Inflammation

MyD88, also called myeloid differentiation primary response gene 88, encodes a cytosolic adapter protein that plays an essential role in innate and adaptive immune responses. The innate immune system recognizes the presence of bacterial pathogens through the expression of a family known as Toll-like receptors (TLRs).

Platelet endothelial cell adhesion molecule PECAM1 (also called CD31) is a 130 kDa type I transmembrane glycoprotein that is expressed on most cells of the hematopoietic lineage including platelets, monocytes, neutrophils and certain lymphocyte subsets (1). It has also been suggested that PECAM-1 contributes to endothelial cell barrier function.

Pathogenic microorganisms utilize a variety of cell surface receptors to gain entry into host cells and to bypass the natural defense mechanisms. One of the most prominent receptors used in this fashion is the leukocyte adhesion receptor CD11b/c.

MCP1, also known as CCL2, is a small chemokine factor belonging to the CC chemokine family. It is predominantly produced by endothelial cells and macrophages, and specifically is a chemoattractant for monocytes and basophils. It is produced by a wide range of cell types in reaction to diverse inflammatory stimuli including tissue injury, infection, and inflammation.

Nuclear Factor kappa B (NFkB) binds to the kappa-beta site of the immunoglobulin kappa light chain gene enhancer. Thus NFkB has become one of the widely studied transcription factors in innate and adaptive immune responses.

The beta-2 integrins, a family of four cell surface transmembrane glycoproteins expressed only on leukocytes, include CD11a/CD18, CD11b/CD18, CD11c/CD18, and CD11d/CD18. They consist of a common beta subunit (CD18) and homologous alpha subunits (CD11a-d) that bind noncovalently to form an alpha/beta heterodimer.

Toll-like receptor 9 (TLR9) is a member of the toll-like receptor family that plays a key role in pathogen recognition and activation of innate immunity. Scientists using TLR9 antibodies have found the protein is highly conserved from Drosophila to humans, with a high degree of structural and functional homology (1,2).

Myeloid differentiation primary response gene 88 (MYD88) encodes a cytosolic adapter protein that plays an essential role in innate and adaptive immune responses.

Perforin, also known as the pore-forming protein, pfp, is a 70 kD cytolytic protein expressed in the cytoplasmic granules of cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells.

The myeloid differentiation protein MyD88 (myeloid differentiation primary response protein) was originally identified and characterized as a primary upregulated response gene in interleukin-6 mediated myeloid differentiation.