PNLIP is an enzyme which belongs to the lipase family. Secreted from the pancreas, PNLIP is the primary lipase that hydrolyzes dietary fat molecules in the human digestive system, converting triglyceride substrates found in ingested oils to monoglycerides and free fatty acids. Bile salts secreted from the liver and stored in gallbladder are released into the duodenum where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers (2 free fatty acids and one 2-monoacylglycerol) are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal.
Phospholipid transfer protein, also known as Lipid transfer protein II and PLTP, is a secreted protein which belongs to theBPI/LBP/Plunc superfamily and BPI / LBP family. PLTP is nearly ubiquitously expressed in cells and tissues. PLTP converts HDL into larger and smaller particles. It may play a key role in extracellular phospholipid transport and modulation of hdl particles. High-density lipoproteins (HDL) play a major protective role against the development of coronary artery disease. PLTP is a main factor regulating the size and composition of HDL in the circulation and plays an important role in controlling plasma HDL levels. This is achieved via both the phospholipid transfer activity of PLTP and its capability to cause HDL conversion. PLTP is one of the key lipid transfer proteins in plasma and cerebrospinal fluid. It is involved in novel intracellular functions. PLTP is an important modulator of lipoprotein metabolism, including interparticle phospholipid transfer, remodeling of HDL, cholesterol and phospholipid efflux from peripheral tissues, and the production of hepatic VLDL. PLTP also plays an important role in inflammation and oxidative stress. Accordingly, PLTP has also been implicated in the development of atherosclerosis.
Phosphomannomutase 1 (PMM1) blongs to the eukaryotic PMM family. Phosphomannomutase 1 can catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose which required for a number of critical mannosyl transfer reactions. PMM1 is highly expressed in liver, heart, brain, and pancreas, but lower expression in skeletal muscle. In addition, PMM1 may be responsible for the degradation of glucose-1,6 bisphosphate in ischemic brain.
Phosphomannomutase 2 (PMM2) is an enzyme that is a member of the highly variable methyltransferase superfamily. PMM2 is a cytoplasmic protein and catalyzes the isomerization of mannose 6-phosphate to mannose 1-phosphate.In addition, PMM2 involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose that required for a number of critical mannosyl transfer reactions. Defects in PMM2 can results in congenital disorder of glycosylation type 1A (CDG1A). Congenital disorders of glycosylation are metabolic deficiencies in glycoprotein biosynthesis that usually cause severe mental and psychomotor retardation.
Myelin P2 Protein (PMP2) is a cytoplasmic protein which belongs to the Fatty-acid binding protein (FABP) family of calycin superfamily. PMP2 is a small, basic, and cytoplasmic lipid binding protein of peripheral myelin. PMP2 is found in peripheral nerve myelin and spinal cord myelin, the oligodendrocytes and Schwann cells, respectively. PMP2 may be involved in lipid transport protein in Schwann cells. It may decrease the inhibitory effect of T suppressors in the culture of immune lymph node cells.
Pancreatic Lipase-Related Protein 1 (PNLIPRP1) belongs to the Lipase family within the AB hydrolase superfamily. PNLIPRP1 is a secreted protein and contains one PLAT domain. PNLIPRP1 is involved in lipid metabolic process, acting as a negative regulator of pancreatic lipase activity by competing with pancreatic lipase for colipase occupancy. PNLIPRP1 may play a role in inhibiting dietary triglyceride digestion, but it lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters.
Podocin, encoded by the NPHS2 gene, is an approximately 50 kDa membrane protein that plays an important role in podocyte function in the kidney. Loss of Podocin function results in albuminuria, hypercholesterolemia, hypertension, and renal failure. Human Podocin consists of a 102 amino acid (aa) cytoplasmic domain, a 21 aa intramembrane segment, and a second 262 aa cytoplasmic domain. Alternative splicing generates a short isoform with a 68 aa deletion in the second cytoplasmic domain. Within aa 259-383 (the region common to both isoforms), human Podocin shares 90% aa sequence identity with mouse and rat Podocin. Podicin localizes to areas of cell-cell contact between podocytes in the renal glomerulus. It associates into oligomers and forms complexes with Nephrin, CAR, ZO-1, and the cation ion channel TRPC6. It contributes to podocyte function by regulating the activation of TRPC6 and Nephrin mediated signaling. Multiple polymorphisms in NPHS2 are associated with steroid-resistant nephrotic syndrome.
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