CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumor growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.
PCK1 (Phosphoenolpyruvate carboxykinase 1, also PEPCK-C [cytosolic]) is a monomeric, 67-68 kDa member of the PEP carboxykinase family of enzymes. It is expressed in postnatal cells such as mammary epithelium, white and brown adipocytes, skeletal muscle cells and hepatocytes. PCK1 has multiple functions, some of which are cell-specific. In particular, PCK1 has both cataplerotic (Greek: to fill down, or remove) and anaplerotic (to fill up, or replace) activity, where it removes and replaces elements of the TCA cycle. It is also gluconeogenic, and promotes glucose formation via PEP generation. Finally, it is glyceroneogenic, creating glycerol-3-phosphate that is used to reesterify and store just-released free fatty acids in adipocytes. It contains one kinase domain (aa 27-615), and two potential acetylation sites at Lys70 and 71. There are four potential splice forms. Two have alternative start sites at Met460 and Met315, while two others show a deletion of aa 34-546, plus a three aa substitution for aa 85-204, respectively.
Pepsinogen C, also known as PGC, is an aspartic proteinase that belongs to the peptidase family A1. Pepsinogen C is synthesized in the gastric mucosa as inactive precursors, known as zymogens. Pepsinogen C contains a prosegment that serves to stabilize the inactive form and prevent entry of the substrate to the active site. At low PH conditions, Pepsinogen C undergoes conversion into active enzyme. Pepsinogen C has been found expressed in all regions of the stomach mucosa and also in the proximal duodenal mucosa. In stomach cancer tissues and cancer cell lines, the expressions of the pepsinogen genes were decreased or lost, in good accordance with their pepsinogen productions. No gross structural changes of the pepsinogen genes were observed in these cancers, but the methylation patterns of the pepsinogen genes were found to be altered in different ways in different cancers. Serum levels of Pepsinogen C are used as a biomarker for certain gastric diseases including Helicobacter pylori related gastritis.
PNLIPRP1, also known as PLRP1, belongs to the AB hydrolase superfamily, Lipase family. PNLIPRP1 is structurally similar to PLRP2. However, these two proteins display different functional properties. PNLIPRP1 may function as inhibitor of dietary triglyceride digestion. It lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters. PLRP2 hydrolyses milk fat with a lower catalytic efficiency than that of PL. PLRP2 activity, higher on homogenized than on native milk fat, is differently influenced by fatty acids and colipase depending on a proteolytic cleavage in the lid domain.
Podoplanin, also known asPDPN, is a type-I integral membrane glycoprotein with diverse distribution in human tissues. The physiological function of this protein may be related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor. The specific function of this protein has not been determined. Alternatively spliced transcript variants encoding different isoforms have been identified.PDPN is a mucin-type glycoprotein negatively charged by extensive O-glycosylation and a high content of sialic acid, which expresses the adhesive property. It is selectively expressed in lymphatic endothelium as well as lymphangiomas, Kaposi sarcomas, and in a subset of angiosarcomas with probable lymphatic differentiation. PDPN may contribute to form odontoblastic fiber or function as the anchorage to the tooth development and in proliferating epithelial cells of cervical loop and apical bud. The intensity of podoplanin expression is negatively correlated with the expression of CD34 and factor VIII. Podoplanin would be useful as a diagnostic marker for epithelioid hemangioendothelioma in liver tumors.
Peroxisome Proliferator-Activated Receptor alpha (PPAR alpha , NR1C1) is a member of the Nuclear Receptor superfamily. PPAR alpha exhibits the highest affinity with unsaturated fatty acids, and linolenic acids. PPAR alpha is expressed in brown fat, liver, kidney, heart, mucosa of the stomach and duodenum, retina, adrenal gland, skeletal muscle, pancreatic islets and smooth muscle cells. PPAR alpha plays important roles in lipid and glucose metabolism, and has been implicated in obesity-related metabolic diseases such as hyperlipidemia, insulin resistance, and coronary artery disease. Three members have been identified and are called PPAR alpha, δ, and lambda. Retinoid X Receptor (RXR) is an obligate partner for PPAR.
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