Decorin is a ubiquitous small cellular or pericellular matrix proteoglycan and is closely related in structure to biglycan protein. It belongs to the small leucine-rich proteoglycan (SLRP) family and consists of a core protein and a covalently linked glycosaminoglycan chain which is either chondroitin sulfate (CS) or dermatan sulfate (DS). As a component of connective tissue, decorin interacts with several extracellular matrix components, such as type I collagen and fibronectin, and plays a role in matrix assembly. Decorin resides in the tumor microenvironment and affects the biology of various types of cancer by downregulating the activity of several receptors involved in cell growth and survival. Decorin binds to and modulates the signaling of the epidermal growth factor receptor and other members of the ErbB family of receptor tyrosine kinases. It exerts its antitumor activity by a dual mechanism: via inhibition of these key receptors throμgh their physical downregulation coupled with attenuation of their signaling, and by binding to and sequestering TGFbeta. Decorin also modulates the insulin-like growth factor receptor and the low-density lipoprotein receptor-related protein 1, which indirectly affects the TGFbeta receptor pathway. Decorin plays significant roles in tissue development and assembly, as well as playing both direct and indirect signaling roles.
Decorin is a secreted chondroitin/dermatan sulfate proteoglycan in the family of small leucine-rich proteoglycans (SLRPs). SLRP family members are characterized by N-terminal and C-terminal cysteine-rich regions which flank the central region containing 10-12 tandem leucine-rich repeats (LRR). The human Decorin cDNA encodes a 359 amino acid (aa) precursor that includes a 16 aa signal sequence and a 14 aa propeptide. Alternate splicing of human Decorin generates five isoforms with variable length deletions. Decorin is an N-glycosylated protein that also carries a variablysized hybrid chondroitin/dermatan sulfate chain at Ser34. Decorin regulates assembly of the extracellular collagen matrix and the bioactivity of the matrix associated growth factors FGF2;GDF8/Myostatin; TGFβ;and WISP1. It also binds and activates EGF R; ErbB4; and IGFI-R. In vivo; Decorin promotes myoblast differentiation; supports angiogenesis; and inhibits tumor progression.
Dectin-1 was recently identified as the most important receptor for beta-glucan. It is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans, and is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. Recognition of beta-glucan by dectin-1 triggers effective immune response, including phagocytosis and proinflammatory factor production, to eliminate infecting fungi, which especially benefits immunocompromised patients against opportunistic fungal infection. In addition, dectin-1 is involved in the adaptive immune response as well as autoimmune diseases and immune tolerance. Dectin-1 can recognize and respond to live fungal pathogens and is being increasingly appreciated as having a key role in the innate responses to these pathogens. In addition to its exogenous ligands, Dectin-1 can recognize an unidentified endogenous ligand on T cells and may act as a co-stimulatory molecule. Recent studies have highlighted the importance of Dectin-1 in anti-fungal immunity, in both mice and humans, and have suggested a possible involvement of this receptor in the control of mycobacterial infections.
Dectin-1 was recently identified as the most important receptor for beta-glucan. It is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans, and is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. Recognition of beta-glucan by dectin-1 triggers effective immune response, including phagocytosis and proinflammatory factor production, to eliminate infecting fungi, which especially benefits immunocompromised patients against opportunistic fungal infection.
Defensins are cationic peptides. It is an important ingredient of the innate immune system. β-defensins are expressed on some leukocytes and epithelial surfaces. Four human β-Defensins have been identified to date: BD-1, BD-2, BD-3 and BD-4. β-defensins contain a six-cysteine motif, they forms three intra-molecular disulfide bonds. β-defensins are also chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors; they are released by proteolytic cleavage of a signal sequence.
The DEFB1 gene, encoding for the constitutively expressed human beta-defensin 1 (hBD1) antimicrobial peptide is a potential candidate when studying genetic susceptibility to caries. DEFB1 genetic variations have been reported as contributing to hBD1 production impairment, leading to a greater susceptibility to be infected by oral pathogens, also leading to periodontitis. To counteract host immunity, Cryptosporidium parvum has evolved multiple strategies to suppress host antimicrobial defense. One such strategy is to reduce the production of the antimicrobial peptide beta-defensin 1 (DEFB1) by host epithelial cells. Beta-Defensin-1, an antimicrobial peptide encoded by the DEFB1 gene, is known to play an important role in lung mucosal immunity.
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