UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. As a result, energy is dissipated in the form of heat. May play a role in the modulation of tissue respiratory control. Participates in thermogenesis and energy balance.
Uteroglobin-Related Protein 1 (UGRP1) belongs to the secretoglobin family which has been suggested to play a role in lung inflammation and allergic diseases. UGRP1 is a 17 kDa secreted homodimeric protein that shows amino acid sequence similarity with uteroglobin. UGRP1 is expressed predominantly in the lung and low levels of expression are detected in the thyroid. Expression of UGRP1 in lung epithelial cells is enhanced by IL-10 and decreased through the activities of IL-9 and IL-5. UGRP1 interacts with the macrophage scavenger receptor with collagenous structure which is expressed by alveolar macrophages in the lung. It have suggested that UGRP1 may be involved in inflammation and pathogen clearance in the lung by binding to its receptor.
UL16-binding proteins (ULBP) or retinoic acid early transcripts-1 (RAET1) are ligands to the activating receptor; NKG2D. Ten members of the human ULBP/RAET1 gene family have been identified to encode for potentially functional proteins; and have tissue-specific expressions. ULBP1; also known as RAET1I and NKG2DL1; together with at least ULBP 2 and 3; are well-known ligands for NKG2D; and activate multiple signaling pathways in primary NK cells; resulting in the production of cytokines and chemokines. ULBP1 is expressed in T-cells; B-cells; erythroleukemia cell lines and in a wide range of tissues including heart; brain; lung; liver and bone marrow; as well as some tumor cells. As an unconventional member of the MHC class I family; ULBP1 function in immune responses; especially in cancer and infectious diseases. Unlike other ULBP members; ULBP1 is able to interact with soluble CMV glycoprotein UL16 in CMV infected cells. The interaction with UL16 blocked the interaction with the NKG2D receptor; and thus might escape the immune surveillance. Furthermore; UL16 also causes ULBP1 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. The ULBP1 regulation may have implications for development of new therapeutic strategies against cancer cells.
NKG2D ligand 2; also known as N2DL-2; NKG2DL2; ALCAN-alpha; Retinoic acid early transcript 1H; UL16-binding protein 2; ULBP2 and N2DL2; is cell membrane protein which belongs to theMHC class I family. ULBP2 / N2DL-2 is expressed in various types of cancer cell lines and in the fetus; but not in normal tissues. ULBP2 / N2DL-2 is a ligand for the NKG2D receptor; together with at least ULBP1 and ULBP3. ULBPs activate multiple signaling pathways in primary NK cells; resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2; STAT5; ERK and PI3K kinase/Akt signal transduction pathway.
NKG2D Ligand 2 (N2DL2) is a member of a family of cell-surface proteins. N2DL2 function as ligands for human cytomegalovirus glycoprotein UL16. N2DL2 is anchored to the membrane via a GPI-linkage. N2DL2 is bind to human NKG2D; an activating receptor expressed on NK cells; NKT cells; T cells. Engagement of NKG2D results in the activation of cytolytic activity and cytokine production by these effects cells. The ULBPs are expressed on some tumor cells and have been implicated in tumor surveillance.
Urokinase plasminogen activator (uPA) and/or its receptor (uPAR) are essential for metastasis, and overexpression of these molecules is strongly correlated with poor prognosis in a variety of malignant tumours. uPAR and uPA levels in both resected tumor tissue and plasma are of independent prognostic significance for patient survival in several types of human cancer. This system has classically been thought to drive tumor progression by mediating directed extracellular proteolysis on the surface of migrating or invading cells, and intervening with this proteolysis by targeting uPAR has been proposed to represent a novel approach for inhibiting tumor progression. uPAR, also known as PLAUR or CD87, has been implicated in the growth, metastasis, and angiogenesis of several solid and hemotologic malignancies. uPAR is a highly glycosylated, 55-60kDa integral membrane protein linked to the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. It is part of a cell surface system that also consists of the serine protease uPA and several specific inhibitors (plasminogen activator inhibitors 1 and 2). Additionally, the analysis of CD87 (urokinase-type plasminogen activator receptor - uPAR) expression has a potential role in the diagnostic or prognostic work-up of several hematological malignancies, particularly acute leukemia and multiple myeloma.
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