Induction of antibody responses to breast carcinoma associated mucins using synthetic peptide constructs as immunogens

Denton, G.; Sekowski, M.; Price, M.R.

doi:10.1016/0304-3835(93)90224-w

Cited by 18 publications

(32 citation statements)

References 17 publications

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“…Peptide libraries are important tools for epitope mapping, mimotope discovery, and the identification of new binding sites and ligands (173,174). Selected peptides are useful as diagnostic reagents, affinity ligands, or immunogens for monoclonal antibodies, anti-epitope production or vaccine preparation (175)(176)(177)(178)(179). Mimotopes, mainly obtained by random peptide libraries, are peptides able to mimic the reaction between epitopes in antigens and the antibodies they elicit (180).…”

Section: Peptidic Ligandsmentioning

confidence: 99%

Antibodies and Genetically Engineered Related Molecules: Production and Purification

Roque

Lowe

Taipa³

2004

Biotechnol. Prog.

328

203

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Antibodies and antibody derivatives constitute 20 % of biopharmaceutical products currently in development, and despite early failures of murine products, chimeric and humanized monoclonal antibodies are now viable therapeutics. A number of genetically engineered antibody constructions have emerged, including molecular hybrids or chimeras that can deliver a powerful toxin to a target such as a tumor cell. However, the general use in clinical practice of antibody therapeutics is dependent not only on the availability of products with required efficacy but also on the costs of therapy. As a rule, a significant percentage (50-80%) of the total manufacturing cost of a therapeutic antibody is incurred during downstream processing. The critical challenges posed by the production of novel antibody therapeutics include improving process economics and efficiency, to reduce costs, and fulfilling increasingly demanding quality criteria for Food and Drug Administration (FDA) approval. It is anticipated that novel affinity-based separations will emerge from the development of synthetic ligands tailored to specific biotechnological needs. These synthetic affinity ligands include peptides obtained by synthesis and screening of peptide combinatorial libraries and artificial non-peptidic ligands generated by a de novo process design and synthesis. The exceptional stability, improved selectivity, and low cost of these ligands can lead to more efficient, less expensive, and safer procedures for antibody purification at manufacturing scales. This review aims to highlight the current trends in the design and construction of genetically engineered antibodies and related molecules, the recombinant systems used for their production, and the development of novel affinity-based strategies for antibody recovery and purification.

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Section: Peptidic Ligandsmentioning

confidence: 99%

Antibodies and Genetically Engineered Related Molecules: Production and Purification

Roque

Lowe

Taipa³

2004

Biotechnol. Prog.

328

203

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“…The preparation of anti-pCD IgG has been described elsewhere (Vetvicka et al, 1993). Anti-mucin MAb was prepared in our laboratory against a synthetic peptide sequence representing the MUC-1 mucin protein core (Denton et al, 1993). Hybridomas secreting anti-CD3 and anti-CD8 MAb were obtained from the ATCC (Rockville, MD).…”

Section: Animalsmentioning

confidence: 99%

Analysis of the interaction of procathepsin D activation peptide with breast cancer cells

et al. 1997

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“…This altered antigenicity of cancer cells may trigger immune responses, and the use of anticancer-mucin antibodies therefore has therapeutic potential [Kotera et al, 1994]. Mucins with cancer-specific glycosylation may also be useful as a vaccine [Denton et al, 1993;Finn et al, 1995;Graham et al, 1996].…”

Section: Mucins and O-glycans In Cancermentioning

confidence: 99%

Glycoproteins and Their Relationship to Human Disease

Brockhausen

Schutzbach

Kuhns

1998

Cells Tissues Organs

169

105

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Glycoproteins are proteins that carry N- and O-glycosidically-linked carbohydrate chains of complex structures and functions. N-glycan chains are assembled in the endoplasmic reticulum and the Golgi by a controlled sequence of glycosyltransferase and glycosidase processing reactions involving dolichol intermediates. The assembly of O-glycans occurs in the Golgi and does not involve dolichol. For most reactions, families of glycosyltransferases exist; the expression of the individual enzymes within a family is often subject to complex regulation. The biosynthesis of N- and O-glycan is controlled at the level of gene expression, mRNA, enzyme protein activity and localization, and through substrate and cofactor concentrations at the site of synthesis. This complex regulation results in many hundreds of structures, the range of which varies in different species, cell types, tissue types, states of development and differentiation. In diseased cells, the relative proportions of these structures are often characteristically different from normal, and may be useful for the assessment of the stage of the disease and for diagnosis. Knowledge of disease-specific glycoprotein structures and their functions may be used therapeutically, in immunotherapy, in blocking cell adhesion or interfering with other binding or biological processes. Recently, some of the mechanisms underlying glycoprotein alterations in disease have been elucidated. This opens the possibility of an active interference in the disease process. The functions of glycans in diseased cells will become more clear with the tools of molecular biology and transgenic animal models.

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Induction of antibody responses to breast carcinoma associated mucins using synthetic peptide constructs as immunogens

Cited by 18 publications

References 17 publications

Antibodies and Genetically Engineered Related Molecules: Production and Purification

Antibodies and Genetically Engineered Related Molecules: Production and Purification

Analysis of the interaction of procathepsin D activation peptide with breast cancer cells

Glycoproteins and Their Relationship to Human Disease

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