Elafin is a secreted protein. Elafin consists of two domains: the transglutaminase substrate domain (cementoin moiety) and the elastase inhibitor domain. The transglutaminase substrate domain serves as an anchor to localize Elafin covalently to specific sites on extracellular matrix proteins. It is shown that Elafin can be used as a biomarker for graft versus host disease of the skin. Elafin is expressed in the skin during wound healing through activation of the epidermal growth factor receptor. Elafin may prevent elastase-mediated tissue proteolysis.
This gene encodes a protein that is induced by the steroid hormone progesterone and plays a role in the maintenance of pregnancy. The encoded protein regulates multiple facets of the immune system to promote normal pregnancy including cytokine synthesis, natural killer (NK) cell activity, and arachidonic acid metabolism. Low serum levels of this protein have been associated with spontaneous pre-term labor in humans. This protein may promote the proliferation, migration and invasion of glioma. [provided by RefSeq, Mar 2017]
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.
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