Soluble urokinase plasminogen activator receptor (suPAR) as a prognostic marker of mortality in healthy, general and patient populations: protocol for a systematic review and meta-analysis
Introduction: Chronic inflammation is increasingly recognized as a major contributor to disease, disability and eventually death, but measure the degree of chronic inflammation remains non-saints, making it difficult to relate to chronic inflammation and death. Soluble urokinase plasminogen activator receptor (Supar), an emerging biomarker of chronic inflammation, has been proposed as a prognostic biomarker associated with the future occurrence of chronic diseases and mortality in general and patient populations.
precise prognostic biomarkers are important because they can help improve risk stratification in clinical settings and provide guidance in the treatment or lifestyle decisions as well as in the design of randomized trials. Here, we would like to summarize the evidence on the overall relationship of biomarker Supar death in the healthy population, the public and patients throughout the disease.
Methods and analysis: The search will be performed using Medline, Embase and Scopus databases from their inception to June 3, 2020 to identify studies investigating the ‘Supar’ and ‘death’. Observational studies and a control group of the study interventions were written in English or Danish will be included. Tools ‘Quality At Prognosis Studies’ will be used to assess the risk of bias of included studies. measures unadjusted and adjusted mortality outcomes (eg, risk ratio, OR, HR) with 95% CI are extracted to a healthy individual, general and patient populations. The primary outcome was all-cause mortality in any given follow-up. subgroup analysis will be based on the time of the results, the cause of death, type of population, adjusting for conventional risk factors and markers of inflammation.
Ethics and deployment: This systematic review will synthesize evidence on Supar use as a prognostic marker for mortality. The results will be disseminated by publications in peer-reviewed journals. Data used will be obtained from published studies, and therefore ethics approval is not required for this systematic review.
Soluble urokinase plasminogen activator receptor (suPAR) as a prognostic marker of mortality in healthy, general and patient populations: protocol for a systematic review and meta-analysis
Helicobacter pylori colonization Drives Urokinase Receptor (Upar) The expression in murine gastric epithelium During the Early Pathogenesis
Background: Persistent infection with Helicobacter pylori is the most important risk factor for gastric cancer. The urokinase receptor (Upar) upregulated in lesions and inflammation keep cancer invasion. evidence of H. pylori colonization tends to be correlated with increased expression of Upar in human gastric epithelium, but the link has not been established proximate cause in vivo; (2) Method: In a mouse model of H. pylori-induced gastritis, we investigate the emergence of Upar temporal protein expression in gastric mucosa in response to H. pylori (SS1 strain) infection; (3)
Results: We observed intense Upar foveolar immunoreactivity in the epithelial cells of the corpus of the stomach due to de novo synthesis, compared with non-infected animals. Upar induction is a response to the very beginning, but increased progressively over time as do the infiltration of immune cells. Eradication of H. pylori infections with antimicrobial therapy causes regression Upar expression to basic physiological level.
Description: PLAU, a member of the peptidase family S1, is a potent plasminogen activator and is clinically used for therapy of thrombolytic disorders. PLAU specifically cleaves the Arg-|-Val bond in plasminogen to form plasmin. The protein is found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A. Cleavage occurs after residue 155 in the low molecular mass form to yield a short A1 chain. The protein is used in Pulmonary Embolism (PE) to initiates fibrinolysis. Structurally, PLAU contains 1 EGF-like domain and 1 kringle domain.
Description: Recombinant Human Urokinase-Type Plasminogen Activator is a serine protease, which specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. Urokinase-Type Plasminogen Activator is a potent marker of invasion and metastasis in many human cancers associated with breast, colon, stomach, bladder, brain, ovary and endometrium. Human Urokinase-Type Plasminogen Activator is initially synthesized as 431 amino acid precursor with a N-terminal signal peptide residues. The single chain molecule is processed into a disulfide-linked two-chain molecule. There exists two forms A chain, the long A chain contains an EGF-like domain that is responsible for binding of the uPA receptor. The B chain corresponds to the catalytic domain.
Description: A polyclonal antibody for detection of uPA from Human. This uPA antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human uPA
Description: A polyclonal antibody for detection of uPA from Human. This uPA antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human uPA
Description: A polyclonal antibody for detection of uPA from Human. This uPA antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human uPA
Description: PLAU (plasminogen activator, urokinase) encodes a secreted serine protease that converts plasminogen to plasmin. The encoded preproprotein is proteolytically processed to generate A and B polypeptide chains. These chains associate via a single disulfide bond to form the catalytically inactive high molecular weight urokinase-type plasminogen activator (HMW-uPA). HMW-uPA can be further processed into the catalytically active low molecular weight urokinase-type plasminogen activator (LMW-uPA). This low molecular weight form does not bind to the urokinase-type plasminogen activator receptor. Mutations in PLAU may be associated with Quebec platelet disorder and late-onset Alzheimer's disease. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
Description: PLAU (plasminogen activator, urokinase) encodes a secreted serine protease that converts plasminogen to plasmin. The encoded preproprotein is proteolytically processed to generate A and B polypeptide chains. These chains associate via a single disulfide bond to form the catalytically inactive high molecular weight urokinase-type plasminogen activator (HMW-uPA). HMW-uPA can be further processed into the catalytically active low molecular weight urokinase-type plasminogen activator (LMW-uPA). This low molecular weight form does not bind to the urokinase-type plasminogen activator receptor. Mutations in PLAU may be associated with Quebec platelet disorder and late-onset Alzheimer's disease. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
Description: PLAU (plasminogen activator, urokinase) encodes a secreted serine protease that converts plasminogen to plasmin. The encoded preproprotein is proteolytically processed to generate A and B polypeptide chains. These chains associate via a single disulfide bond to form the catalytically inactive high molecular weight urokinase-type plasminogen activator (HMW-uPA). HMW-uPA can be further processed into the catalytically active low molecular weight urokinase-type plasminogen activator (LMW-uPA). This low molecular weight form does not bind to the urokinase-type plasminogen activator receptor. Mutations in PLAU may be associated with Quebec platelet disorder and late-onset Alzheimer's disease. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
Description: PLAUR (Plasminogen activator receptor, urokinase-type), also known as uPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol(GPI) anchor. It consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. The protein was originally identified as a saturable binding site for urokinase on the cell surface. The gene plays an important role in many normal as well as pathologic processes. It is localized to 19q13.31. uPAR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. It binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane, indicating it is an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a uPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (Plasminogen Activator Receptor, Urokinase-Type), also known as UPAR (uPA Receptor) or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (PLASMINOGEN ACTIVATOR RECEPTOR, UROKINASE-TYPE), also known as UPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (Plasminogen activator receptor, urokinase-type), also known as UPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (PLASMINOGEN ACTIVATOR RECEPTOR, UROKINASE-TYPE), also known as UPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: u-Plasminogen Activator (uPA) is a serine protease that converts plasminogen to plasmin, with roles in a variety of normal and pathological processes that include cell migration and tissue destruction. uPA is a potent marker of invasion and metastasis in a variety of human cancers including breast, stomach, colon, bladder, ovarian, brain, and endometrium.
Description: PLAU, a member of the peptidase family S1, is a potent plasminogen activator and is clinically used for therapy of thrombolytic disorders. PLAU specifically cleaves the Arg-|-Val bond in plasminogen to form plasmin. The protein is found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A. Cleavage occurs after residue 155 in the low molecular mass form to yield a short A1 chain. The protein is used in Pulmonary Embolism (PE) to initiates fibrinolysis. Structurally, PLAU contains 1 EGF-like domain and 1 kringle domain.
Description: PLAU, a member of the peptidase family S1, is a potent plasminogen activator and is clinically used for therapy of thrombolytic disorders. PLAU specifically cleaves the Arg-|-Val bond in plasminogen to form plasmin. The protein is found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A. Cleavage occurs after residue 155 in the low molecular mass form to yield a short A1 chain. The protein is used in Pulmonary Embolism (PE) to initiates fibrinolysis. Structurally, PLAU contains 1 EGF-like domain and 1 kringle domain.
Description: Urokinase, also known as urokinase-type plasminogen activator (uPA), is a serine protease present in humans and other animals. This gene encodes a secreted serine protease that converts plasminogen to plasmin. The encoded preproprotein is proteolytically processed to generate A and B polypeptide chains. These chains associate via a single disulfide bond to form the catalytically inactive high molecular weight urokinase-type plasminogen activator (HMW-uPA). HMW-uPA can be further processed into the catalytically active low molecular weight urokinase-type plasminogen activator (LMW-uPA). This low molecular weight form does not bind to the urokinase-type plasminogen activator receptor. Mutations in this gene may be associated with Quebec platelet disorder and late-onset Alzheimer's disease. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
Description: Urokinase - type plasminogen activator is also known as PLAU and UPA, a serine protease with an extremely limited substrate specificity, cleaving the sequence Cys – Pro – Gly - Arg560 - Val561 – Val – Gly – Gly – Cys in plasminogen to form plasmin. uPA is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium.uPA and its receptor (uPAR) have been implicated in a broad spectrum of pathophysiological processes, including fibrinolysis, proteolysis, inflammation, atherogenesis and plaque destabilization, all of which are involved in the pathogenesis of MI (myocardial infarction).
Description: Description of target: Plasminogen activator,urokinase (PLAU, uPA) converts plasminogen to plasmin. Plasmin is involved in processing of amyloid precursor protein and degrades secreted and aggregated amyloid-beta, a hallmark of Alzheimer disease (AD). Urokinase has a molecular mass of about 54 kD and is composed of 2 disulfide-linked chains, A and B, of molecular masses 18 kD and 33 kD, respectively. It localized on 10q24. uPA facilitates cell migration by localizing proteolisys on the cell surface and by inducing intracellular signalling pathways. In human vascular smooth muscle cell (VSMC), uPA stimulates migration via the uPA receptor (uPAR) signalling complex containing TYK2 and phosphatidylinositol 3-kinase (PI3-K).;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 5 pg/mL
Suppression of the inflammatory response by prostaglandin E2 expression Upar debilitating treatment. Despite this relationship, H. pylori does not induce the expression of Upar in vitro in cells co-cultured with gastric cancer; (4) Conclusion: We showed that persistent H. pylori colonization is an important event for the emergence of a relatively high Upar protein expression in murine gastric epithelial cells.
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