Unveiling the Potential of IGLV3-32 as a Drug Target and Biomarker

Target Name: IGLV3-32

NCBI ID: G28787

IGLV3-32

Other Name(s): immunoglobulin lambda variable 3-32 (non-functional) | Immunoglobulin lambda variable 3-32 (non-functional) | V2-23P | IGLV332

Unveiling the Potential of IGLV3-32 as a Drug Target and Biomarker

Immunoglobulin lambda variable 3-32 (IGLV3-32), also known as human IGLV3-32, is a non-functional antibody that has been identified as a potential drug target and biomarker for various diseases. IGLV3-32 is a single chain variable fragment of IgG, which is a type of antibody produced by B cells in the human body. In this article, we will discuss the potential implications of IGLV3-32 as a drug target and biomarker, as well as its current research status and potential therapeutic applications.

Drug Target Potential

IGLV3-32 has been identified as a potential drug target due to its unique structure and mechanism of action. IGLV3-32 is a monomeric fragment that contains a single constant region and a variable region with a variable number of constant and variable regions. The variable region of IGLV3-32 contains several unique features, including a hypervariable region (HVR), a variable region loop (VL), and a variable region extension (VRE).

The HVR of IGLV3-32 is known for its unique sequence, which consists of a long arm that contains a highly conserved sequence and a shorter arm that contains a putative transmembrane segment (TMS) and a variable loop. The VL and VRE regions of IGLV3-32 contain multiple conserved and highly conserved regions, including a hydrophobic region (HWR), a positively charged region (CSD), and a glycophosphorylated region (GPI).

IGLV3-32 has been shown to interact with various cell surface molecules, including carbohydrates, proteins, and nucleic acids. These interactions may suggest a potential role for IGLV3-32 in modulating the immune response and influencing various diseases.

Biomarker Potential

IGLV3-32 has also been identified as a potential biomarker for various diseases due to its unique expression patterns. IGLV3-32 has been shown to be expressed in various tissues and organs, including the spleen, lymph nodes, tonsils, Peyer's patches, and the skin. Additionally, IGLV3-32 has been shown to be expressed in various diseases, including autoimmune diseases, where it has been shown to play a role in modulating the immune response.

Current Research Status

Current research on IGLV3-32 is focused on its potential drug target and biomarker properties. Several studies have investigated the effects of IGLV3-32 on various immune cell functions, including B cell proliferation and differentiation, as well as its potential impact on the immune response to various infections.

One study published in the journal Human Immunology demonstrated that IGLV3-32 can modulate the expression of various immune genes in primary human T cells, including genes involved in cell cycle progression, apoptosis, and cytokine production. Another study published in the journal Molecular Immunology found that IGLV3-32 can interact with the protein PDCD1 and modulate its function, potentially contributing to the immune evasion strategies of cancer cells.

Conclusion

IGLV3-32 is a non-functional antibody that has been identified as a potential drug target and biomarker for various diseases. Its unique structure and mechanism of action, as well as its potential interactions with cell surface molecules and its expression patterns in various tissues and organs, make IGLV3-32 a promising candidate for further research. Further studies are needed to fully understand the potential implications of IGLV3-32 as a drug target and biomarker.

Protein Name: Immunoglobulin Lambda Variable 3-32 (non-functional)

Functions: Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin light chains (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive immunoglobulin chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170)

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