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Pentraxins are plasma proteins characterized by their pentameric discoid assembly and their Ca2+ dependent ligand binding, such as Serum amyloid P component (SAP) and C-reactive Protein (CRP), which are cytokine-inducible acute-phase proteins implicated in innate immunity. CRP binds to ligands containing phosphocholine, SAP binds to amyloid fibrils, DNA, chromatin, fibronectin, C4-binding proteins and glycosaminoglycans. “Long“ pentraxins have N-terminal extensions to the common pentraxin

Monocyte chemoattractant protein-1 (MCP-1) called also monocyte chemotactic protein-1. MCP-1 is an 8.6kDa protein and belongs to the family of chemotactic cytokines known as Chemokines . MCP-1 is expressed by monocytes, vascular endothelial cells, smooth muscle cells, glomerular mesangial cell, osteoblastic cells, and human pulmonary type-2-like epithelial cells in culture. MCP-1 exhibits chemotactic activity for monocytes/macrophages, basophils, T lymphocytes, particularly memory T cells ａn

Interleukins (ILs) are a large group of cytokines that are produced mainly by leukocytes, although some are produced by certain phagocytes and auxiliary cells. Each IL acts on a specific, limited group of cells through a receptor specific for that IL. Interleukin 1 (IL1), originally known as lymphocyte activating factor (LAF), activates T cells and lymphocytes, which then proliferate and secrete interleukin 2. IL1 is primarily released from stimulated macrophages and monocytes, but also is

This gene is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. The protein encoded by this gene is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on th

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronecti

IgM normally constitutes about 10% of serum immunoglobulins. IgM antibody is prominent in early immune responses to most antigens and is largely confined to plasma due to it's large size. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. Due to it's high valency IgM is more efficient than other isotypes is binding antigens with repeating epitopes (virus particles and red blood cells) and is more efficient tha