IGHD: A Potential Drug Target for Cancer, Autoimmune Disorders and Neurodegenerative Diseases

Target Name: IGHD

NCBI ID: G3495

IGHD

Other Name(s): immunoglobulin heavy constant delta | Ig delta chain C region WAH | Ig delta chain C region NIG-65 | IGHD_HUMAN | Immunoglobulin heavy constant delta

IGHD: A Potential Drug Target for Cancer, Autoimmune Disorders and Neurodegenerative Diseases

Immunoglobulin heavy constant delta (IGHD) is a protein that is expressed in various tissues throughout the body. It is a type of immunoglobulin, which is a protein that is composed of four polypeptide chains. IGHD is different from other immunoglobulins in that it has a higher constant value than other immunoglobulins. This higher constant value is due to the presence of a variable region on the protein that is responsible for the recognition of antigens.

IGHD has been identified as a potential drug target and biomarker for various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. In this article, we will discuss the biology and potential drug targets of IGHD.

Biography of IGHD

IGHD is a type of immunoglobulin that is characterized by its high constant value. This high constant value is due to the presence of a variable region on the protein that is responsible for the recognition of antigens. IGHD has four polypeptide chains and is expressed in various tissues throughout the body, including the liver, spleen, kidney, and pancreas.

IGHD is involved in various physiological processes in the body, including immune response, inflammation, and tissue repair. It is a key player in the immune system and plays a crucial role in protecting the body against foreign particles and diseases.

Potential Drug Targets

IGHD has been identified as a potential drug target for various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. One of the main reasons for its potential as a drug target is its unique structure and biology.

In cancer, IGHD has been shown to be overexpressed in various types of cancer, including breast, ovarian, and colorectal cancer. This overexpression is thought to contribute to the development and progression of these diseases. Therefore, targeting IGHD with drugs that can inhibit its expression could be an effective way to treat cancer.

In autoimmune disorders, IGHD has been shown to play a role in the development and progression of autoimmune diseases, including rheumatoid arthritis, lupus, and multiple sclerosis. Therefore, targeting IGHD with drugs that can modulate its activity could be an effective way to treat these disorders.

In neurodegenerative diseases, IGHD has been shown to be involved in the development and progression of various neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. Therefore, targeting IGHD with drugs that can inhibit its expression could be an effective way to treat these diseases.

Conclusion

IGHD is a protein that is expressed in various tissues throughout the body and is involved in various physiological processes in the body. It has been identified as a potential drug target and biomarker for various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. The unique structure and biology of IGHD make it an attractive target for drug development, with the potential to improve treatment outcomes for these diseases.

Targeting IGHD with drugs that can inhibit its expression could be an effective way to treat these diseases and improve patient outcomes. Further research is needed to understand the biology and pharmacology of IGHD, as well as the potential drug targets it has.

Protein Name: Immunoglobulin Heavy Constant Delta

Functions: Constant region of immunoglobulin heavy chains. 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:17576170, PubMed:20176268). IgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. The membrane-bound IgD (mIgD) induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. Soluble IgD (sIgD) concentration in serum below those of IgG, IgA, and IgM but much higher than that of IgE. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. After the antigen binds to the B-cell receptor, the secreted form sIgD is shut off. IgD is a potent inducer of TNF, IL1B, and IL1RN. IgD also induces release of IL6, IL10, and LIF from peripheral blood mononuclear cells. Monocytes seem to be the main producers of cytokines in vitro in the presence of IgD (PubMed:8774350, PubMed:10702483, PubMed:11282392)

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