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Immunohistochemical characterization of intracellular J-chain and binding site for secretory component (SC) in human immunoglobulin (Ig)-producing cells. 1983

P Brandtzaeg

J-chain staining of IgA- and IgM-producing immunocytes was significantly enhanced when tissue sections were pretreated with acid urea, apparently because molecular unfolding exposed concealed J-chains. This indicated substantial completion of the Ig polymers at the cytoplasmic level, which was verified by diffuse binding of SC in vitro to the cytoplasm of most J-chain-positive IgA and IgM cells. This process involved specific non-covalent forces which showed the same interrelation as that noted for isolated dimeric IgA and 19S IgM--the latter as well as IgM cells exhibiting stronger binding of SC than the IgA counterparts. Conversely, J-chain staining of IgD and IgG immunocytes was not enhanced by acid urea and these cells did not generally express affinity for SC; rare exceptions could apparently be ascribed to artifacts or dual isotype production including IgA or IgM polymers. Parallel demonstration of J-chain and SC binding seems to be the best available method for studies of polymer-producing immunocyte populations and offers the advantage of in situ evaluation of cell distribution in relation to morphology. The reliability of this approach was attested to by the fact that IgA immunocytes in all secretory tissues investigated (salivary, mammary and lacrimal glands; nasal and intestinal mucosae) expressed J-chain (87-97%) and SC affinity (84-87%) in comparable proportions, indicating that almost 90% of the cells were engaged mainly in dimer production. The observation that most IgD and 50-70% of the IgG immunocytes in secretory tissues expressed J-chain, has implications for the differentiation of B-cell clones homing to such sites. Conversely, IgG cells in extra-glandular tissues showed strikingly reduced J-chain production and such sites contained IgA immunocytes with heterogeneous expression of J-chain and SC affinity. Thus, in the extra-follicular area of palatine tonsils 70-80% of the IgA cells seemed to be pure monomer producers and the remainders apparently generated a mixed product. Most immunocytes in extra-glandular tissues may therefore belong to mature clones with completely or partially repressed J-chain synthesis.

UI MeSH Term Description Entries
D007070 Immunoglobulin A Represents 15-20% of the human serum immunoglobulins, mostly as the 4-chain polymer in humans or dimer in other mammals. Secretory IgA (IMMUNOGLOBULIN A, SECRETORY) is the main immunoglobulin in secretions. IgA,IgA Antibody,IgA1,IgA2,Antibody, IgA
D007072 Immunoglobulin D An immunoglobulin which accounts for less than 1% of plasma immunoglobulin. It is found on the membrane of many circulating B LYMPHOCYTES. IgD,IgD1,IgD2
D007075 Immunoglobulin M A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally was called a macroglobulin. Gamma Globulin, 19S,IgM,IgM Antibody,IgM1,IgM2,19S Gamma Globulin,Antibody, IgM
D007128 Immunoglobulin Fragments Partial immunoglobulin molecules resulting from selective cleavage by proteolytic enzymes or generated through PROTEIN ENGINEERING techniques. Antibody Fragment,Antibody Fragments,Ig Fragment,Ig Fragments,Immunoglobulin Fragment,Fragment, Antibody,Fragment, Ig,Fragment, Immunoglobulin,Fragments, Antibody,Fragments, Ig,Fragments, Immunoglobulin
D007144 Immunoglobulin J-Chains A 15 kDa "joining" peptide that forms one of the linkages between monomers of IMMUNOGLOBULIN A or IMMUNOGLOBULIN M in the formation of polymeric immunoglobulins. There is one J chain per one IgA dimer or one IgM pentamer. It is also involved in binding the polymeric immunoglobulins to POLYMERIC IMMUNOGLOBULIN RECEPTOR which is necessary for their transcytosis to the lumen. It is distinguished from the IMMUNOGLOBULIN JOINING REGION which is part of the IMMUNOGLOBULIN VARIABLE REGION of the immunoglobulin light and heavy chains. Ig J Chains,J-Chains, Immunoglobulin,Ig J-Peptide,Immunoglobulin J Polypeptide,Immunoglobulin J-Peptide,Chains, Ig J,Ig J Peptide,Immunoglobulin J Chains,Immunoglobulin J Peptide,J Chains, Ig,J Chains, Immunoglobulin,J Polypeptide, Immunoglobulin,J-Peptide, Ig,J-Peptide, Immunoglobulin,Polypeptide, Immunoglobulin J
D003593 Cytoplasm The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990) Protoplasm,Cytoplasms,Protoplasms
D005455 Fluorescent Antibody Technique Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy. Antinuclear Antibody Test, Fluorescent,Coon's Technique,Fluorescent Antinuclear Antibody Test,Fluorescent Protein Tracing,Immunofluorescence Technique,Coon's Technic,Fluorescent Antibody Technic,Immunofluorescence,Immunofluorescence Technic,Antibody Technic, Fluorescent,Antibody Technics, Fluorescent,Antibody Technique, Fluorescent,Antibody Techniques, Fluorescent,Coon Technic,Coon Technique,Coons Technic,Coons Technique,Fluorescent Antibody Technics,Fluorescent Antibody Techniques,Fluorescent Protein Tracings,Immunofluorescence Technics,Immunofluorescence Techniques,Protein Tracing, Fluorescent,Protein Tracings, Fluorescent,Technic, Coon's,Technic, Fluorescent Antibody,Technic, Immunofluorescence,Technics, Fluorescent Antibody,Technics, Immunofluorescence,Technique, Coon's,Technique, Fluorescent Antibody,Technique, Immunofluorescence,Techniques, Fluorescent Antibody,Techniques, Immunofluorescence,Tracing, Fluorescent Protein,Tracings, Fluorescent Protein
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000915 Antibody Affinity A measure of the binding strength between antibody and a simple hapten or antigen determinant. It depends on the closeness of stereochemical fit between antibody combining sites and antigen determinants, on the size of the area of contact between them, and on the distribution of charged and hydrophobic groups. It includes the concept of "avidity," which refers to the strength of the antigen-antibody bond after formation of reversible complexes. Affinity, Antibody,Antibody Avidity,Avidity, Antibody,Affinities, Antibody,Antibody Affinities,Antibody Avidities,Avidities, Antibody
D000918 Antibody Specificity The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site. Antibody Specificities,Specificities, Antibody,Specificity, Antibody

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