Written | 2009-09 | Benedikte Jacobsen, Martin Illemann, Michael Ploug |
Finsen Laboratory 3735, Rigshospitalet, Copenhagen Biocenter, 2200 Copenhagen N, Denmark |
Identity |
Alias (NCBI) | CD87 | MO3 | UPAR | URKR |
HGNC (Hugo) | PLAUR |
HGNC Alias symb | URKR | UPAR | CD87 |
HGNC Alias name | urokinase-type plasminogen activator (uPA) receptor | urokinase plasminogen activator surface receptor |
LocusID (NCBI) | 5329 |
Atlas_Id | 41741 |
Location | 19q13.31 [Link to chromosome band 19q13] |
Location_base_pair | Starts at 43648579 and ends at 43670169 bp from pter ( according to GRCh38/hg38-Dec_2013) [Mapping PLAUR.png] |
Fusion genes (updated 2017) | Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands) |
PLAUR (19q13.31) / EXOC3L2 (19q13.32) | PLAUR (19q13.31) / MARK4 (19q13.32) | PLAUR (19q13.31) / ZNF576 (19q13.31) | |
DNA/RNA |
Note | The gene for human urokinase-type plasminogen activator receptor (uPAR) is located on chromosome 19q13 within a 2 Mb cluster harbouring all presently known glycosylphosphatidylinositol (GPI)-anchored, multi-domain proteins of the Ly6/uPAR/alpha-neurotoxin (LU) domain family (Kjaergaard et al., 2008). |
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Figure 1: Location of the uPAR gene in the uPAR-like gene cluster on chromosome 19q13. Each of the three LU domains of uPAR is encoded by separate exon sets, flanked by phase-1 introns (Casey et al., 1994). The introns dividing these 3 exon sets are also phase-1 and are located at a position corresponding to the surface-exposed tip of loop 2 in the three-finger fold of the LU domains (Ploug, 2003). The other known multi LU-domain members of this protein family, which are all present within this gene cluster, are: PRV1/CD177, TEX101, C4.4A, PRO4356 and GPQH2552. | |
Description | 24254 bp; 7 exons (Figure 1). |
Transcription | Transcription of the uPAR gene is regulated by a TATA-less proximal promoter, partly through binding to SP1 (Soravia et al., 1995). |
Protein |
Note | uPAR was originally identified on the monocyte-like human cell line U937 as the membrane receptor for the serine protease urokinase-type plasminogen activator (uPA) (Vassalli et al., 1985). It has since been implicated in a large number of physiological and pathological conditions, including cancer invasion and metastasis. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Figure 2: Structure of the uPAR protein. Panel A - Schematic representation of the amino acid sequence of human uPAR showing its three homologous LU domains. Consensus disulfide bonds defining the LU domains are coloured black. The position of the C-terminal glycolipid anchor (GPI) is shown (modified from Ploug and Ellis, 1994, with permission). Insert: The archetypical three-finger fold is illustrated by a ribbon diagram for a single secreted LU-domain protein (snake venom toxin-a) using the PDB coordinates 1NEA and PyMOLTM (DeLano Scientific). Panel B - LU domain signatures in the primary sequence of human uPAR. The three LU domains (DI, DII and DIII) of uPAR are aligned with the consensus structures being highlighted (disulfide bonds in yellow and the invariant asparagines in red). The number of residues between the individual cysteines is represented by dots or numbers in brackets (modified from Kjaergaard et al., 2008). Panel C - The crystal structure solved for uPAR in complex with a peptide antagonist is shown as a ribbon diagram (Llinas et al., 2005). The individual LU domains are colour-coded (DI in yellow, DII in blue and DIII in red), and N-linked carbohydrates are shown as white sticks. The attachment to the cell surface by a glycolipid anchor is modelled in this cartoon. The insert shows uPAR in a surface representation, with the hydrophobic ligand-binding cavity marked with hatched lines; carbon, nitrogen and oxygen atoms are coloured white, blue and red, respectively. These structures are visualized by PyMOLTM (DeLano Scientific), using the PDB coordinates 1YWH (reproduced from Kjaergaard et al., 2008). | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Description | uPAR is a multi-domain member of the Ly6/uPAR/alpha-neurotoxin (LU) protein family (Ploug, 2003), containing three of these LU domains (DI, DII and DIII; Figure 2), each of ~ 90 amino acids, adopting a "three-fingered" folding topology, and encompassing 4 consensus disulfide bonds and an invariant C-terminal asparagine (Figure 2B). Intriguingly, one of the consensus disulfide bonds, which is crucial to the proper folding of the single domain LU proteins, is missing in the N-terminal LU domain of uPAR. As evident from the crystal structures solved for human uPAR, the three LU domains cooperate in creating a deep and hydrophobic ligand-binding cavity (Figure 2C), in which the growth factor-like domain (GFD) of the cognate protease ligand uPA (Huai et al., 2006; Barinka et al., 2006) or synthetic peptide antagonists (Llinas et al., 2005) are buried during formation of the corresponding high-affinity receptor complexes. The 335 amino acid residue long single polypeptide chain of human uPAR is processed to a mature protein of only 283 residues after post-translational excision of signal peptides at the N- and C-termini, the latter event being responsible for tethering uPAR to the cell membrane via a GPI moiety (Figure 2A+C; Ploug et al 1991). Human uPAR contains 5 potential N-glycosylation sites, of which only four are utilized (Ploug et al., 1998; Gårdsvoll et al., 2004). | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Expression | Under normal homeostatic conditions, uPAR is expressed by the following bone marrow-derived blood cells: monocytes, neutrophils, eosinophils and macrophages. In the bone marrow itself, uPAR has been demonstrated in myelocytes, mature myeloid elements and monocytes. Expression of the receptor is significantly upregulated upon cytokine stimulation of various monocyte-derived cell lines in vitro (Plesner et al., 1994a). Consistent with these observations, uPAR is classified as a differentiation antigen and is also denoted CD87. The amount of uPAR in homeostatic organs is in general low, and when present, usually associated to quiescent endothelial cells, as demonstrated in e.g. the lung, kidney, thymus, liver and heart of normal mice (Solberg et al., 2001). Expression of uPAR in kidney and thymus has also been recapitulated in human samples (Wei et al., 2008; Plesner et al., 1994a). Whereas uPAR is scarce under normal conditions, pronounced receptor expression has been observed in various non-homeostatic tissue remodeling processes. First, during wound healing, strong uPAR immunoreactivity is found in migrating keratinocytes at the leading re-epithelialization edge of the wound, while non-migrating keratinocytes are negative (Rømer et al., 1994). In addition, uPAR is located in infiltrating granulocytes located underneath the wound crush, and in endothelial cells in the wound area (Solberg et al., 2001). In squamous cell carcinoma of the skin, uPAR mRNA and protein is seen in well-differentiated cancer cells at the invasive front of the tumour lesion (Rømer et al., 2001; Ferrier et al., 2002). In view of the localization of uPAR in the leading-edge keratinocytes in regenerating epidermis during mouse skin wound healing, it has been proposed that similarities exist between the mechanisms of generation and regulation of extracellular proteolysis during skin re-epithelialization and squamous cell carcinoma invasion (Rømer et al., 2001). As a second example of tissue remodeling, late pregnancy in mouse shows uPAR expression in spongiotrophoblasts and endothelial cells in the placenta (Solberg et al., 2001). In the human counterpart, uPAR was encountered in endothelial cells and macrophages in association with fibrinoid deposits, suggesting a participation of uPAR in placental development and fibrin surveillance (Pierleoni et al., 1998 and 2003). Third, uPAR is present in the regression of mammary glands in post-lactational involution in mice (Solberg et al., 2001). These three processes mimic some of the characteristics of cancer invasion and can accordingly be used as model systems for the elucidation of the role of uPAR in malignant transformation. Indeed, the receptor is upregulated in several cancer types, expression often being confined to stromal cells associated with the tumour, as detailed later for gastro-intestinal, breast and squamous cell cancers (Figure 3). Other examples conforming to this pattern include hepatocellular carcinoma, where uPAR has been found in macrophages and fibroblasts, as well as in a subpopulation of rare CK7-positive tumoural hepatocytes (Akahane et al., 1998; Dubuisson et al., 2000). In invasive lesions of human prostate adenocarcinoma, uPAR mRNA and protein is also expressed by macrophages, located throughout the interstitial tissue of tumours (Figure 3D), whereas in benign lesions, it is confined to intraluminal macrophages (Usher et al., 2005). A summary of uPAR expression patterns in various cancer forms can be found in Table 1. Table 1
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Figure 3: Expression of uPAR in cancer tissue. Peroxidase stainings with the same batch of a polyclonal antibody against uPAR produced at the Finsen Laboratory (Copenhagen, Denmark), showing reactivity in stromal cells associated with the tumour. Panel A - Primary colorectal adenocarcinoma (1) and a corresponding liver metastasis (2) (reproduced from Illemann et al., 2009). Panel B - Ductal carcinoma in situ lesion of the breast with microinvasion (1) and normal breast (2) (reproduced from Nielsen et al., 2007). Panel C - Gastric cancer, intestinal subtype (courtesy of W. Alpízar-Alpízar, Finsen Laboratory, Copenhagen, Denmark). Panel D - Prostate carcinoma (reproduced from Usher et al., 2005, Copyright (2004, Wiley-Liss, Inc.), with permission of John Wiley & Sons, Inc.). | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Localisation | The cell membrane attachment of uPAR via GPI implicates a differential partitioning of the receptor into detergent-resistant microdomain lipid rafts that are enriched in cholesterol and sphingolipids. In complex with uPA and the plasminogen activator inhibitor type 1, uPAR can also be internalized (Cubellis et al., 1990), and later recycled back to the membrane (Nykjær et al., 1997). Interestingly, upon stimulation of resting neutrophils, uPAR is rapidly translocated from secretory vesicles to the cell surface (Plesner et al., 1994b). Proteolytic cleavage of the receptor either in the linker region between DI and DII, e.g. by its own ligand uPA (Høyer-Hansen et al., 1992), or between domain III and the GPI-anchor, yield various soluble uPAR fragments that are detectable in body fluids such as plasma and urine, the levels of which have been shown to correlate to overall survival in several human cancers (Høyer-Hansen and Lund, 2007). | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Function | Through its high-affinity interaction with the serine protease urokinase-type plasminogen activator (uPA), uPAR plays a central role in cell surface-associated plasminogen activation, entailing proteolytic degradation of the extracellular matrix surrounding the cells (Ellis et al., 1989; Stephens et al., 1989). This cascade, mediated by the broad-spectrum serine protease plasmin, is involved in several tissue remodeling processes such as wound healing and mammary gland involution (Ploug, 2003; Danø et al., 2005). The proteolytic role of uPAR in tumour invasion and metastasis is reflected by the frequently encountered expression of uPAR at the invasive front of cancer tissue, and by the impact of uPAR status in malignant cells disseminated to the bone marrow on the prognosis of gastric cancer patients (Heiss et al., 2002). Other ligands with which uPAR allegedly also interacts include the matrix component vitronectin (Waltz and Chapman, 1994; Wei et al., 1994; Gårdsvoll and Ploug, 2007; Huai et al., 2008), various integrins (Wei et al., 1996; Aguirre Ghiso et al., 1999) and the G-protein coupled receptor FPRL1 (Resnati et al., 1996), affecting cell adhesion and migration, as well as signal transduction (Figure 4; for reviews, see Ossowski and Aguirre-Ghiso, 2000; Blasi and Carmeliet, 2002; Kjøller, 2002; Kugler et al., 2003; Ragno, 2006; Tang and Wei, 2008). | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Figure 4: uPAR ligands. Schematic representation of the functions of uPAR via its interaction with uPA, integrins, and vitronectin (modified from Kjaergaard et al., 2008). | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Homology | uPAR is homologous to the other multi-domain proteins of the Ly6/uPAR/alpha-neurotoxin protein domain family (C4.4A, PRV-1/CD177, TEX101, PRO4356, GPQH2552), of which C4.4A is the best-studied until now (Jacobsen and Ploug, 2008), and to a vast number of single LU-domain proteins such as the Ly-6 antigens, CD59, SLURP 1 and SLURP 2, the extracellular ligand-binding domains of the TGF-receptor family and the snake venom alpha-neurotoxins (Ploug and Ellis, 1994; Ploug, 2003). |
Mutations |
Note | An mRNA splice variant of uPAR, lacking exons 4 and 5, which encode domain II of the receptor, has recently been shown to have prognostic relevance in breast cancer (Kotzsch et al., 2008). Restriction fragment length polymorphisms of the uPAR gene have been identified by EcoRI and PstI (Børglum et al., 1991 and 1992), and a highly polymorphic CA/GT repeat is present in intron 3 (Kohonen-Corish et al., 1996). In a comparison of the latter in colon cancer patients and controls, however, there were no significant differences in the frequencies of alleles (Przybylowska et al., 2008; Kohonen-Corish et al., 1998). Genetic linkage and association analyses on 587 families with high incidences of asthma have revealed a correlation between asthma/lung function decline and certain SNP in the uPAR gene (Barton et al., 2009). |
Implicated in |
Note | |
Entity | Colon cancer |
Note | The first study on uPAR expression was performed by in situ hybridization on samples of human colon cancer (Pyke et al., 1991), which revealed the presence of uPAR mRNA both in stromal cells and some cancer cells located at the invasive foci. Using immunohistochemistry and antibodies raised against recombinant human uPAR protein, this finding was substantiated, and demonstrated that uPAR is expressed primarily by macrophages, some a-smooth-muscle-actin (a-SMA)-positive myofibroblasts, a few endothelial cells located at the front of the cancer, as well as by some so-called budding cancer cells (Figure 3A1; Pyke et al., 1994; Ohtani et al., 1995; Illemann et al., 2009). Interestingly, these uPAR-positive budding cancer cells also produce the 2-chain of laminin 5 (LN5.2), which has been shown to correlate with poor prognosis in colon cancer, in addition to being a marker of early invasion of cervix cancers (Pyke et al., 1995; Lenander et al., 2001; Skyldberg et al., 1999). Furthermore, by combining immunohistochemistry and in situ hybridization, it became clear that these uPAR- and LN5.2-positive budding cancer cells produce uPA mRNA, thus linking uPA and its receptor to cancer cells with high invasive potential (Illemann et al., 2009). uPAR is also found in neutrophils scattered throughout colon cancer tissue and in nerve bundles located in muscularis propia (Pyke et al., 1994; Illemann et al., 2009). In fact, immunohistochemical staining in neutrophils represents a valuable internal positive control, as uPAR is synthesized in these cells during differentiation in the bone marrow and is present in all circulating neutrophils (Plesner et al., 1994a). In colon cancer liver metastasis with encapsulation of the secondary tumour, uPAR expression is in general very similar to that found in the primary tumour (Figure 3A2; Illemann et al., 2009). |
Prognosis | The high expression of uPAR encountered in malignant tissue can be furthered into its potential as a prognostic marker in several cancer forms, including colon cancer. Preoperative levels of soluble uPAR is an independent predictor of survival in patients with colorectal cancer, as observed in a study encompassing 591 patients (Stephens et al., 1999), with highest clinical utility in early stage disease (Dukes' stage B). |
Entity | Gastro-intestinal cancer |
Note | In adenocarcinomas of the lower esophagus/gastroesophageal junction, the pattern of uPAR is reminiscent of that described in colon cancer (Laerum et al., 2009), which is also the case for adenocarcinomas of the lower stomach (Figure 3C; Heiss et al., 1995; Migita et al., 1999; Alpízar-Alpízar et al., 2009), i.e. expression by invasive cancer cells, macrophages, a-SMA-positive myofibroblasts, and some endothelial cells, as well as scattered neutrophils and nerves bundles in the muscularis propia. Interestingly, in these two cancer types, a much higher number of invasive cancer cells are found to contain uPAR as compared to colon cancer, which, in view of the poorer prognosis of these patients, points to an association of uPAR cancer cell expression with a higher invasive potential (Alpízar-Alpízar et al., 2009). In the lower esophagus and gastroesophageal junction, uPAR expression is confined to invasive foci (Laerum et al., 2009), whereas in the lower stomach, uPAR is also present in benign lesions (Alpízar-Alpízar et al., 2009). Cancer in the latter region is believed to be caused by infection of Helicobacter pylori (Suzuki et al., 2007). As non-neoplastic mucosa infected with H. pylori has been shown to be positive for uPAR, in both the epithelial cells and macrophages, the receptor appears to be present in the tissue already at the onset of tumourigenesis (Alpízar-Alpízar et al., 2009; Kenny et al., 2008). |
Prognosis | Importantly, in metastatic disease, uPAR positivity in tumour cells that have disseminated to the bone marrow is a strong negative prognostic indicator for disease-free and overall survival in curatively resected gastric cancer patients (Heiss et al., 2002). |
Entity | Breast cancer |
Note | In human ductal breast carcinomas, uPAR is primarily expressed by tumour-associated macrophages and a-SMA-positive myofibroblasts (Pyke et al., 1993; Nielsen et al., 2007), whereas normal breast tissue is devoid of reactivity (Figure 3B2). In some biopsies, uPAR has in addition been found in invasive tumour cells and a few endothelial cells. As for other solid cancer forms, neutrophils also display uPAR immunoreactivity in the breast. In early invasive ductal carcinoma in situ (DCIS) lesions without microinvasion, the receptor is confined to ductal macrophages and few neoplastic cells within the epithelial lesion. The advent of microinvasion is accompanied by a strong uPAR signal in several layers of tumour-associated macrophages and a-SMA-positive myofibroblasts surrounding the DCIS lesions (Figure 3B1). These results indicate that restricted expression of uPAR in myofibroblasts and macrophages is an early event in breast carcinogenesis, which is strongly amplified after transition to invasive ductal carcinoma. Furthermore, uPAR and uPA co-localize in both macrophages and myofibroblasts located at the front of collapsed ducts in DCIS lesions with microinvasion (Nielsen et al., 2007). |
Prognosis | uPAR has shown potential as a prognostic marker in breast cancer, with high levels of uPAR in cytosolic extracts from primary breast tumours significantly correlating with a shorter overall survival (Grøndahl-Hansen et al., 1995). Similarly, there was a significant association between age-adjusted levels of the receptor in preoperative serum from breast cancer patients and their relapse-free and overall survival, independent of lymph node status, tumour size, and estrogen receptor status (Riisbro et al., 2002). |
Entity | Oral cancer |
Note | In squamous cell carcinoma (SCC) of the oral cavity, uPAR is strongly upregulated in areas with incipient and invasive SCC compared to areas with dysplastic and normal epithelium. The receptor is predominantly observed in stromal cells, primarily macrophages, but also in fibroblasts as well as neutrophils. uPAR-positive neoplastic cells found in areas with incipient and invasive SCC are also reported to express LN5.2 (Lindberg et al., 2006), which as mentioned above is a marker for invasiveness. |
Entity | Glioblastoma |
Note | Presence of uPAR at the invasive edge of the cancer, as seen in colon, breast and skin cancer, is recapitulated in human glioblastomas, but with the notable difference that the mRNA for uPAR in this particular case is predominantly expressed by tumour cells, as well as in some endothelial cells, indicating that uPAR is related to tumour cell invasiveness and endothelial cell migration (Yamamoto et al., 1994). |
Entity | Lung cancer |
Prognosis | The prognostic significance of uPAR in non-small cell lung cancer is apparent for patients with the histologic subtype of squamous cell carcinoma, where high levels of uPAR is an independent marker of prognosis, as evaluated in tumour extracts (Pedersen et al., 1994). Measuring the levels of uPAR domain I alone in these same extracts similarly predicted overall survival (Almasi et al., 2005). |
Entity | Ovarian cancer |
Prognosis | Like in non-small cell lung cancer, uPAR domain I present in high concentrations in preoperative plasma independently predicts poor survival of patients with ovarian cancer. Furthermore, soluble full-length uPAR + the soluble fragment of uPAR domains II+III can, together with CA125 in plasma collected preoperatively, serve as a diagnostic tool, discriminating between malignant and benign ovarian tumours (Henic et al., 2008). |
Entity | Prostate cancer |
Prognosis | As described for breast, colon and lung cancer, uPAR also correlates with shorter survival of patients with prostate cancer, where serum levels of the receptor are elevated as compared to healthy controls (Miyake et al., 1999). |
Entity | Haematological malignancies |
Note | In line with its expression in normal hematopoietic cells, uPAR is also observed in various hematopoietic disorders, most importantly acute leukemia and multiple myeloma, and its level could have diagnostic and prognostic implications for these diseases (Béné et al., 2004). |
Entity | Paroxysmal nocturnal haemoglobinuria |
Note | As a consequence of being a GPI-anchored protein, membranous uPAR is absent from blood cells derived from clonally expanded bone marrow cells affected by point mutations causing the haematological disease paroxysmal nocturnal haemoglobinuria, PNH (Ploug et al., 1992). |
Entity | Inflammatory conditions |
Note | In inflammatory conditions such as Crohn's disease and chronic ulcerative colitis, uPAR immunoreactivity is seen in numerous macrophages, including granulomas and granulocytes located throughout the whole intestinal wall, as well as in nerve bundles (Laerum et al., 2008), providing a possible link between uPAR and inflammation. |
To be noted |
As a result of the well-established correlation of uPAR to tumour invasion and metastasis, several targeting strategies with therapeutic potential have been devised to interfere with the receptor (Mazar, 2008): New strategies are constantly unfolding regarding the intervention of the uPA-uPAR interaction, as illustrated by the recent reports of synthetic self-assembly nanoparticles taken up by uPAR-expressing cells via receptor-mediated endocytosis (Wang et al., 2009), molecular imaging of pancreatic cancer using dual-modality nanoparticles (Yang et al., 2009), and an oncolytic measles virus retargeted against the receptor with potent anti-tumour effect in a breast cancer xenograft model (Jing et al., 2009). | |
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Bibliography |
Tumor dormancy induced by downregulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling. |
Aguirre Ghiso JA, Kovalski K, Ossowski L. |
J Cell Biol. 1999 Oct 4;147(1):89-104. |
PMID 10508858 |
Stromal expression of urokinase-type plasminogen activator receptor (uPAR) is associated with invasive growth in primary liver cancer. |
Akahane T, Ishii M, Ohtani H, Nagura H, Toyota T. |
Liver. 1998 Dec;18(6):414-9. |
PMID 9869396 |
Prognostic impact of liberated domain I of the urokinase plasminogen activator receptor in squamous cell lung cancer tissue. |
Almasi CE, Hoyer-Hansen G, Christensen IJ, Dano K, Pappot H. |
Lung Cancer. 2005 Jun;48(3):349-55. |
PMID 15893003 |
Urokinase plasminogen activator receptor is expressed in invasive cells in gastric carcinomas from high- and low-risk countries. |
Alpizar-Alpizar W, Nielsen BS, Sierra R, Illemann M, Ramirez JA, Arias A, Duran S, Skarstein A, Ovrebo K, Lund LR, Laerum OD. |
Int J Cancer. 2009 Jul 16. [Epub ahead of print] |
PMID 19609941 |
Structural basis of interaction between urokinase-type plasminogen activator and its receptor. |
Barinka C, Parry G, Callahan J, Shaw DE, Kuo A, Bdeir K, Cines DB, Mazar A, Lubkowski J. |
J Mol Biol. 2006 Oct 20;363(2):482-95. Epub 2006 Aug 26. |
PMID 16979660 |
PLAUR polymorphisms are associated with asthma, PLAUR levels, and lung function decline. |
Barton SJ, Koppelman GH, Vonk JM, Browning CA, Nolte IM, Stewart CE, Bainbridge S, Mutch S, Rose-Zerilli MJ, Postma DS, Maniatis N, Henry AP, Hall IP, Holgate ST, Tighe P, Holloway JW, Sayers I. |
J Allergy Clin Immunol. 2009 Jun;123(6):1391-400.e17. Epub 2009 May 13. |
PMID 19443020 |
Targeting of urokinase plasminogen activator receptor in human pancreatic carcinoma cells inhibits c-Met- and insulin-like growth factor-I receptor-mediated migration and invasion and orthotopic tumor growth in mice. |
Bauer TW, Liu W, Fan F, Camp ER, Yang A, Somcio RJ, Bucana CD, Callahan J, Parry GC, Evans DB, Boyd DD, Mazar AP, Ellis LM. |
Cancer Res. 2005 Sep 1;65(17):7775-81. |
PMID 16140945 |
CD87 (urokinase-type plasminogen activator receptor), function and pathology in hematological disorders: a review. |
Bene MC, Castoldi G, Knapp W, Rigolin GM, Escribano L, Lemez P, Ludwig WD, Matutes E, Orfao A, Lanza F, van't Veer M; EGIL, European Group on Immunological Classification of Leukemias. |
Leukemia. 2004 Mar;18(3):394-400. (REVIEW) |
PMID 14671631 |
uPAR: a versatile signalling orchestrator. |
Blasi F, Carmeliet P. |
Nat Rev Mol Cell Biol. 2002 Dec;3(12):932-43. (REVIEW) |
PMID 12461559 |
Two PstI polymorphisms for the urokinase-type plasminogen activator receptor gene (PLAUR). |
Borglum AD, Byskov A, Roldan AL, Kruse TA. |
Hum Genet. 1992 Jul;89(5):584. |
PMID 1353059 |
The structure of the urokinase-type plasminogen activator receptor gene. |
Casey JR, Petranka JG, Kottra J, Fleenor DE, Rosse WF. |
Blood. 1994 Aug 15;84(4):1151-6. |
PMID 8049431 |
Receptor-mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI-1. |
Cubellis MV, Wun TC, Blasi F. |
EMBO J. 1990 Apr;9(4):1079-85. |
PMID 2157592 |
Plasminogen activation and cancer. |
Dano K, Behrendt N, Hoyer-Hansen G, Johnsen M, Lund LR, Ploug M, Romer J. |
Thromb Haemost. 2005 Apr;93(4):676-81. (REVIEW) |
PMID 15841311 |
Expression and cellular localization of the urokinase-type plasminogen activator and its receptor in human hepatocellular carcinoma. |
Dubuisson L, Monvoisin A, Nielsen BS, Le Bail B, Bioulac-Sage P, Rosenbaum J. |
J Pathol. 2000 Feb;190(2):190-5. |
PMID 10657018 |
Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes. |
Ellis V, Scully MF, Kakkar VV. |
J Biol Chem. 1989 Feb 5;264(4):2185-8. |
PMID 2521625 |
Spitz naevi may express components of the plasminogen activation system. |
Ferrier CM, Van Geloof WL, Straatman H, Van De Molengraft FJ, Van Muijen GN, Ruiter DJ. |
J Pathol. 2002 Sep;198(1):92-9. |
PMID 12210068 |
Mapping of the vitronectin-binding site on the urokinase receptor: involvement of a coherent receptor interface consisting of residues from both domain I and the flanking interdomain linker region. |
Gardsvoll H, Ploug M. |
J Biol Chem. 2007 May 4;282(18):13561-72. Epub 2007 Mar 13. |
PMID 17355965 |
Prognostic significance of the receptor for urokinase plasminogen activator in breast cancer. |
Grondahl-Hansen J, Peters HA, van Putten WL, Look MP, Pappot H, Ronne E, Dano K, Klijn JG, Brunner N, Foekens JA. |
Clin Cancer Res. 1995 Oct;1(10):1079-87. |
PMID 9815897 |
Tumor-associated proteolysis and prognosis: new functional risk factors in gastric cancer defined by the urokinase-type plasminogen activator system. |
Heiss MM, Babic R, Allgayer H, Gruetzner KU, Jauch KW, Loehrs U, Schildberg FW. |
J Clin Oncol. 1995 Aug;13(8):2084-93. |
PMID 7636552 |
Minimal residual disease in gastric cancer: evidence of an independent prognostic relevance of urokinase receptor expression by disseminated tumor cells in the bone marrow. |
Heiss MM, Simon EH, Beyer BC, Gruetzner KU, Tarabichi A, Babic R, Schildberg FW, Allgayer H. |
J Clin Oncol. 2002 Apr 15;20(8):2005-16. |
PMID 11956259 |
Cleaved forms of the urokinase plasminogen activator receptor in plasma have diagnostic potential and predict postoperative survival in patients with ovarian cancer. |
Henic E, Borgfeldt C, Christensen IJ, Casslen B, Hoyer-Hansen G. |
Clin Cancer Res. 2008 Sep 15;14(18):5785-93. |
PMID 18794088 |
Urokinase receptor variants in tissue and body fluids. |
Hoyer-Hansen G, Lund IK. |
Adv Clin Chem. 2007;44:65-102. (REVIEW) |
PMID 17682340 |
Structure of human urokinase plasminogen activator in complex with its receptor. |
Huai Q, Mazar AP, Kuo A, Parry GC, Shaw DE, Callahan J, Li Y, Yuan C, Bian C, Chen L, Furie B, Furie BC, Cines DB, Huang M. |
Science. 2006 Feb 3;311(5761):656-9. |
PMID 16456079 |
Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes. |
Huai Q, Zhou A, Lin L, Mazar AP, Parry GC, Callahan J, Shaw DE, Furie B, Furie BC, Huang M. |
Nat Struct Mol Biol. 2008 Apr;15(4):422-3. Epub 2008 Mar 23. |
PMID 18376415 |
Two distinct expression patterns of urokinase, urokinase receptor and plasminogen activator inhibitor-1 in colon cancer liver metastases. |
Illemann M, Bird N, Majeed A, Laerum OD, Lund LR, Dano K, Nielsen BS. |
Int J Cancer. 2009 Apr 15;124(8):1860-70. |
PMID 19123477 |
The urokinase receptor and its structural homologue C4.4A in human cancer: expression, prognosis and pharmacological inhibition. |
Jacobsen B, Ploug M. |
Current Medicinal Chemistry. 2008; 15 (25): 2559-73. (REVIEW) |
PMID 18855679 |
Tumor and vascular targeting of a novel oncolytic measles virus retargeted against the urokinase receptor. |
Jing Y, Tong C, Zhang J, Nakamura T, Iankov I, Russell SJ, Merchan JR. |
Cancer Res. 2009 Feb 15;69(4):1459-68. Epub 2009 Feb 10. |
PMID 19208845 |
Systemic administration of anti-urokinase plasminogen activator receptor monoclonal antibodies induces hepatic fibrin deposition in tissue-type plasminogen activator deficient mice. |
Jogi A, Pass J, Hoyer-Hansen G, Lund LR, Nielsen BS, Dano K, Romer J. |
J Thromb Haemost. 2007 Sep;5(9):1936-44. |
PMID 17723133 |
Increased expression of the urokinase plasminogen activator system by Helicobacter pylori in gastric epithelial cells. |
Kenny S, Duval C, Sammut SJ, Steele I, Pritchard DM, Atherton JC, Argent RH, Dimaline R, Dockray GJ, Varro A. |
Am J Physiol Gastrointest Liver Physiol. 2008 Sep;295(3):G431-41. Epub 2008 Jul 3. |
PMID 18599586 |
Structure and ligand interactions of the urokinase receptor (uPAR). |
Kjaergaard M, Hansen LV, Jacobsen B, Gardsvoll H, Ploug M. |
Front Biosci. 2008 May 1;13:5441-61. (REVIEW) |
PMID 18508598 |
The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility. |
Kjoller L. |
Biol Chem. 2002 Jan;383(1):5-19. (REVIEW) |
PMID 11928822 |
Development and evaluation of peptidic ligands targeting tumour-associated urokinase plasminogen activator receptor (uPAR) for use in alpha-emitter therapy for disseminated ovarian cancer. |
Knor S, Sato S, Huber T, Morgenstern A, Bruchertseifer F, Schmitt M, Kessler H, Senekowitsch-Schmidtke R, Magdolen V, Seidl C. |
Eur J Nucl Med Mol Imaging. 2008 Jan;35(1):53-64. Epub 2007 Sep 22. |
PMID 17891393 |
Urokinase receptor genotypes in colorectal cancer. |
Kohonen-Corish M, Young J, Chenevix-Trench G, Doe WF. |
Carcinogenesis. 1998 Jun;19(6):1149-51. |
PMID 9667756 |
Urokinase receptor splice variant uPAR-del4/5-associated gene expression in breast cancer: identification of rab31 as an independent prognostic factor. |
Kotzsch M, Sieuwerts AM, Grosser M, Meye A, Fuessel S, Meijer-van Gelder ME, Smid M, Schmitt M, Baretton G, Luther T, Magdolen V, Foekens JA. |
Breast Cancer Res Treat. 2008 Sep;111(2):229-40. Epub 2007 Oct 20. |
PMID 17952591 |
Urokinase receptor and integrin interactions. |
Kugler MC, Wei Y, Chapman HA. |
Curr Pharm Des. 2003;9(19):1565-74. (REVIEW) |
PMID 12871068 |
Crohn's disease but not chronic ulcerative colitis induces the expression of PAI-1 in enteric neurons. |
Laerum OD, Illemann M, Skarstein A, Helgeland L, Ovrebo K, Dano K, Nielsen BS. |
Am J Gastroenterol. 2008 Sep;103(9):2350-8. |
PMID 18844621 |
Prognosis in adenocarcinomas of lower esophagus and gastroesophageal junction can be directly evaluated by immunohistochemistry of uPAR. |
Laerum OD, Ovrebo K, Skarstein A, Christensen IJ, Alpizar-Alpizar W, Helgeland L, Dano K, Nielsen BS, Illemann M. |
Manuscript in preparation, 2009. |
Laminin-5 gamma 2 chain expression correlates with unfavorable prognosis in colon carcinomas. |
Lenander C, Habermann JK, Ost A, Nilsson B, Schimmelpenning H, Tryggvason K, Auer G. |
Anal Cell Pathol. 2001;22(4):201-9. |
PMID 11564896 |
Imaging of urokinase-type plasminogen activator receptor expression using a 64Cu-labeled linear peptide antagonist by microPET. |
Li ZB, Niu G, Wang H, He L, Yang L, Ploug M, Chen X. |
Clin Cancer Res. 2008 Aug 1;14(15):4758-66. |
PMID 18676745 |
Expression of plasminogen activator inhibitor-1, urokinase receptor and laminin gamma-2 chain is an early coordinated event in incipient oral squamous cell carcinoma. |
Lindberg P, Larsson A, Nielsen BS. |
Int J Cancer. 2006 Jun 15;118(12):2948-56. |
PMID 16395714 |
Synthesis and Characterization of an (111)In-Labeled Peptide for the in Vivo Localization of Human Cancers Expressing the Urokinase-Type Plasminogen Activator Receptor (uPAR). |
Liu D, Overbey D, Watkinson L, Giblin MF. |
Bioconjug Chem. 2009 Apr 8. [Epub ahead of print] |
PMID 19354275 |
Targeting of tumor cells by cell surface urokinase plasminogen activator-dependent anthrax toxin. |
Liu S, Bugge TH, Leppla SH. |
J Biol Chem. 2001 May 25;276(21):17976-84. Epub 2001 Mar 12. |
PMID 11278833 |
Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide. |
Llinas P, Le Du MH, Gardsvoll H, Dano K, Ploug M, Gilquin B, Stura EA, Menez A. |
EMBO J. 2005 May 4;24(9):1655-63. Epub 2005 Apr 7. |
PMID 15861141 |
Urokinase plasminogen activator receptor choreographs multiple ligand interactions: implications for tumor progression and therapy. |
Mazar AP. |
Clin Cancer Res. 2008 Sep 15;14(18):5649-55. (REVIEW) |
PMID 18794071 |
Differing expression of MMPs-1 and -9 and urokinase receptor between diffuse- and intestinal-type gastric carcinoma. |
Migita T, Sato E, Saito K, Mizoi T, Shiiba K, Matsuno S, Nagura H, Ohtani H. |
Int J Cancer. 1999 Feb 19;84(1):74-9. |
PMID 9988236 |
Elevation of serum levels of urokinase-type plasminogen activator and its receptor is associated with disease progression and prognosis in patients with prostate cancer. |
Miyake H, Hara I, Yamanaka K, Gohji K, Arakawa S, Kamidono S. |
Prostate. 1999 May;39(2):123-9. |
PMID 10221568 |
Cancer cells overexpress mRNA of urokinase-type plasminogen activator, its receptor and inhibitors in human non-small-cell lung cancer tissue: analysis by Northern blotting and in situ hybridization. |
Morita S, Sato A, Hayakawa H, Ihara H, Urano T, Takada Y, Takada A. |
Int J Cancer. 1998 Oct 29;78(3):286-92. |
PMID 9766559 |
Stromal cells associated with early invasive foci in human mammary ductal carcinoma in situ coexpress urokinase and urokinase receptor. |
Nielsen BS, Rank F, Illemann M, Lund LR, Dano K. |
Int J Cancer. 2007 May 15;120(10):2086-95. |
PMID 17290405 |
Recycling of the urokinase receptor upon internalization of the uPA:serpin complexes. |
Nykjaer A, Conese M, Christensen EI, Olson D, Cremona O, Gliemann J, Blasi F. |
EMBO J. 1997 May 15;16(10):2610-20. |
PMID 9184208 |
Expression of urokinase receptor in various stromal-cell populations in human colon cancer: immunoelectron microscopical analysis. |
Ohtani H, Pyke C, Dano K, Nagura H. |
Int J Cancer. 1995 Sep 15;62(6):691-6. |
PMID 7558416 |
Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth. |
Ossowski L, Aguirre-Ghiso JA. |
Curr Opin Cell Biol. 2000 Oct;12(5):613-20. (REVIEW) |
PMID 10978898 |
Levels of plasminogen activator inhibitor type 1 and urokinase plasminogen activator receptor in non-small cell lung cancer as measured by quantitative ELISA and semiquantitative immunohistochemistry. |
Pappot H, Skov BG, Pyke C, Grondahl-Hansen J. |
Lung Cancer. 1997 Jul;17(2-3):197-209. |
PMID 9237155 |
Murine monoclonal antibodies against murine uPA receptor produced in gene-deficient mice: inhibitory effects on receptor-mediated uPA activity in vitro and in vivo. |
Pass J, Jogi A, Lund IK, Rono B, Rasch MG, Gardsvoll H, Lund LR, Ploug M, Romer J, Dano K, Hoyer-Hansen G. |
Thromb Haemost. 2007 Jun;97(6):1013-22. |
PMID 17549305 |
Prognostic impact of urokinase, urokinase receptor, and type 1 plasminogen activator inhibitor in squamous and large cell lung cancer tissue. |
Pedersen H, Brunner N, Francis D, Osterlind K, Ronne E, Hansen HH, Dano K, Grondahl-Hansen J. |
Cancer Res. 1994 Sep 1;54(17):4671-5. |
PMID 8062262 |
Urokinase receptor is up-regulated in endothelial cells and macrophages associated with fibrinoid deposits in the human placenta. |
Pierleoni C, Castellucci M, Kaufmann P, Lund LR, Schnack Nielsen B. |
Placenta. 2003 Jul;24(6):677-85. |
PMID 12828926 |
The urokinase plasminogen activator receptor as a gene therapy target for cancer. |
Pillay V, Dass CR, Choong PF. |
Trends Biotechnol. 2007 Jan;25(1):33-9. Epub 2006 Nov 7. (REVIEW) |
PMID 17084931 |
The receptor for urokinase-type plasminogen activator and urokinase is translocated from two distinct intracellular compartments to the plasma membrane on stimulation of human neutrophils. |
Plesner T, Ploug M, Ellis V, Ronne E, Hoyer-Hansen G, Wittrup M, Pedersen TL, Tscherning T, Dano K, Hansen NE. |
Blood. 1994b Feb 1;83(3):808-15. |
PMID 8298141 |
Expression of the receptor for urokinase-type plasminogen activator in normal and neoplastic blood cells and hematopoietic tissue. |
Plesner T, Ralfkiaer E, Wittrup M, Johnsen H, Pyke C, Pedersen TL, Hansen NE, Dano K. |
Am J Clin Pathol. 1994a Dec;102(6):835-41. |
PMID 7801901 |
Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom alpha-neurotoxins. |
Ploug M, Ellis V. |
FEBS Lett. 1994 Aug 1;349(2):163-8. (REVIEW) |
PMID 8050560 |
The receptor for urokinase-type plasminogen activator is deficient on peripheral blood leukocytes in patients with paroxysmal nocturnal hemoglobinuria. |
Ploug M, Plesner T, Ronne E, Ellis V, Hoyer-Hansen G, Hansen NE, Dano K. |
Blood. 1992 Mar 15;79(6):1447-55. |
PMID 1312369 |
Glycosylation profile of a recombinant urokinase-type plasminogen activator receptor expressed in Chinese hamster ovary cells. |
Ploug M, Rahbek-Nielsen H, Nielsen PF, Roepstorff P, Dano K. |
J Biol Chem. 1998 May 29;273(22):13933-43. |
PMID 9593742 |
Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol. |
Ploug M, Ronne E, Behrendt N, Jensen AL, Blasi F, Dano K. |
J Biol Chem. 1991 Jan 25;266(3):1926-33. |
PMID 1846368 |
Structure-function relationships in the interaction between the urokinase-type plasminogen activator and its receptor. |
Ploug M. |
Curr Pharm Des. 2003;9(19):1499-528. (REVIEW) |
PMID 12871065 |
Antigen levels of urokinase-type plasminogen activator receptor and its gene polymorphism related to microvessel density in colorectal cancer. |
Przybylowska K, Szemraj J, Kulig A, Dziki A, Ulanska J, Blasiak J. |
Acta Biochim Pol. 2008;55(2):357-63. Epub 2008 May 29. |
PMID 18511987 |
Receptor for urokinase is present in tumor-associated macrophages in ductal breast carcinoma. |
Pyke C, Graem N, Ralfkiaer E, Ronne E, Hoyer-Hansen G, Brunner N, Dano K. |
Cancer Res. 1993 Apr 15;53(8):1911-5. |
PMID 8385573 |
Urokinase-type plasminogen activator is expressed in stromal cells and its receptor in cancer cells at invasive foci in human colon adenocarcinomas. |
Pyke C, Kristensen P, Ralfkiaer E, Grondahl-Hansen J, Eriksen J, Blasi F, Dano K. |
Am J Pathol. 1991 May;138(5):1059-67. |
PMID 1850957 |
Immunohistochemical detection of the receptor for urokinase plasminogen activator in human colon cancer. |
Pyke C, Ralfkiaer E, Ronne E, Hoyer-Hansen G, Kirkeby L, Dano K. |
Histopathology. 1994 Feb;24(2):131-8. |
PMID 8181805 |
Laminin-5 is a marker of invading cancer cells in some human carcinomas and is coexpressed with the receptor for urokinase plasminogen activator in budding cancer cells in colon adenocarcinomas. |
Pyke C, Salo S, Ralfkiaer E, Romer J, Dano K, Tryggvason K. |
Cancer Res. 1995 Sep 15;55(18):4132-9. |
PMID 7664291 |
The urokinase receptor: a ligand or a receptor? Story of a sociable molecule. |
Ragno P. |
Cell Mol Life Sci. 2006 May;63(9):1028-37. (REVIEW) |
PMID 16465446 |
Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect. |
Resnati M, Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F. |
EMBO J. 1996 Apr 1;15(7):1572-82. |
PMID 8612581 |
Urokinase-type plasminogen activator (uPA) and its receptor (uPAR): development of antagonists of uPA/uPAR interaction and their effects in vitro and in vivo. |
Reuning U, Sperl S, Kopitz C, Kessler H, Kruger A, Schmitt M, Magdolen V. |
Curr Pharm Des. 2003;9(19):1529-43. (REVIEW) |
PMID 12871066 |
Prognostic significance of soluble urokinase plasminogen activator receptor in serum and cytosol of tumor tissue from patients with primary breast cancer. |
Riisbro R, Christensen IJ, Piironen T, Greenall M, Larsen B, Stephens RW, Han C, Hoyer-Hansen G, Smith K, Brunner N, Harris AL. |
Clin Cancer Res. 2002 May;8(5):1132-41. |
PMID 12006529 |
The receptor for urokinase-type plasminogen activator is expressed by keratinocytes at the leading edge during re-epithelialization of mouse skin wounds. |
Romer J, Lund LR, Eriksen J, Pyke C, Kristensen P, Dano K. |
J Invest Dermatol. 1994 Apr;102(4):519-22. |
PMID 8151132 |
The urokinase receptor as a potential target in cancer therapy. |
Romer J, Nielsen BS, Ploug M. |
Curr Pharm Des. 2004;10(19):2359-76. (REVIEW) |
PMID 15279614 |
Cancer cell expression of urokinase-type plasminogen activator receptor mRNA in squamous cell carcinomas of the skin. |
Romer J, Pyke C, Lund LR, Ralfkiaer E, Dano K. |
J Invest Dermatol. 2001 Mar;116(3):353-8. |
PMID 11231307 |
Targeting the over-expressed urokinase-type plasminogen activator receptor on glioblastoma multiforme. |
Rustamzadeh E, Li C, Doumbia S, Hall WA, Vallera DA. |
J Neurooncol. 2003 Oct;65(1):63-75. (REVIEW) |
PMID 14649886 |
Laminin-5 as a marker of invasiveness in cervical lesions. |
Skyldberg B, Salo S, Eriksson E, Aspenblad U, Moberger B, Tryggvason K, Auer G. |
J Natl Cancer Inst. 1999 Nov 3;91(21):1882-7. |
PMID 10547396 |
The murine receptor for urokinase-type plasminogen activator is primarily expressed in tissues actively undergoing remodeling. |
Solberg H, Ploug M, Hoyer-Hansen G, Nielsen BS, Lund LR. |
J Histochem Cytochem. 2001 Feb;49(2):237-46. |
PMID 11156692 |
A conserved TATA-less proximal promoter drives basal transcription from the urokinase-type plasminogen activator receptor gene. |
Soravia E, Grebe A, De Luca P, Helin K, Suh TT, Degen JL, Blasi F. |
Blood. 1995 Jul 15;86(2):624-35. |
PMID 7605992 |
Plasma urokinase receptor levels in patients with colorectal cancer: relationship to prognosis. |
Stephens RW, Nielsen HJ, Christensen IJ, Thorlacius-Ussing O, Sorensen S, Dano K, Brunner N. |
J Natl Cancer Inst. 1999 May 19;91(10):869-74. |
PMID 10340907 |
Helicobacter pylori: present status and future prospects in Japan. |
Suzuki H, Hibi T, Marshall BJ. |
J Gastroenterol. 2007 Jan;42(1):1-15. Epub 2007 Feb 16. (REVIEW) |
PMID 17322988 |
The urokinase receptor and integrins in cancer progression. |
Tang CH, Wei Y. |
Cell Mol Life Sci. 2008 Jun;65(12):1916-32. (REVIEW) |
PMID 18345479 |
Peptides and small molecules targeting the plasminogen activation system: towards prophylactic anti-metastasis drugs for breast cancer. |
Tyndall JD, Kelso MJ, Clingan P, Ranson M. |
Recent Pat Anticancer Drug Discov. 2008 Jan;3(1):1-13. (REVIEW) |
PMID 18289119 |
Expression of urokinase plasminogen activator, its receptor and type-1 inhibitor in malignant and benign prostate tissue. |
Usher PA, Thomsen OF, Iversen P, Johnsen M, Brunner N, Hoyer-Hansen G, Andreasen P, Dano K, Nielsen BS. |
Int J Cancer. 2005 Mar 1;113(6):870-80. |
PMID 15515049 |
A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase. |
Vassalli JD, Baccino D, Belin D. |
J Cell Biol. 1985 Jan;100(1):86-92. |
PMID 3880760 |
Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy. |
Waltz DA, Chapman HA. |
J Biol Chem. 1994 May 20;269(20):14746-50. |
PMID 7514182 |
Targeting the urokinase plasminogen activator receptor with synthetic self-assembly nanoparticles. |
Wang M, Lowik DW, Miller AD, Thanou M. |
Bioconjug Chem. 2009 Jan;20(1):32-40. |
PMID 19099499 |
Modification of kidney barrier function by the urokinase receptor. |
Wei C, Moller CC, Altintas MM, Li J, Schwarz K, Zacchigna S, Xie L, Henger A, Schmid H, Rastaldi MP, Cowan P, Kretzler M, Parrilla R, Bendayan M, Gupta V, Nikolic B, Kalluri R, Carmeliet P, Mundel P, Reiser J. |
Nat Med. 2008 Jan;14(1):55-63. Epub 2007 Dec 16. |
PMID 18084301 |
Regulation of integrin function by the urokinase receptor. |
Wei Y, Lukashev M, Simon DI, Bodary SC, Rosenberg S, Doyle MV, Chapman HA. |
Science. 1996 Sep 13;273(5281):1551-5. |
PMID 8703217 |
Identification of the urokinase receptor as an adhesion receptor for vitronectin. |
Wei Y, Waltz DA, Rao N, Drummond RJ, Rosenberg S, Chapman HA. |
J Biol Chem. 1994 Dec 23;269(51):32380-8. |
PMID 7528215 |
Expression and localization of urokinase-type plasminogen activator receptor in human gliomas. |
Yamamoto M, Sawaya R, Mohanam S, Rao VH, Bruner JM, Nicolson GL, Rao JS. |
Cancer Res. 1994 Sep 15;54(18):5016-20. |
PMID 8069869 |
Molecular imaging of pancreatic cancer in an animal model using targeted multifunctional nanoparticles. |
Yang L, Mao H, Cao Z, Wang YA, Peng X, Wang X, Sajja HK, Wang L, Duan H, Ni C, Staley CA, Wood WC, Gao X, Nie S. |
Gastroenterology. 2009 May;136(5):1514-1525.e2. Epub 2009 Jan 14. |
PMID 19208341 |
Correlative studies on uPA mRNA and uPAR mRNA expression with vascular endothelial growth factor, microvessel density, progression and survival time of patients with gastric cancer. |
Zhang L, Zhao ZS, Ru GQ, Ma J. |
World J Gastroenterol. 2006 Jul 7;12(25):3970-6. |
PMID 16810742 |
Citation |
This paper should be referenced as such : |
Jacobsen, B ; Illemann, M ; Ploug, M |
PLAUR (plasminogen activator, urokinase receptor) |
Atlas Genet Cytogenet Oncol Haematol. 2010;14(8):720-731. |
Free journal version : [ pdf ] [ DOI ] |
Other Leukemias implicated (Data extracted from papers in the Atlas) [ 2 ] |
t(19;19)(q13;q13) PLAUR/EXOC3L2
t(19;19)(q13;q13) PLAUR/MARK4 |
External links |
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