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.
Podoplanin is a type-1 transmembrane protein that belongs to Podoplanin family. PDPN expressed in various specialized cell types throughout the body. It highly expressed in placenta; lung; skeletal muscle and brain; weakly expressed in brain; kidney and liver. In placenta; PDPN expressed on the apical plasma membrane of endothelium; in lung; expressed in alveolar epithelium. PDPN physiological function is related to its mucin-type character. PDPN may be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes; induces changes in cell morphology with transfected cells showing an elongated shape; numerous membrane protrusions; and major reorganization of the actin cytoskeleton; increased motility and decreased cell adhesion. It requires for normal lung cell proliferation and alveolus formation at birth and Induces platelet aggregation. Nevertheless; it doesn’t have any effect on amino acid transport and the aquaporin-type water channels.
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.
This gene encodes a member of the sialomucin protein family. The encoded protein was originally identified as an important component of glomerular podocytes. Podocytes are highly differentiated epithelial cells with interdigitating foot processes covering the outer aspect of the glomerular basement membrane. Other biological activities of the encoded protein include: binding in a membrane protein complex with Na+/H+ exchanger regulatory factor to intracellular cytoskeletal elements, playing a role in hematopoetic cell differentiation, and being expressed in vascular endothelium cells and binding to L-selectin.
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