Glycan Binding Proteins

Surfactant protein D (SP-D) is synthesized and secreted by lung epithelial cells. It belongs to group III of the family of C-type lectins and members of this group has overall structure consisting of multiple globular 'head' regions linked by triple-helical, collagen-like, strands. This group also includes SP-A and the serum proteins mannan-binding protein, conglutinin and collectin-43, all of which have been shown to bind to the C1q receptor found on a wide variety of cells. Both SP-D and SP-A have been shown to enhance oxygen radical production by alveolar macrophages.

Surfactant protein D (SP-D) is synthesized and secreted by lung epithelial cells. It belongs to group III of the family of C-type lectins and members of this group has overall structure consisting of multiple globular 'head' regions linked by triple-helical, collagen-like, strands. This group also includes SP-A and the serum proteins mannan-binding protein, conglutinin and collectin-43, all of which have been shown to bind to the C1q receptor found on a wide variety of cells. Both SP-D and SP-A have been shown to enhance oxygen radical production by alveolar macrophages.

Mannan-binding lectin (MBL), also called mannose-binding lectin or protein, belongs to the C-type family of collectins, showing calcium-dependent binding to certain sugars. It consists of oligomers of triple-chain subunits and its binding and complement activating activities depend on its normal oligomerization. On binding to mannan-like microbial surface carbohydrates, MBL activates the complement system by means of its own lectin pathway, depending on the MBL-associated serine proteases (MASPs).

Mannan-binding lectin (MBL), also called mannose-binding lectin or protein, belongs to the C-type family of collectins, showing calcium-dependent binding to certain sugars. It consists of oligomers of triple-chain subunits and its binding and complement activating activities depend on its normal oligomerization. On binding to mannan-like microbial surface carbohydrates, MBL activates the complement system by means of its own lectin pathway, depending on the MBL-associated serine proteases (MASPs).

Mannan-binding lectin (MBL), also called mannose-binding lectin or protein, belongs to the C-type family of collectins, showing calcium-dependent binding to certain sugars. It consists of oligomers of triple-chain subunits and its binding and complement activating activities depend on its normal oligomerization. On binding to mannan-like microbial surface carbohydrates, MBL activates the complement system by means of its own lectin pathway, dependent on the MBL-associated serine proteases (MASPs).