LDL Receptor, also known as LDLR, is a mosaic protein which belongs to the Low density lipoprotein receptor gene family. The low density lipoprotein receptor (LDLR) gene family consists of cell surface proteins involved in receptor-mediated endocytosis of specific ligands. LDL Receptor consists of 840 amino acids (after removal of signal peptide) and mediates the endocytosis of cholesterol-rich LDL. Low density lipoprotein (LDL) is normally bound at the cell membrane and taken into the cell ending up in lysosomes where the protein is degraded and the cholesterol is made available for repression of microsomal enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase, the rate-limiting step in cholesterol synthesis. At the same time, a reciprocal stimulation of cholesterol ester synthesis takes place. LDL Receptor is a cell-surface receptor that recognizes the apoprotein B100 which is embedded in the phospholipid outer layer of LDL particles. The receptor also recognizes the apoE protein found in chylomicron remnants and VLDL remnants.
Mouse Legumain,also known as LGMN, is a cysteine protease belonging to peptidase family C13 and is expressed in kidney and placenta abundantly. LGMN has a strict specificity for hydrolysis of asparaginyl bonds. It can also cleave aspartyl bonds slowly, especially under acidic conditions. The mammalian legumain is involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. It plays a role in the regulation of cell proliferation via its role in EGFR degradation. Legumain deficiency causes the accumulation of pro-Cathepsins B, H and L, another group of lysosomal cysteine proteases. Overexpression of Legumain in tumors is significant for invasion/metastasis. Mammalian legumain is inhibited by iodoacetamide and maleimides. Legumain activation appears to be autocatalytic and can be triggered by acidic pH.
The Mammalian Legumain, also known as LGMN, also called asparaginyl endopeptidase (AEP), is a cysteine protease belonging to peptidase family C13 with a strict specificity for hydrolysis of asparaginyl bonds. Known previously only from plants and invertebrates, Legumain is discovered as a lysosomal endopeptidase in mammals. Mammalian Legumain is a cysteine endopeptidase, inhibited by iodoacetamide and maleimides, but unaffected by compound E64. The Mammalian Legumain is involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Legumain has been observed to be highly expressed in several types of solid tumors. It was demonstrated in membrane-associated vesicles concentrated at the invadopodia of tumor cells and on cell surfaces where it colocalized with integrins. Legumain was demonstrated to activate progelatinase A. Cells overexpressing Legumain possessed increased migratory and invasive activity in vitro and adopted an invasive and metastatic phenotype in vivo, inferring significance of Legumain in tumor invasion and metastasis. In addition, Legumain is expressed in both murine and human atherosclerotic lesions. The macrophage-specific expression of Legumain in vivo and ability of Legumain to induce chemotaxis of monocytes and endothelial cells in vitro suggest that Legumain may play a functional role in atherogenesis.
Leptin receptor (OB-R), also named B219, is a type I cytokine receptor family protein with an significant amino acid sequence identity with an gp130, G-CSF receptor, and the LIF receptor. Multiple isoforms of Human and Mouse OB-R, including a long form (OB-RL) with an a large cytoplasmic domain capable of signal-transduction, and several receptor isoforms with an short cytoplasmic domains (OB-Rs) lacking signal-transducing capabilities, have been identified. The extracellular domains of the short and long forms of OB-R are identical. An OB-R transcript lacking a transmembrane domain and potentially encoding a soluble form of the receptor has also been described. Circulating soluble OB-R, complexed to leptin, has been detected in Mouse serum. Serum soluble OB-R levels have been shown to increase during pregnancy. OB-RL transcripts were reported to be expressed predominantly in regions of the hypothalamus previously thought to be important in body weight regulation. Expression of OB-Rs transcripts have been found in multiple tissues, including the choroid plexus, lung, kidney and primitive hematopoietic cell populations. OB-R has recently been shown to be encoded by the Mouse diabetes (db) and rat fatty (fa) genes. Rodents homozygous for the db or fa mutations have been known to exhibit an obesity phenotype. Mouse OB-R long form encodes a 1162 amino acid (aa) residue precursor protein with an a 22 aa residue signal peptide, an 817 aa residue extracellular domain, a 21 aa residue transmembrane domain, and a 302 aa residue cytoplasmic domain. The extracellular domain of OB-R contains two hemopoietin receptor domains, a fibronectin type III domain and the WSXWS domain. Recombinant murine soluble OB-R has been shown to bind leptin with an high affinity and is a potent leptin antagonist.
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