scholarly journals Gouania willdenowi is a teleost fish without immunoglobulin genes

2019 ◽  
Author(s):  
Serafin Mirete-Bachiller ◽  
David N. Olivieri ◽  
Francisco Gambón-Deza
Keyword(s):  
Detailed Analysis ◽  
Heavy Chain ◽  
Teleost Fish ◽  
Chromosomal Region ◽  
Light Chains ◽  
Immunoglobulin Genes ◽  
Protein Molecules ◽  
V Genes ◽  
Lymphocyte Receptors

AbstractIn the study of immunoglobulin V genes in fish genomes, we found that the species Gouania willdenowi does not possess any such regions, neither for the heavy chain nor for the light chains. Also, genes that code for the immunoglobulin constant regions were also not found. A detailed analysis of the chromosomal region of these genes revealed a deletion in the entire locus for regions of the heavy and light chains. These studies provide evidence that this species does not possess genes coding for immunoglobulins. Additionally, we found the genes that code for CD79a and CD79b protein molecules have also been deleted. Regions for the Tα/β lymphocyte receptors are present but the T γ/δ receptors were not found. In transcripts of two other Gobiesocidae species, Acystus sp. and Tomicodon sp., no antibody sequences could be detected, possibly indicating the absence of immunoglobulins in all species of this family.

The variability, arrangement, and rearrangement of immunoglobulin genes

1980 ◽  
Vol 58 (3) ◽  
pp. 176-187 ◽  
Author(s):  
T. H. Rabbitts ◽  
P. H. Hamlyn ◽  
G. Matthyssens ◽  
B. A. Roe
Keyword(s):  
Heavy Chain ◽  
Cdna Clone ◽  
Variable Region ◽  
Immunoglobulin Genes ◽  
Constant Region ◽  
Cross Hybridization ◽  
Heavy Chain Variable Region ◽  
Human Dna ◽  
V Genes

The multiplicity of heavy-chain variable-region (VH) genes in mouse and human DNA has been estimated using a mouse heavy- (H) chain cDNA clone. We found about 10 hybridization components in mouse DNA and about 20 components in human DNA. Cross-hybridization studies of variable region (V) genes indicate that these components represent the numbers of genes within the VH subgroups of each of these species. The arrangement and rearrangement of the H-chain γ subclasses have been studied in order to assess possible mechanisms of the H-chain switch. Evidence has been found for rearrangement events involving the γ2a and γ2b constant-region (CH) genes in DNA from cells making IgG2a and IgG2b respectively. In addition we found that cells making IgG2a lack detectable genes for γ1 and γ2b. Both sets of observations are discussed in relation to H-chain diversity and the switch.

scholarly journals Genetic analysis of self-associating immunoglobulin G rheumatoid factors from two rheumatoid synovia implicates an antigen-driven response.

1992 ◽  
Vol 175 (3) ◽  
pp. 831-842 ◽  
Author(s):  
T Olee ◽  
E W Lu ◽  
D F Huang ◽  
R W Soto-Gil ◽  
M Deftos ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heavy Chain ◽  
Immunoglobulin M ◽  
Natural Antibody ◽  
Antibody Repertoire ◽  
Rheumatoid Factors ◽  
Variable Regions ◽  
Genetic Origins ◽  
V Genes ◽  
Vh Gene

Although much has been learned about the molecular basis of immunoglobulin M (IgM) rheumatoid factors (RFs) in healthy individuals and in patients with mixed cryoglobulinemia and rheumatoid arthritis, little is known about the genetic origins of the potentially pathogenic IgG RFs in the inflamed rheumatoid synovia of patients. Recently, we generated from unmanipulated synovium B cells several hybridomas that secreted self-associating IgG RFs. To delineate the genetic origins of such potentially pathogenic RFs, we adapted the anchored polymerase chain reaction to rapidly clone and characterize the expressed Ig V genes for the L1 and the D1 IgG RFs. Then, we identified the germline counterparts of the expressed L1 IgG RF V genes. The results showed that the L1 heavy chain was encoded by a Vh gene that is expressed preferentially during early ontogenic development, and that is probably located within 240 kb upstream of the Jh locus. The overlap between this RF Vh gene and the restricted fetal antibody repertoire is reminiscent of the natural antibody-associated Vh genes, and suggests that at least part of the "potential pathogenic" IgG RFs in rheumatoid synovium may derive from the "physiological" natural antibody repertoire in a normal immune system. Indeed, the corresponding germline Vh gene for L1 encodes the heavy chain of an IgM RF found in a 19-wk-old fetal spleen. Furthermore, the comparisons of the expressed RF V genes and their germline counterparts reveal that the L1 heavy and light chain variable regions had, respectively, 16 and 7 somatic mutations, which resulted in eight and four amino acid changes. Strikingly, all eight mutations in the complementarity determining regions of the V gene-encoded regions were replacement changes, while only 6 of 11 mutations in the framework regions caused amino acid changes. Combined with L1's high binding affinity toward the Fc fragment, these results suggest strongly that the L1 IgG RF must have been driven by the Fc antigen.

In vitro and in vivo expression of a nephritogenic Ig heavy chain determinant: Pathogenic autoreactivity requires permissive light chains

2001 ◽  
Vol 79 (3) ◽  
pp. 222-230 ◽  
Author(s):  
Brenda G Cooperstone ◽  
Mohammed M Rahman ◽  
Earl H Rudolph ◽  
Mary H Foster
Keyword(s):  
Heavy Chain ◽  
Light Chains ◽  
In Vivo Expression ◽  
Ig Heavy Chain

Nuclear transcripts of mouse heavy chain immunoglobulin genes contain only the expressed class of C-region sequences

Science ◽  
1979 ◽  
Vol 204 (4397) ◽  
pp. 1087-1088 ◽  
Author(s):  
K. Marcu ◽  
U Schibler ◽  
R. Perry
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin Genes

scholarly journals Myosins and pathology: genetics and biology.

2002 ◽  
Vol 49 (4) ◽  
pp. 789-804 ◽  
Author(s):  
Maria Jolanta Redowicz
Keyword(s):  
Hypertrophic Cardiomyopathy ◽  
Myosin Heavy Chain ◽  
Inner Ear ◽  
Heavy Chain ◽  
Hair Cells ◽  
Familial Hypertrophic Cardiomyopathy ◽  
Light Chains ◽  
Myosin Isoforms ◽  
Cardiac Myosin ◽  
Genes Encoding

This article summarizes current knowledge on the genetics and possible molecular mechanisms of Human pathologies resulted from mutations within the genes encoding several myosin isoforms. Mutations within the genes encoding some myosin isoforms have been found to be responsible for blindness (myosins III and VIIA), deafness (myosins I, IIA, IIIA, VI, VIIA and XV) and familial hypertrophic cardiomyopathy (beta cardiac myosin heavy chain and both the regulatory and essential light chains). Myosin III localizes predominantly to photoreceptor cells and is proved to be engaged in the vision process in Drosophila. In the inner ear, myosin I is postulated to play a role as an adaptive motor in the tip links of stereocilia of hair cells, myosin IIA seems to be responsible for stabilizing the contacts between adjacent inner ear hair cells, myosin VI plays a role as an intracellular motor transporting membrane structures within the hair cells while myosin VIIA most probably participates in forming links between neighbouring stereocilia and myosin XV probably stabilizes the stereocilia structure. About 30% of patients with familial hypertrophic cardiomyopathy have mutations within the genes encoding the beta cardiac myosin heavy chain and both light chains that are grouped within the regions of myosin head crucial for its functions. The alterations lead to the destabilization of sarcomeres and to a decrease of the myosin ATPase activity and its ability to move actin filaments.

scholarly journals Affinity labelling of the binding site of rabbit antibody. Evidence for the involvement of the hypervariable regions of the heavy chain

1974 ◽  
Vol 139 (1) ◽  
pp. 135-149 ◽  
Author(s):  
Christopher E. Fisher ◽  
Elizabeth M. Press
Keyword(s):  
Binding Site ◽  
Heavy Chain ◽  
Binding Sites ◽  
Light Chains ◽  
Rabbit Antibody ◽  
Heavy Chains ◽  
Group 4 ◽  
Hypervariable Regions ◽  
Affinity Labelling ◽  
Antibody Complex

The binding sites of rabbit antibodies with affinity for the haptenic group 4-azido-2-nitrophenyl-lysine have been specifically labelled by photolysis of the hapten–antibody complex. The extent of covalent labelling was 0.5–0.9mol of hapten bound/mol of antibody and, by using an immunoadsorbent, antibody with 1.3mol of hapten/mol was obtained. The antibody was specifically labelled in the binding site and the ratio of labelling of heavy and light chains was in the range 3.3–5.0. The labelled heavy chains were cleaved by CNBr treatment and after reduction and alkylation of the intrachain bonds, were digested with trypsin. Evidence is presented that two regions of the heavy chain, positions 29–34 and 95–114, together contain about 80% of the label on the heavy chain; these two regions respectively include two of the hypervariable regions of rabbit heavy chain.

scholarly journals Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment

1968 ◽  
Vol 106 (1) ◽  
pp. 15-21 ◽  
Author(s):  
B. Frangione ◽  
C. Milstein ◽  
Edward C. Franklin
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
The Other ◽  
Light Chains ◽  
Fc Fragment ◽  
Heavy Chains ◽  
Human Immunoglobulins ◽  
Other Hand ◽  
Terminal Loop ◽  
Heavy Chain Disease

The disulphide bridges of the Fc fragment (C-terminal half of the heavy chain) have been studied in several human immunoglobulins, containing heavy chains of different antigenic types (γ1, γ2, γ3 and γ4), and in heavy-chain-disease proteins. Two intrachain disulphide bridges were found to be present. The sequences appear to be identical in the Fc fragments of two types of chain studied (γ1 and γ3), and very similar to corresponding sequences of the Fc fragment in rabbit. These results suggest that the C-terminal half of the heavy chains is covalently folded (in a similar fashion to the light chains) with a C-terminal loop and an N-terminal loop. The similarity is emphasized by comparison of the sequence and location of the disulphide-bridged peptides of the C-terminal loop of heavy and light chains. The N-terminal loop, on the other hand, appears to be very different in Fc fragments and light chains. The C-terminal loop is the only one present in the F′c fragment.

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