L-Lactate Dehydrogenase B Chain (LDH-B) is a member of the lactate dehydrogenase family that consists of three members, LDH-A, LDH-B and LDH-C, members of this family function as powerful markers for germ cell tumors. LDH-B is an oxidoreductase that catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. It converts pyruvate to lactate when oxygen is absent or in short supply and it performs the reverse reaction during the Cori cycle in the liver. It is also called Hydroxybutyrate Dehydrogenase (HBD) due to its ability to catalyze the oxidation of hydroxybutyrate.
Possible role in sperm motility.
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.
Low-Density Lipoprotein Receptor (LDLR) is a transmembrane glycoprotein that plays a critical role in cholesterol homeostasis. LDLR mediates blood cholesterol level by interacting with lipoprotein particles like LDL and VLDL. The extracellular domain of LDLR contains LDL receptor type A (ligand-binding) modules (LA repeats), epidermal growth factor-like modules, and LY repeats containing the YWTD consensus motif that are important in binding and releasing of ApoB-100 and ApoE in lipoprotein particles. The C terminal domain of LDLR inside the cell is required for the receptor internalization. Loss of function mutations in the LDLR gene causes Familial Hypercholesterolemia (FH).
LDL Receptor, also known as LDLR, is a mosaic protein that 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.
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