IGHV7-81 as A Potential Drug Target for Hematological Malignancies

Target Name: IGHV7-81

NCBI ID: G28378

IGHV7-81

Other Name(s): IGHV781 | immunoglobulin heavy variable 7-81 (non-functional) | Immunoglobulin heavy variable 7-81 (non-functional)

IGHV7-81 as A Potential Drug Target for Hematological Malignancies

IGHV7-81 (IGHV781) is a non-coding RNA (ncRNA) that has been identified as a potential drug target (or biomarker) in the context of human hematological malignancies. IGHV7-81 is a long non-coding RNA molecule that is expressed in various tissues and cell types, including blood cells, tissues, and organs. It is characterized by its ability to bind to and enter into the nuclear compartments of target cells, where it can interact with various nuclear proteins and contribute to the regulation of gene expression.

Recent studies have identified IGHV7-81 as a potential drug target in the context of several hematological malignancies, including acute myeloid leukemia (AML), myelodysplastic syndromes (MDS), and multiple myeloma (MM). In these diseases, IGHV7-81 is often overexpressed or underexpressed compared to its matched control tissue, and it has been shown to play a role in the development and progression of these diseases.

One of the key mechanisms through which IGHV7-81 contributes to the development and progression of hematological malignancies is its ability to promote the transformation of normal cells into cancerous cells. This process is known as oncogenic transformation, and it is a critical step in the development of cancer. IGHV7-81 has been shown to promote the oncogenic transformation of normal blood cells into leukemia cells in cell culture models, and it has also been shown to contribute to the development of leukemia in animal models.

Another mechanism through which IGHV7-81 contributes to the development and progression of hematological malignancies is its ability to inhibit the apoptosis (programmed cell death) of cancer cells. Apoptosis is a natural process that helps eliminate damaged or dysfunctional cells in the body, and it is an important checkpoint against cancer. However, cancer cells often evade apoptosis and continue to divide and proliferate uncontrollably. IGHV7-81 has been shown to inhibit the apoptosis of cancer cells, which may contribute to their survival and the development of cancer.

IGHV7-81 has also been shown to contribute to the development and progression of hematological malignancies by regulating the expression of genes involved in cell growth, differentiation, and inflammation. For example, IGHV7-81 has been shown to promote the expression of genes involved in the production of factors that promote cell growth and differentiation, such as GATA1 and NF-E2. These factors can contribute to the oncogenic transformation of normal cells. IGHV7-81 has also been shown to regulate the expression of genes involved in inflammation, such as TLR4 and MyD88. These genes can contribute to the production of pro-inflammatory cytokines, which can contribute to the development of cancer.

In conclusion, IGHV7-81 is a non-coding RNA that has been identified as a potential drug target (or biomarker) in the context of human hematological malignancies. Its ability to bind to and enter into the nuclear compartments of target cells, as well as its ability to promote the transformation of normal cells into cancerous cells and inhibit the apoptosis of cancer cells, make IGHV7-81 a promising target for the development of new treatments for hematological malignancies. Further research is needed to fully understand the mechanisms through which IGHV7 -81 contributes to the development and progression of hematological malignancies, and to determine its safety and efficacy as a potential drug.

Protein Name: Immunoglobulin Heavy Variable 7-81 (non-functional)

Functions: Probable non-functional open reading frame (ORF) of V region of the variable domain of immunoglobulin heavy 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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