraphy (RIS) and by biopsy measurement (De Bree et al, 1994b, 1995a in 24 and ten HNSCC patients respectively.…”

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confidence: 99%

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Selection of monoclonal antibody E48 IgG or U36 IgG for adjuvant radioimmunotherapy in head and neck cancer patients

Bree

Roos²,

Plaizier

et al. 1997

Br J Cancer

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Summary Preliminary data from recent clinical radioimmunoscintigraphy studies indicate that 99mTc-labelled murine monoclonal antibodies (MAbs) E48 and U36 have a similar ability to target squamous cell carcinoma of the head and neck (HNSCC) selectively. In the present study we describe additional aspects of murine and chimeric MAb (mMAb and cMAb) E48 and U36, which might influence the selection of one MAb for adjuvant radioimmunotherapy. To make direct comparison possible, ten patients received 11.2 ± 0.3 and 11.1 ± 0.2 mg (n = 5) or 51.1 ± 0.1 and 51.0 ± 0.4 mg (n= 5) of both mE48 IgG and mU36 IgG labelled with 1311 and 1251 simultaneously and underwent surgery 7-8 days after injection. The mean uptake of iodine-labelled mE48 IgG and mU36 was highest in tumour tissue, 8.9 ± 8.9 and 8.2 ± 4.4 %ID kg-' respectively. Tumour to non-tumour ratios for oral mucosa, skin, muscle, blood and bone marrow aspirate were 2.5, 5.5, 25.2, 4.7 and 4.0 respectively in the case of mE48 IgG and 2.3, 4.1, 21.0, 5.8 and 5.8 respectively in the case of mU36 IgG. The distribution of mMAbs E48 and U36 throughout tumours that had been collected in previous studies was heterogeneous when administered at a dose of 1 or 12 mg, and homogeneous when administered at a dose of 52 mg. Administration of mE48 IgG (1-52 mg) resulted in a human anti-mouse antibody response in 12 out of 28 patients, while for mU36 IgG (1-52 mg), this figure was three out of 18 patients. cMAb E48 was shown to be highly effective in mediating antibody-dependent cellular cytotoxicity in vitro, while cMAb U36 and mMAbs E48 and U36 were not effective at all. Rationales are provided that give priority to the start of adjuvant radioimmunotherapy trials with 1'6Re-labelled cMAb U36 IgG in head and neck cancer patients who are at high risk for the development of locoregional recurrences and distant metastases.Keywords: monoclonal antibodies; head and neck cancer; squamous cell carcinoma; biodistribution; human anti-mouse antibody response; antibody-dependent cellular cytotoxicityDuring 1996 approximately 41 090 Americans will develop head and neck cancer and 12 510 will die from it. Worldwide more than 500 000 new cases are projected annually, and the incidence is rising. In head and neck cancer, squamous cell carcinoma accounts for approximately 90% of all tumours (Parker et al, 1996). About one-third of these patients present with early-stage (I and II) head and neck squamous cell carcinoma (HNSCC), while two-thirds present with advanced disease (stage III and IV) (Vernham and Crowther, 1994). Although early-stage HNSCC can, in the great majority of cases, be cured with surgery or radiotherapy alone, the local failure rate after surgery and/or radiotherapy in advanced stages is more than 50%. Moreover, about 25% of these patients develop distant metastases (Stupp et al, 1994).Despite an increase in the locoregional control of HNSCC, owing to improved surgery and radiotherapy, current therapy regimens have failed to increase the 5-year survival rate in HNSCC patients (Pa...

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Section: Monoclonal Antibodiesmentioning

confidence: 70%

Section: British Journal Of Cancermentioning

confidence: 99%

mentioning

confidence: 99%

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Selection of monoclonal antibody E48 IgG or U36 IgG for adjuvant radioimmunotherapy in head and neck cancer patients

Bree

Roos²,

Plaizier

et al. 1997

Br J Cancer

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“…35 By contrast, Ep-CAM expression on certain tumors such as prostate and gastric carcinoma reaches 100% as examined by immunohistochemistry. 16,36 Moreover, Ep-CAM was found to be significantly upregulated with disease progression in several cancers including breast cancer, [17][18][19]37 suggesting that Ep-CAM expression on tumor cells confers a growth, invasion and/or survival benefit. A recent study showed that Ep-CAM can interact with the negative regulatory receptor LAIR-1 present on most immune cells.…”

Section: Discussionmentioning

confidence: 99%

In vitro and in vivo activity of MT201, a fully human monoclonal antibody for pancarcinoma treatment

Naundorf

Preithner

Mayer

et al. 2002

Intl Journal of Cancer

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In our study, a novel, fully human, recombinant monoclonal antibody of the IgG1 isotype, called MT201, was characterized for its binding properties, complement-dependent (CDC) and antibody-dependent cellular cytotoxicity (ADCC), as well as for its in vivo antitumor activity in a nude mouse model. MT201 was found to bind its target, the epithelial cell adhesion molecule (Ep-CAM; also called 17-1A antigen, KSA, EGP-2, GA733-2), with low affinity in a range similar to that of the clinically validated, murine monoclonal IgG2a antibody edrecolomab (Panorexா). MT201 exhibited Ep-CAM-specific CDC with a potency similar to that of edrecolomab. However, the efficacy of ADCC of MT201, as mediated by human immune effector cells, was by 2 orders of magnitude higher than that of edrecolomab. Addition of human serum reduced the ADCC of MT201 while it essentially abolished ADCC of edrecolomab within the concentration range tested. In a nude mouse xenograft model, growth of tumors derived from the human colon carcinoma line HT-29 was significantly and comparably suppressed by MT201 and edrecolomab. The fully human nature and the improved ADCC of MT201 with human effector cells will make MT201 a promising candidate for the clinical development of a novel pan-carcinoma antibody that is superior to edrecolomab.

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“…Previous studies with monoclonal antibodies against the pancarcinoma antigen, epithelial cell adhesion molecule (Ep-CAM), have shown tumour selectivity (De Bree et al, 1994;Riethmuller et al, 1994). We have already demonstrated that chemical conjugates consisting of the anti-Ep-CAM monoclonal antibody 323/ A3 and GUSh specifically localised into the Ep-CAM expressing tumour in nude mice bearing human ovarian cancer xenografts (Houba et al, 2001b).…”

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confidence: 95%

A fully human anti-Ep-CAM scFv-beta-glucuronidase fusion protein for selective chemotherapy with a glucuronide prodrug

et al. 2002

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Monoclonal antibodies against tumour-associated antigens could be useful to deliver enzymes selectively to the site of a tumour for activation of a non-toxic prodrug. A completely human fusion protein may be advantageous for repeated administration, as host immune responses may be avoided. We have constructed a fusion protein consisting of a human single chain Fv antibody, C28, against the epithelial cell adhesion molecule and the human enzyme b-glucuronidase. The sequences encoding C28 and human enzyme b-glucuronidase were joined by a sequence encoding a flexible linker, and were preceded by the IgGk signal sequence for secretion of the fusion protein. A CHO cell line was engineered to secrete C28-bglucuronidase fusion protein. Antibody specificity and enzyme activity were retained in the secreted fusion protein that had an apparent molecular mass of 100 kDa under denaturing conditions. The fusion protein was able to convert a non-toxic prodrug of doxorubicin, N-

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Clinical screening of monoclonal antibodies 323/A3, cSF-25 and K928 for suitability of targetting tumours in the upper aerodigestive and respiratory tract

Cited by 31 publications

References 0 publications

Selection of monoclonal antibody E48 IgG or U36 IgG for adjuvant radioimmunotherapy in head and neck cancer patients

Selection of monoclonal antibody E48 IgG or U36 IgG for adjuvant radioimmunotherapy in head and neck cancer patients

In vitro and in vivo activity of MT201, a fully human monoclonal antibody for pancarcinoma treatment

A fully human anti-Ep-CAM scFv-beta-glucuronidase fusion protein for selective chemotherapy with a glucuronide prodrug

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