PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 11391933

[Flow cytometry].

K Nakahara
View original source ↗Export metadata ↓

Abstract

Recently, flow-cytometric analysis has become the most popular type of cell-surface marker examination and it is particularly indispensable in diagnosing hematological disorders such as leukemia. Since diagnosis becomes more reliable using monoclonal antibodies, cell-surface marker analysis contributes greatly to the diagnosis of hematological disorders. In particular in lymphocytic leukemias, immunological classification becomes possible and since this classification has a close relation to pathophysiology and prognosis, it is very useful in diagnosing and treating patients with lymphocytic leukemia. Attempts at quantitative analysis of cell-surface antigens and expected benefits such as improved detail are also described. Additionally the standardization of cell-surface analysis using flow-cytometry is discussed.

Explore related subjects

Antibodies, MonoclonalAntigens, SurfaceFlow CytometryHematologic DiseasesHumansEnglish AbstractJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

K Nakahara. 2001. [Flow cytometry].. https://pubmed.ncbi.nlm.nih.gov/11391933/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2026

ZrO₂@C-based colorimetric/photothermal dual-mode immunosensor coupled with a novel monoclonal antibody for quantification of Aspergillus ochraceus biomass.

Aspergillus ochraceus contaminates agricultural products and produces nephrotoxic, carcinogenic ochratoxin A (OTA), posing severe food safety hazards. A dual-signal lateral flow immunochromatographic assay (dLFIA) based on ZrO₂@C nanoprobes was established for quantitative detection of A. ochraceus biomass. A novel monoclonal antibody (mAb 4B4) was prepared as the capture antibody to immobilize A. ochraceus mycelial lysate antigen on the test line, and a rabbit polyclonal antibody (pAb G2801) as the detection antibody to modify ZrO₂@C composites (synthesized via UiO-66 pyrolysis) into 200 nm colorimetric/photothermal nanoprobes. This dLFIA achieved limits of detection of 0.164 μg/mL (colorimetric) and 0.517 μg/mL (photothermal). This efficient and reliable method allows quantitative analysis of A. ochraceus biomass, which is suitable for routine monitoring of fungal contamination in agro-food matrices.

Antibodies, Monoclonal↗
PubMed2003

Differences in T-cell immunity toward tumor-associated antigens in colorectal cancer and breast cancer patients.

There is increasing evidence that tumors elicit specific T-cell responses in a substantial proportion of patients. Recently, we have shown that in patients with colorectal cancer specific T cells against the tumor-associated antigens (TAA) Ep-CAM, her-2/neu or CEA can be detected in peripheral blood using IFNgamma-ELISPOT assay. In our study, we have analyzed T-cell responses against HLA-A*0201-restricted epitopes of these TAA in peripheral blood of patients with breast cancer and colorectal cancer. Surprisingly, a complete absence of ex vivo T-cell responses against these TAA was found in 20 patients with breast cancer. In contrast, specific T cells were detectable in 12 of 49 patients with colorectal cancer against at least 1 of these TAA, confirming our previous results. T-cell responses against influenza-derived peptides were similar in both malignancies. The results of our study indicate a difference either of tumor immunogenicity or of the migratory pattern of tumor-specific T cells between breast cancer and colorectal cancer patients. The findings reported here have implications for the development of antigen-specific T-cell therapies.

Antibodies, Monoclonal↗
PubMed2003

Structural analysis of the ErbB-2 receptor using monoclonal antibodies: Implications for receptor signalling.

The extracellular part of ErbB-2 is formed by 4 domains, specifically, L1, L2 that adopt a beta-helical structure and S1, S2 that consist of several cysteine-rich, EGF-fold modules. These ectodomains mediate ErbB-2 dimerisation with itself or with other members of the epidermal growth factor receptor (EGFR) family, events essential to both ErbB-2 signaling and the development of certain malignancies. The anti-ErbB-2 monoclonal antibodies N12, N28 and L87 bind to the polypeptides C531-A586, T216-C235 and C220-C235 respectively. In this study, glycine walking and random mutagenesis were used to further delineate the critical residues involved in antibody binding. A molecular model of ErbB-2 ectodomains was then constructed based on the recently published coordinates of the EGFR (EGFR) model. This model rationalized successfully many features of our epitope mapping, including their location in modules within the S1 and S2 domains and the importance of Arg545, Gln548 and Leu561 for N12 binding. Further investigation of the functional effects of the anti-ErbB-2 monoclonal antibodies demonstrated that N28 strongly stimulated ErbB-2 phosphorylation and MAPK activation whereas N12 had no effect. As bivalency is required for the action of these antibodies we propose that at least 2 different kinds of ErbB-2 homodimers can be formed as relative rotational isomers and that the S1 and S2 domains are instrumental in determining the relative orientations of the ErbB-2 homodimers, such that different signaling effects are induced.

Antibodies, Monoclonal↗