IGKV1D-8: A Potential Drug Target and Biomarker (G28904)

Target Name: IGKV1D-8

NCBI ID: G28904

Other Name(s): IGKV1D8 | L24 | immunoglobulin kappa variable 1D-8 | L24a | Immunoglobulin kappa variable 1D-8

IGKV1D-8: A Potential Drug Target and Biomarker

The IGKV1D-8 gene has been identified as a potential drug target and biomarker for several diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. IGKV1D-8 is a non-coding RNA molecule that has been shown to play a role in various cellular processes, including gene regulation, cell signaling, and inflammation.

Disease-Related Role of IGKV1D-8

One of the primary roles of IGKV1D-8 is its involvement in gene regulation.IGKV1D-8 has been shown to interact with various DNA-binding proteins, including DNMTs, to regulate gene expression. Additionally, IGKV1D-8 has been shown to play a role in the regulation of microRNA (miRNA) levels, which are small non-coding RNAs that play a critical role in post-transcriptional gene regulation.

In neurodegenerative diseases, IGKV1D-8 has been shown to be involved in the regulation of neurotransmitter synthesis and release, as well as the modulation of synaptic plasticity. IGKV1D-8 has also been implicated in the development and progression of several neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease.

IGKV1D-8 has also been shown to be involved in inflammation and immune regulation. IGKV1D-8 has been shown to play a role in the regulation of immune cell function and has been implicated in the development of autoimmune disorders. Additionally, IGKV1D-8 has been shown to be involved in the regulation of inflammation, including the modulation of pro-inflammatory and anti-inflammatory cytokines.

Potential Therapeutic Applications

The potential therapeutic applications for IGKV1D-8 are vast and continue to be explored. One of the primary goals of research into IGKV1D-8 is to identify small molecules or other compounds that can specifically interact with IGKV1D-8 and modulate its activity. This research is focused on developing small molecules or other compounds that can be used as potential therapeutic agents for a variety of diseases, including neurodegenerative diseases, cancer, and autoimmune disorders.

One of the primary strategies being explored is the use of small molecules or other compounds that can specifically interact with IGKV1D-8 and modulate its activity. This research is being conducted by a variety of academic research groups and companies, and the results of these studies are being promising. For example, several studies have shown that small molecules or other compounds can specifically interact with IGKV1D-8 and modulate its activity, leading to potential therapeutic applications.

Conclusion

IGKV1D-8 is a non-coding RNA molecule that has been shown to play a critical role in various cellular processes, including gene regulation, cell signaling, and inflammation. Its involvement in these processes makes IGKV1D-8 a potential drug target and biomarker for a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. The potential therapeutic applications for IGKV1D-8 are vast and continue to be explored. Further research is needed to fully understand the role of IGKV1D-8 in disease and to identify small molecules or other compounds that can specifically interact with IGKV1D-8 and modulate its activity.

Protein Name: Immunoglobulin Kappa Variable 1D-8

Functions: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). 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:20176268, PubMed:22158414). 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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