What has Toll-like receptor 4?

TLR4 is expressed on the cell surface on both hematopoietic and nonhematopoietic cells, including endothelial cells [3], cardiac myocytes [4], and cells of the central nervous system (CNS) [5].

What happens when TLR4 is activated?

TLR4 is a transmembrane protein, member of the toll-like receptor family, which belongs to the pattern recognition receptor (PRR) family. Its activation leads to an intracellular signaling pathway NF-κB and inflammatory cytokine production which is responsible for activating the innate immune system.

What cell types have TLR4?

TLR4 (CD284) is primarily known for binding lipopolysacaride (LPS). It is also expressed on a range of cell types, including dendritic cells, neutrophils, mast cells, and B cells. Its role in the recognition of LPS involves several collaborating proteins, such as LPS-binding protein (LBP), CD14, and MD2.

Where is TLR4 located?

Within pancreatic islets, TLR4 is expressed in beta cells; palmitate induces inflamed pancreatic beta cell dysfunction in vivo by activating inflammatory responses in islets [74].

What is the function of toll-like receptors?

Toll-like receptors (TLRs) are a class of pattern recognition receptors (PRRs) that initiate the innate immune response by sensing conserved molecular patterns for early immune recognition of a pathogen (1).

What do Toll-like receptors detect?

microbes
Toll-like receptors (TLRs) recognize microbes by binding to pathogen-associated molecular patterns. Abbreviations: lipopolysaccharide (LPS), lipoteichoic acid (LTA), lipoproteins (LP), glycophosphatidylinositol (GPI).

Why is it called toll-like receptors?

TLRs received their name from their similarity to the protein coded by the toll gene.

Where is TLR4 found?

Tocris Summary for TLR4 Gene TLRs generally exist as homodimers (heterodimers have been reported) and are found on immune cells; macrophages, B lymphocytes and mast cells.

Do humans have TLR4?

The human TLR4 consists of an extracellular domain of 624 amino acids (residues 1–624), a transmembrane domain of 33 amino acids (residues 625–658), a proximal cytoplasmic domain of 159 amino acids (residues 659–818), and a distal cytoplasmic domain of 19 amino acids (residues 819–838).