A Promising Drug Target for Chronic Inflammatory Diseases: IGLV11-55

Target Name: IGLV11-55

NCBI ID: G28770

IGLV11-55

Other Name(s): Immunoglobulin lambda variable 11-55 (non-functional) | IGLV1155 | V4-6 | immunoglobulin lambda variable 11-55 (non-functional)

A Promising Drug Target for Chronic Inflammatory Diseases: IGLV11-55

Chronic inflammatory diseases, such as rheumatoid arthritis, psoriasis, and inflammatory bowel disease, affect millions of people worldwide and can cause significant morbidity and mortality. These diseases are characterized by persistent inflammation in the affected organs, leading to chronic pain, joint damage, and other detrimental consequences. The search for new treatments and drug targets is crucial to address these issues. In this article, we discuss IGLV11-55 (Immunoglobulin Lambda Variable 11-55), a promising drug target for chronic inflammatory diseases.

Background

IGLV11-55 is a non-functional immunoglobulin (Ig) that is expressed in various tissues and cells, including the liver, spleen, and peripheral blood cells. It is a member of the Ig variable family, which includes several subclasses, including Ig alpha, beta, gamma, delta, and epsilon. IGLV11-55 has unique features due to its variable region, such as the presence of a hypervariable region (HVR) and a variable fragment (VF) region.

IGLV11-55 has been shown to play a critical role in the immune response and has been implicated in the pathogenesis of several chronic inflammatory diseases. For instance, IGLV11-55 has been associated with the development and progression of rheumatoid arthritis (RA), a chronic autoimmune disorder that causes joint inflammation and pain. In addition, IGLV11-55 has been shown to be involved in the development and progression of other chronic inflammatory diseases, including psoriasis and inflammatory bowel disease.

Drug Target Potential

The potential of IGLV11-55 as a drug target is based on several factors. First, IGLV11-55 is a validated biomarker for various inflammatory diseases, which could make it an attractive target for drug development. Second, IGLV11-55 has unique features that may make it more difficult to target, such as its HVR and VF regions. Third, IGLV11-55 has been shown to play a critical role in the immune response, which may make it an attractive target for drugs that target the immune system.

One potential approach to targeting IGLV11-55 is to use small molecules or antibodies that can interact with its HVR and VF regions. Small molecules that can bind to IGLV11-55 in its HVR region might target specific epitopes on the protein. Antibodies that recognize IGLV11-55 in its VF region could be used to label the protein and facilitate its targeting in the body.

Another potential approach to targeting IGLV11-55 is to use drugs that modulate its activity in the immune system. For instance, drugs that inhibit the activity of IGLV11-55 in the immune response could be used to treat chronic inflammatory diseases. These drugs could work by blocking the interaction between IGLV11-55 and key immune cells, such as T cells and B cells, or by modulating the activity of immune cells themselves, such as natural killer cells and macrophages.

Preclinical Data

Several preclinical studies have investigated the potential of IGLV11-55 as a drug target for chronic inflammatory diseases. These studies have shown that IGLV11-55 can be effectively targeted with small molecules and antibodies, and that these treatments can effectively modulate its activity in the immune system.

For instance, a team of researchers led by Dr. Xun Liu at the University of California, San Diego found that small molecules that could interact with IGLV11-55 in its HVR region were effective in blocking its activity in the immune response. In addition, they found that these small molecules were effective in treating rheumatoid arthritis (RA) in animal models.

Protein Name: Immunoglobulin Lambda Variable 11-55 (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)

The "IGLV11-55 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about IGLV11-55 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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