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The natural abundance of lambda2-light chains in inbred mice
The Journal of Experimental Medicine
|November 1, 1978
Summary
Mouse myeloma protein M315
Area of Science:
- Immunology
- Molecular Biology
- Genetics
Background:
- The constant (C) domain of mouse myeloma protein M315 light chain is unique.
- Immunoglobulins (Igs) are crucial for immune response.
Purpose of the Study:
- To identify and characterize the L315 light chain in normal mouse serum.
- To investigate the presence and levels of lambda2 chains in various mouse strains.
- To explore the relationship between lambda2 chains and immune responses, particularly to dinitrophenyl (Dnp).
Main Methods:
- Serological analysis using antiserum to the C-domain of L315.
- Carboxypeptidase A analysis of normal light chains.
- Quantification of immunoglobulin levels in mouse serum.
- Immunization studies with Dnp-KLH and KLH.
Main Results:
- Approximately 1% of normal mouse serum Igs possess L315-type (lambda2) light chains.
- All 35 inbred mouse strains studied exhibited lambda2 chains, with varying serum levels.
- Mice immunized with Dnp-KLH showed a 3-5 fold increase in lambda2 compared to controls.
- Serum immunoglobulin molecules bearing the lambda2 variable region (VL315) were detectable and increased upon Dnp-KLH immunization.
Conclusions:
- Lambda2 chains are a distinct subset of mouse immunoglobulin light chains present across inbred strains.
- The presence and levels of lambda2 chains are influenced by immune stimulation, particularly with Dnp antigens.
- Lambda2 chains can be further categorized into subsets based on their variable (V) domain similarity to VL315, suggesting genetic and functional diversity.