Polymeric immunoglobulin receptor, also known asPIGR, is a member of the immunoglobulin superfamilyand aFc receptor. The ectodomain of this receptor consists of five units with homology to the variable units of immunoglobulins and a transmembrane region, which also has some homology to certain immunoglobulin variable regions. PIGR is expressed on several glandular epithelia including those of liver and breast. The deduced amino-acid sequence has a length of 764 residues and shows an overall similarity of 56% and 64% with the rabbit and rat counterpart. PIGR mediates transcellular transport of polymeric immunoglobulin molecules, and thus facilitates the secretion ofIgAandIgM. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment of PIGR.
PIGR binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment.
The human Polymeric Immunoglobulin Receptor (pIgR) is a 100 kDa type I transmembrane glycoprotein. Its precursor is 764 amino acids. It contains an 18 amino acid signal sequence, a 620 amino acid extracellular region, a 23 amino acid transmembrane fragment, and a 103 amino acid cytoplasmic domain. pIgR is synthesized by secretory epithelial cells with five Ig-like domains in extracellular region, and transfer to the basolateral plasma membrane. For IgA and IgM polymers, in addition to α-heavy chains and light Ig chains, a short polypeptide named joining chain (J chain) is also contained and required. pIgR can bind larger polymers of IgA (pIgA) and pentameric IgM as a carrier that transports IgA and IgM across epithelium. The receptor-ligand complexes are endocytosed and transcytosed to the apical surface, then proteolytic cleavage of the sixth extracellular domain of pIgR and generate secretory IgA (SIgA), the pIgR fragment is referred to as secretory component (SC). SIgA is a important component of the mucosal immune system. SC is anti-microbial properties and protects SIgA from proteolytic degradation
Polymeric immunoglobulin receptor, also known as ,PIGR, is a member of the immunoglobulin superfamily ,and a ,Fc receptor. The ectodomain of this receptor consists of five units with homology to the variable units of immunoglobulins and a transmembrane region, which also has some homology to certain immunoglobulin variable regions. PIGR is expressed on several glandular epithelia including those of liver and breast. The deduced amino-acid sequence has a length of 764 residues and shows an overall similarity of 56% and 64% with the rabbit and rat counterpart. PIGR mediates transcellular transport of polymeric immunoglobulin molecules, and thus facilitates the secretion of ,IgA ,and ,IgM. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment of PIGR.
Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.
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