Clec4E: A Promising Drug Target and Biomarker for the Superfamily Member 9 (C-Type Lectins)

Target Name: CLEC4E

NCBI ID: G26253

CLEC4E

Clec4E: A Promising Drug Target and Biomarker for the Superfamily Member 9 (C-Type Lectins)

Introduction

The C-type lectins, also known as carbohydrate-recognition domain (CRD) proteins, are a family of transmembrane proteins that play a crucial role in various physiological processes, including cell adhesion, migration, and signaling. These lectins are involved in many different cellular processes, including the regulation of cell surface carbohydrates, which are essential for various cellular functions. One of the most well-studied C-type lectins is Clec4E, which is a member of the superfamily member 9 (SMM) and has been shown to play a critical role in various cellular processes.

In this article, we will explore Clec4E, its functions, and potential as a drug target and biomarker. We will discuss the current state of research on Clec4E and its potential as a drug, as well as its potential applications in various fields, including drug development, diagnostics, and biotechnology.

FUNCTION AND PURPOSE

Clec4E is a 23-kDa protein that is expressed in various tissues and cells, including epithelial, hematopoietic, and neural cells. Clec4E is a type I transmembrane protein that consists of an N-terminal cytoplasmic domain, a single transmembrane segment, and an C -terminal carbohydrate-binding domain (CBD). Clec4E functions by recognizing and interacting with specific carbohydrates, which are essential for various cellular processes, including cell adhesion, migration, and signaling.

POTENTIAL AS A DRUG TARGET

Clec4E has been shown to be a potential drug target due to its unique structure and its ability to interact with specific carbohydrates. Several studies have shown that Clec4E can interact with various carbohydrates, including glycophorin A, which is a transmembrane protein that is expressed in most tissues and is involved in cell adhesion. Furthermore, Clec4E has been shown to interact with integrins, which is a cytoskeleton protein that plays a role in cell migration.

Clec4E has also been shown to interact with the protein E-cadherin, which is a transmembrane protein that is involved in cell-cell adhesion. E-cadherin is a glycosylated protein that is involved in various signaling pathways, including the regulation of cell growth, differentiation, and angiogenesis.

SOME POTENTIAL BENEFITS OF Clec4E AS A DRUG TARGET

If Clec4E can be successfully targeted and inhibited, it has the potential to be a drug for various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. For example, Clec4E has been shown to be involved in the regulation of cancer cell growth and has the potential to be a therapeutic target for cancer. Additionally, Clec4E has been shown to be involved in the regulation of neurodegenerative diseases, including Alzheimer's disease, and has the potential to be a therapeutic target for these diseases.

Another potential benefit of Clec4E as a drug target is its potential to treat autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis. Clec4E has been shown to be involved in the regulation of immune cell function and has the potential to be a therapeutic target for these diseases.

IMPACT OF Clec4E ON THE DESCRIPTION OF THE SUPERFAMILY MEMBER 9

The C-type lectins, including Clec4E, belong to the superfamily member 9 (SMM) and have been shown to play a critical role in various cellular processes, including

Protein Name: C-type Lectin Domain Family 4 Member E

Functions: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage-associated molecular patterns (DAMPs) of abnormal self and pathogen-associated molecular patterns (PAMPs) of bacteria and fungi (PubMed:18509109, PubMed:23602766). The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions (PubMed:23602766, PubMed:24101491). Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells (By similarity). Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (By similarity). Also recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation (By similarity). Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue (By similarity)

The "CLEC4E 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 CLEC4E comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   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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