ARH-77
Cat.No.: CSC-C0521
Species: Homo sapiens (Human)
Source: Blood; Peripheral Blood
Morphology: round single cells or clustered growing in suspension, some cells loosely adherent
Culture Properties: suspension
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D13S317: 11,13
D7S820: 7,12
D16S539: 9,13
vWA: 17
THO1: 8,9.3
Amelogenin: X
TPOX: 8
CSF1PO: 6,10
ARH-77 is a human B-lymphoblastoid cell line that was first isolated from peripheral blood taken from a 33-year-old woman with IgG plasma cell leukemia. It was originally suggested to be a myeloma/plasma cell leukemia cell line. However, further characterization has shown that ARH-77 is an Epstein-Barr virus (EBV)-transformed B lymphoblastoid line, and not a true malignant plasma cell line. ARH-77 cells are grown in suspension as either round cells or cell clusters that may or may not loosely adhere to each other.
Phenotypically, ARH-77 expresses CD11a, CD19, CD20, CD28, CD49e, and does not express CD38. It produces IgG1 with kappa light chain. It is EBV-positive and contains latent viral nuclear and capsid antigens, but does not lytically replicate. In initial studies, ARH-77 was shown to strongly proliferate in immunoglobulin-secreting cell numbers when stimulated by either lymphokines or phorbol myristate acetate (PMA). Isotype switching does not occur. Therefore, ARH-77 has been used as an in vitro model to study B-cell activation and mechanisms of IgG secretion. ARH-77, or its engineered derivatives, are also commonly used in immuno-oncology; they are the host cells for many cytotoxicity assays (ADCC, CDC, ADCP) used in the study of antibody-based and cell-based therapeutics. Fast-growing mutants of ARH-77 (HMy2) have also been incorporated in hybridoma systems for monoclonal antibody production.
BRF1A Inhibits Excessive IgG Production in ARH77 Cells without Cytotoxicity
Myeloma cells relentlessly secrete IgE/IgG and rely on NF-κB, c-Myc, and telomerase for survival. Musa et al. evaluated BRF1A, a cannabidiol-enriched extract, for its ability to curb malignant Ig secretion and growth of U266/ARH-77 myeloma cells.
Musa et al. found that BRF1A suppressed IgE-producing myeloma function, therefore they wanted to see if it had a similar effect on IgG-producing myeloma ARH-77 cells. They cultured ARH-77 cells with 1.0 µM BRF1A for 1, 3, and 5 days. Compared to untreated cultures, IgG production significantly decreased on days 1, 3, and 5 (Fig. 1A-C). Within 24 hours, the IgG concentration in BRF1A-cultured cells was 79 to 144 ng/mL, compared to 185 to 299 ng/mL in untreated cells. The IgG concentration continued to decrease on days 3 and 5. On day 3, the treatment group had IgG concentrations of 46 to 99 ng/mL, while the untreated group had 244 to 316 ng/mL. On day 5, the treatment group had 44 to 94 ng/mL, and the untreated group had 278 to 329 ng/mL. No significant cytotoxicity was observed on days 1 and 3 (Fig. 2A-C). Additionally, CCK-8 assays showed that BRF1A had a similar effect on IgG-producing myeloma cells as on IgE-producing cells (Fig. 2D-F). Thus, BRF1A can suppress both IgE- and IgG-producing myeloma cells, highlighting its potential as a therapeutic agent.
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