C-type lectin domain family 1, member B (CLEC1B), also known as CLEC-2, is a protein encoded by the CLEC1B gene in humans. This protein is a member of the C-type lectin superfamily, which is characterized by their ability to bind carbohydrates in a calcium-dependent manner . CLEC1B is a type II transmembrane receptor that plays a crucial role in various physiological processes, including platelet activation, angiogenesis, and immune and inflammatory responses .
CLEC1B is a protein-coding gene that produces a receptor known for its involvement in platelet aggregation and immune responses . The protein contains a C-type lectin-like domain, which is essential for its carbohydrate-binding properties. This domain allows CLEC1B to interact with specific ligands, such as the lymphatic endothelial marker podoplanin (PDPN) and the platelet-aggregating snake venom protein rhodocytin .
Upon ligand binding, CLEC1B undergoes a series of intracellular signaling events. These events include the activation of SRC and SYK tyrosine kinases, leading to the activation of phospholipase C gamma 2 (PLCG2). This signaling cascade ultimately results in platelet activation and aggregation, which are critical for hemostasis and thrombosis .
CLEC1B has been implicated in various diseases, particularly those involving the immune system and cancer. For instance, CLEC1B expression is associated with hepatocellular carcinoma (HCC), where it serves as a potential prognostic biomarker . Studies have shown that CLEC1B expression is downregulated in HCC, and its low expression levels are correlated with poor prognosis . Additionally, CLEC1B is involved in the regulation of immune cell infiltration in the tumor microenvironment, suggesting its role as an immunomodulator .
The clinical significance of CLEC1B extends beyond its role in cancer. As a receptor involved in platelet activation, CLEC1B is also relevant in the context of cardiovascular diseases and bleeding disorders. Its interaction with PDPN and rhodocytin highlights its importance in maintaining vascular integrity and preventing excessive bleeding .
Moreover, the recombinant form of CLEC1B (human recombinant) is utilized in research and therapeutic applications. Recombinant proteins are produced through genetic engineering techniques, allowing for the study of protein function and the development of targeted therapies. Human recombinant CLEC1B can be used to investigate its role in various physiological and pathological processes, providing valuable insights into its potential therapeutic applications.