| 2024 |
J-chain (JC) outcompetes the sixth IgM subunit during assembly of IgM pentamers. Before insertion into IgM, JC exists as largely unstructured, protease-sensitive species with heterogeneous non-native disulfide bonds. JC interacts with hydrophobic β-sheets selectively exposed by nascent pentamers, and completion of an amyloid-like core triggers JC folding and drives disulfide rearrangements that covalently stabilize JC-containing pentamers. The quality control factor ERp44 surveys IgM assembly and prevents secretion of aberrant conformers. |
In vitro reconstitution, in cellula assembly assays, protease sensitivity assays, disulfide bond analysis |
The EMBO journal |
High |
39632981
|
| 1993 |
The Ets-related transcription factor PU.1 is the nuclear protein (NF-JB) that mediates positive regulatory activity of the JB element in the J-chain promoter. PU.1 binds the JB site despite it lacking the canonical GGA Ets core, and a glutamine-rich sequence in the amino-terminal portion of PU.1 is required for transcriptional activation. A dominant negative PU.1 mutant suppresses transcriptional activity of a 1.2-kb J-chain promoter. |
Protein purification, DNA-binding characterization, transient transfection reporter assays, dominant-negative mutagenesis |
Genes & development |
High |
8406004
|
| 1992 |
A bifunctional promoter element (JB, located between -75 and -45) in the J-chain gene acts as a repressor in J-chain-silent B cells and as an activator in J-chain-expressing cells. IL-2 signaling triggers the activator function of JB through a B-cell-specific nuclear protein NF-JB, making JB the likely target of the IL-2 signal. |
Deletion analysis of 5' flanking region, nuclear factor binding assays, transient transfection reporter assays |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
1631082
|
| 1991 |
IL-2 and IL-5 each trigger a decrease in binding of two promoter-specific nuclear repressor proteins to the J-chain promoter, preceding the appearance of J-chain RNA. The two lymphokines act additively, their effects are reversed upon withdrawal, and both are inhibited by IL-4, indicating the IL-2 and IL-5 signal pathways converge to regulate repressor activities of J-chain promoter elements. |
Inducible β-lymphoma cell line, J-chain RNA expression analysis, nuclear factor binding assays, lymphokine withdrawal and IL-4 inhibition experiments |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
1763018
|
| 1986 |
Activation of the J-chain gene during B-cell differentiation to IgM-secreting cells is associated with chromatin remodeling at the 5' end of the gene: a 240-bp region is nuclease-resistant in immature B cells, becomes slightly more accessible in mature B cells, and displays an open DNase I-hypersensitive structure in IgM-secreting cells. This open structure is coinducible with J-chain gene expression in mitogen-stimulated lymphocytes. |
Nuclease sensitivity/DNase I hypersensitivity assays in lymphoid cell lines and mitogen-stimulated lymphocytes |
Molecular and cellular biology |
Medium |
3025626
|
| 2006 |
Stage-specific expression of the IgJ gene in plasma cells is regulated by chromatin accessibility and histone acetylation: hypersensitive site 1 on the IgJ promoter opens in plasma cells, and H3 and H4 histones at the IgJ gene chromatin are hyperacetylated in plasma cells but not in pre-B cells. IL-2 treatment of the BCL1 model cell line induces hyperacetylation of H3 and H4 at the IgJ gene chromatin. |
DNase I hypersensitivity mapping, chromatin immunoprecipitation for histone acetylation, IL-2 stimulation of BCL1 cells |
Journal of immunology |
Medium |
17015728
|
| 2023 |
The N459-glycan on the IgA1-Fc tailpiece is essential for dimer formation in the presence of J-chain (N459Q mutant fails to form proper dimer and instead generates higher-order aggregates). The N49-glycan on J-chain and the N263-glycan on IgA1-Fc both contribute to thermal stability of the Fc–J-chain complex. Fluorescence experiments indicate the N459-glycans cover a hydrophobic surface that prevents excess Fc molecules from approaching the dimeric IgA. |
Site-directed mutagenesis of N-glycosylation sites, mass spectrometry, fluorescence assays, thermofluor (thermal shift) assay, NMR of 13C-labeled Fc |
Biochimica et biophysica acta. General subjects |
High |
38070292
|
| 1983 |
J-chain in IgA- and IgM-producing cells is substantially incorporated into polymeric Ig complexes at the cytoplasmic level; acid-urea pretreatment enhances J-chain staining, indicating molecular unfolding exposes concealed J-chains. The completed polymers bind secretory component (SC) in vitro via specific non-covalent forces at the cytoplasm of J-chain-positive IgA and IgM cells. IgM cells exhibit stronger SC binding than IgA cells. IgG and IgD cells do not generally express affinity for SC. |
Immunohistochemistry with acid-urea pretreatment, in vitro SC binding to tissue sections |
Molecular immunology |
Medium |
6417474
|
| 1983 |
In lymphoblastoid cell lines, J-chain is present in disulfide-linked form in IgM and IgA producers but in free (non-disulfide-linked) form in IgG cells; intracellular J-chain is not disulfide-linked to IgG in IgG/J-chain-producing cells. In PWM-stimulated PBL, J-chain is secreted only in disulfide-linked form associated with polymeric Ig and not as a free form. Subcellular fractionation showed J-chain and Ig associate with fractions containing ribosomes, cell sap, and low molecular weight RNA. |
Immunoprecipitation, immunofluorescence, RIA, subcellular fractionation, biosynthetic labeling |
Molecular immunology |
Medium |
6417475
|
| 1976 |
Structural analysis of a human Fc5μ-like fragment showed that J-chain is covalently linked as a 'clasp' within a single IgM subunit (within the 95 kDa subunit) and not between two subunits, as determined by partial reduction, alkylation, and peptide sequence analysis. |
Partial reduction and alkylation, SDS-PAGE, peptide structural analysis |
Biochimica et biophysica acta |
Medium |
821533
|
| 2007 |
J-chain protein is expressed in a subset of CD11c+ dendritic cells (DC) in mice. J-chain knockout mice have reduced fractions of CD4-/CD8α+ and mPDCA-1+ DC in the spleen, reduced IDO RNA in spleen, fewer IDO-expressing cells in lymph nodes, reduced IDO protein in splenic CD11c+ cells, lower serum kynurenine/tryptophan ratio (indicating reduced IDO activity), and are less susceptible to tolerance induction. |
Flow cytometry, J-chain knockout mice, IDO RNA and protein quantification, serum kynurenine/tryptophan ratio measurement, tolerance induction assays |
Immunology |
Medium |
18028376
|
| 2006 |
J-chain-deficient mice show normal primary IgG responses but compromised secondary IgG responses and reduced B cell repertoire switching from lambda to kappa. Adoptive transfer experiments demonstrated that the compromised secondary immune response is transferred with T cells from J-/- mice, establishing that J-chain deficiency causes a selective defect in T helper cell function that impairs B cell memory formation. |
J-chain knockout mice, immunization with NP-hapten, serum IgG measurement, B cell repertoire analysis, adoptive transfer experiments |
European journal of immunology |
Medium |
16688681
|
| 2005 |
A Stat5-overlapping sequence in the IgJ enhancer is essential for enhancer function in plasma cells and is bound by a ubiquitous protein (not Stat5 or other tested Stat family members, <52 kDa), as identified by in vivo footprinting and EMSA. The opened chromatin of the IgJ enhancer is maintained in plasma cells even in the absence of IL-2/Stat5 signaling. |
In vivo footprinting, EMSA with competitors and antibodies, UV-crosslinking/SDS-PAGE, reporter assays |
Biochemical and biophysical research communications |
Low |
16288984
|
| 2006 |
The HSS3/4 enhancer of the Crlz1-IgJ locus is bound by EBF (early B cell factor) specifically in pre-B cells, as shown by EMSA with oligo-DNA competitors, anti-EBF antibodies, and mutational analysis demonstrating that mutations within the EBF site impair HSS3/4 enhancer activity in pre-B cells but not in plasma cells. |
EMSA with competitors and anti-EBF antibodies, in vivo footprinting, enhancer reporter assay with EBF-site mutations |
Immunology letters |
Medium |
16962668
|
| 2023 |
IGJ overexpression in breast cancer cells suppresses proliferation, invasion, and metastasis in vivo and in vitro by inhibiting epithelial-to-mesenchymal transition (EMT) and suppressing nuclear translocation of p65 (NF-κB). Rescue experiments confirmed that IGJ restricts breast cancer cell proliferation and metastasis via the NF-κB signaling pathway. |
CCK-8 assay, invasion/migration assays, scratch tests, in vivo xenograft, western blot, immunofluorescence for p65 nuclear translocation, GSEA/KEGG analysis, rescue experiments |
International journal of oncology |
Medium |
37539706
|
| 2024 |
IGJ knockdown in rheumatoid arthritis fibroblast-like synoviocytes (MH7A cells) inhibits cell growth, suppresses inflammatory response, and blocks cell motility. Mechanistically, IGJ knockdown suppresses the NF-κB signaling axis in these cells. |
CCK-8 and flow cytometry for growth, ELISA and immunoblot for inflammation, transwell assay for motility, immunoblot for NF-κB pathway components |
International journal of rheumatic diseases |
Low |
39091178
|
| 2025 |
IGJ overexpression in NALM-6 B-ALL cells via CRISPRa leads to increased metabolic activity and confers resistance to dexamethasone, cytarabine, doxorubicin, and methotrexate but not cyclophosphamide, suggesting IGJ promotes metabolic reprogramming contributing to chemoresistance. |
CRISPRa-mediated IGJ overexpression, Seahorse XF metabolic assays, resazurin-based chemoresistance viability assays |
Pediatric blood & cancer |
Low |
41048199
|
| 1988 |
J-chain expression during plasma cell differentiation is independent of immunoglobulin gene rearrangement status. EBV-transformed immunoglobulin-negative precursor B cells with no detectable Ig gene rearrangements still generate subpopulations producing high levels of J-chain, with J-chain production confined to cells that have exited the cell cycle to undergo plasma-cell differentiation. |
Immunoprecipitation after biosynthetic labeling, Northern blot hybridization, immunofluorescence, surface antigen analysis |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
2829207
|