Production of monoclonal antibodies against prostatic acid phosphatase by in vitro immunization of human spleen cells

Yamaura, Noboru; Makino, Masanao; Walsh, Linda; Bruce, Andrew W.; Choe, B. K.

doi:10.1016/0022-1759(85)90419-3

Cited by 19 publications

(3 citation statements)

References 27 publications

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“…Interestingly, within the chimeric antibody definition (“engineered from any species, including human”), there is the possibility that human antibodies engineered for improved affinity or other properties could be considered chimeric. The American Medical Association 9 provide some guidance (also adopted by the INN) on the criteria for defining antibodies derived from different methods e.g., isolation from various display libraries, 13,14 , 15,16 use of animals transgenic for human antibody genes 17,18 , 19,20 , 21 and direct isolation from humans 22,23 , 24,25 , 26 where identity to human sequences must be ≥85%. However, this threshold has recently changed from a previous version that stipulated ≥90%.…”

Section: Impact Of 2014 Who Inn Definition On Human Antibodiesmentioning

confidence: 99%

The INNs and outs of antibody nonproprietary names

Jones

Carter²,

Plückthun

et al. 2015

mAbs

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An important step in drug development is the assignment of an International Nonproprietary Name (INN) by the World Health Organization (WHO) that provides healthcare professionals with a unique and universally available designated name to identify each pharmaceutical substance. Monoclonal antibody INNs comprise a –mab suffix preceded by a substem indicating the antibody type, e.g., chimeric (-xi-), humanized (-zu-), or human (-u-). The WHO publishes INN definitions that specify how new monoclonal antibody therapeutics are categorized and adapts the definitions to new technologies. However, rapid progress in antibody technologies has blurred the boundaries between existing antibody categories and created a burgeoning array of new antibody formats. Thus, revising the INN system for antibodies is akin to aiming for a rapidly moving target. The WHO recently revised INN definitions for antibodies now to be based on amino acid sequence identity. These new definitions, however, are critically flawed as they are ambiguous and go against decades of scientific literature. A key concern is the imposition of an arbitrary threshold for identity against human germline antibody variable region sequences. This leads to inconsistent classification of somatically mutated human antibodies, humanized antibodies as well as antibodies derived from semi-synthetic/synthetic libraries and transgenic animals. Such sequence-based classification implies clear functional distinction between categories (e.g., immunogenicity). However, there is no scientific evidence to support this. Dialog between the WHO INN Expert Group and key stakeholders is needed to develop a new INN system for antibodies and to avoid confusion and miscommunication between researchers and clinicians prescribing antibodies.

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Section: Impact Of 2014 Who Inn Definition On Human Antibodiesmentioning

confidence: 99%

The INNs and outs of antibody nonproprietary names

Jones

Carter²,

Plückthun

et al. 2015

mAbs

View full text Add to dashboard Cite

show abstract

“…The EBV-hybridoma technique was established based on a combination of the two methods. 3,18 The EBV-hybridoma system retains the advantageous features of the other two systems while overcoming their pitfalls for producing hmAb with a defined specificity. 19,20 Rapid advances in development of methods to improve the B cell immortalization and cell fusion, such as electroporation for fusion, may well lead EBV-hybridoma technology into a new era.…”

Section: Immortalization Of Antigen-specific Human B Cell and Hybridomentioning

confidence: 99%

Advances in the production of human monoclonal antibodies

Wang

2011

ANTI

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Since the development of hybridoma technology over three decades ago, numerous monoclonal antibodies have been produced and the use of monoclonal antibodies has become one of the major breakthroughs in medicine. Significant progress has been made on new technologies for generating human monoclonal antibodies. This review serves as an introduction to the immortalization of antigen-specific human B cell and hybridoma technologies, phage display platform, the use of transgenic mice, and the generation of monoclonal antibodies from single B cells.

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“…They fused this heteromyeloma with lymphocytes from immunised donors and established hybridomas which showed stable antibody production in long-term and mass culture. Several other laboratories have used such heteromyelomas between murine myelomas and human myelomas, normal human Blymphocytes or B-lymphoma cells for production of human antibodies (Foung et al, 1984;Yamaura et al, 1985;Teng et al, 1985;Ichimori et al, 1985;Caroll et al, 1986;Martin et al, 1988;Grunow et al, 1988;Vollmers et al, 1989). Some of the heteromyeloma products were stable for 6 months or longer without intensive recloning procedures, but only few of these fusion partners are available.…”

mentioning

confidence: 99%

HAB-1, a new heteromyeloma for continuous production of human monoclonal antibodies

Faller

Vollmers²,

Weiglein³

et al. 1990

Br J Cancer

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Summary To obtain suitable cell lines for the immortalisation of human lymphocytes, we constructed a heteromyeloma between the murine myeloma Ag8 and human lymphocytes from a highly malignant polymorphic, centroblastic B-cell lymphoma. The thioguanine-resistant and HAT-sensitive heteromyeloma HAB-1 neither secretes nor contains cytoplasmatic immunoglobulins, the cells being EBV negative but positively stained for HLA-BC and the human proliferation marker (Foung et al., 1984;Yamaura et al., 1985;Teng et al., 1985;Ichimori et al., 1985;Caroll et al., 1986;Martin et al., 1988;Grunow et al., 1988;Vollmers et al., 1989). Some of the heteromyeloma products were stable for 6 months or longer without intensive recloning procedures, but only few of these fusion partners are available. We describe in this paper a new genetically stable human-mouse heteromyeloma, HAB-1, which was produced by somatic hybridisation of murine Ag8 myeloma cells with human lymphocytes from a patient with a B-cell lymphoma. The cell line has ideal growth and fusion characteristics and has been successfully used for the long-term production of human monoclonal antibodies against stomach carcinoma cells. Materials and methods Cells and culture conditionsThe non-secreting HAT (hypoxanthine-aminopterinthymidine) sensitive heteromyeloma HAB-1 derived from hybridisation of murine Ag8 myeloma cells with lymph node cells from a patient with a highly malignant centroblastic B-cell lymphoma. Selected hybrids were exposed once to 6-thioguanine (5 lAg ml-') and growing clones were tested for HAT-sensitivity. Established cells were maintained in RPMI-1640 with 10% FCS (fetal calf serum) and 1% penicillin/ streptomycin. Lymph nodes and spleens obtained from stomach carcinomas patients during surgery were prepared by mechanical means. Cell suspensions were either incubated in culture medium before cell fusion or stored in liquid nitrogen until 24 h before hybridisation.For growth kinetics, 2 x 105 living cells were plated on 24-well culture plates and counted every day. Doubling time was determined in logarithmic growth phase. Somatic hybridisationsLymph node or spleen cells from stomach carcinoma patients were fused at a ratio of 1:1 with HAB-l and SPM4-0 (kindly provided by Hoffman LaRoche, Switzerland) or 1:5 and 1:10 with Ag8 cells using 40% polyethyleneglycol 1500 (Sigma, FRG). Hybridomas were cultured in RPMI-1640 containing 10% FCS and HAT supplement. After 4-6 weeks the supernatants were screened for antibody production in an enzymelinked immunosorbent assay (ELISA). Positive

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Production of monoclonal antibodies against prostatic acid phosphatase by in vitro immunization of human spleen cells

Cited by 19 publications

References 27 publications

The INNs and outs of antibody nonproprietary names

The INNs and outs of antibody nonproprietary names

Advances in the production of human monoclonal antibodies

HAB-1, a new heteromyeloma for continuous production of human monoclonal antibodies

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