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Lectins are considered a major family of protein antinutrients, which are specific sugar-binding proteins exhibiting reversible carbohydrate-binding activities. [32] Lectins are similar to antibodies in their ability to agglutinate red blood cells. [33] Many legume seeds have been proven to contain high lectin activity, termed hemagglutination ...
All three known members of the selectin family (L-, E-, and P-selectin) share a similar cassette structure: an N-terminal, calcium-dependent lectin domain, an epidermal growth factor (EGF)-like domain, a variable number of consensus repeat units (2, 6, and 9 for L-, E-, and P-selectin, respectively), a transmembrane domain (TM) and an intracellular cytoplasmic tail (cyto).
These glycan-Siglec interactions allow cells to bind one another, allowing signalling in some cases, or in the case of Sialoadhesin, pathogen uptake. Sialoadhesin's function was originally thought to be important in binding to red blood cells. Sialoadhesin lacks a cytosolic ITIM or a positive residue to bind ITAM-containing adaptors and so is ...
Phytohaemagglutinin (PHA, or phytohemagglutinin) is a lectin found in plants, especially certain legumes. PHA actually consists of two closely related proteins, called leucoagglutinin (PHA-L) and PHA-E. These proteins cause blood cells to clump together. PHA-E cause erythrocytes (red blood cells) to clump.
The subsequent complement cascade catalyzed by C3-convertase results in creating a membrane attack complex, which causes lysis of the pathogen as well as altered-self in the context of apoptotic and necrotic cells. MBL/MASP-1 complex also has thrombin-like activity (thrombin clots fibrin to initiate blood clots).
Concanavalin A (ConA) is a lectin (carbohydrate-binding protein) originally extracted from the jack-bean (Canavalia ensiformis).It is a member of the legume lectin family. It binds specifically to certain structures found in various sugars, glycoproteins, and glycolipids, mainly internal and nonreducing terminal α-D-mannosyl and α-D-glucosyl groups.
A C-type lectin (CLEC) is a type of carbohydrate-binding protein known as a lectin. [3] The C-type designation is from their requirement for calcium for binding. [4] Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis.
CD69 (Cluster of Differentiation 69) is a human transmembrane C-Type lectin protein encoded by the CD69 gene. It is an early activation marker that is expressed in hematopoietic stem cells, T cells, and many other cell types in the immune system. [5] It is also implicated in T cell differentiation as well as lymphocyte retention in lymphoid organs.