ArticleProceedings of the National Academy of Sciences of the United States of America1997
The human A33 antigen is a transmembrane glycoprotein and a novel member of the immunoglobulin superfamily.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
51 citing papers in PubMed, 191 citations in OpenAlex.
- Phase 1/2 study of KRN330, a fully human anti-A33 monoclonal antibody, plus irinotecan as second-line treatment for patients with metastatic colorectal cancer.Investigational new drugs · 2014Trial
- 124I-huA33 antibody uptake is driven by A33 antigen concentration in tissues from colorectal cancer patients imaged by immuno-PET.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2011Trial
- (124)I-huA33 antibody PET of colorectal cancer.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2011Trial
- Targeting GPA33 with CAR-macrophages: a novel immunotherapeutic approach for colorectal cancer.Journal of translational medicine · 2026Article
- GPA33-Targeted Trimeric Immunotoxin Exhibits Enhanced Antitumor Activity in Human Colorectal Cancer Xenografts.International journal of molecular sciences · 2026Article
- GPA33 expression in colorectal cancer can be induced by WNT inhibition and targeted by cellular therapy.Oncogene · 2025Article
- Multi-Omic Analysis of Esophageal Adenocarcinoma Uncovers Candidate Therapeutic Targets and Cancer-Selective Posttranscriptional Regulation.Molecular & cellular proteomics : MCP · 2024Article
- Site-Specific Photoaffinity Bioconjugation for the Creation ofMolecular imaging and biology · 2023Article
- Nanobody-Based EGFR-Targeting Immunotoxins for Colorectal Cancer Treatment.Biomolecules · 2023Article
- Article
- Treg in inborn errors of immunity: gaps, knowns and future perspectives.Frontiers in immunology · 2023Review
- Bispecific Antibody-Based Immune-Cell Engagers and Their Emerging Therapeutic Targets in Cancer Immunotherapy.International journal of molecular sciences · 2022Review
- Endoscopic Applications of Near-Infrared Photoimmunotherapy (NIR-PIT) in Cancers of the Digestive and Respiratory Tracts.Biomedicines · 2022Review
- Antibody-Based Immunotoxins for Colorectal Cancer Therapy.Biomedicines · 2021Review
- Near infrared photoimmunotherapy of cancer; possible clinical applications.Nanophotonics (Berlin, Germany) · 2021Review
- GPA33 is expressed on multiple human blood cell types and distinguishes CD4European journal of immunology · 2021Article
- Review
- HarnessingProceedings of the National Academy of Sciences of the United States of America · 2020Article
- A panel of intestinal differentiation markers (CDX2, GPA33, and LI-cadherin) identifies gastric cancer patients with favourable prognosis.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2020Article
- Novel biomarkers for the diagnosis and prognosis of colorectal cancer.Intestinal research · 2020Review
Corrections and comments
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Authors and funding
17 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mAb A33 detects a membrane antigen that is expressed in normal human colonic and small bowel epithelium and > 95% of human colon cancers. It is absent from most other human tissues and tumor types. 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. Using detergent extracts of the human colon carcinoma cell lines LIM1215 and SW1222, in which the antigen is highly expressed, the molecule was purified, yielding a 43-kDa protein. The N-terminal sequence was determined and further internal peptide sequence obtained following enzymatic cleavage. 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. The available data bases have been searched and reveal no overall sequence similarities with known proteins. Based on a hydrophilicity plot, the A33 protein has three distinct structural domains: an extracellular region of 213 amino acids (which, by sequence alignment of conserved residues, contains two putative immunoglobulin-like domains), a single hydrophobic transmembrane domain, and a highly polar intracellular tail containing four consecutive cysteine residues. These data indicate that the A33 antigen is a novel cell surface receptor or cell adhesion molecule in the immunoglobulin superfamily.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.