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  1. Article: Etude pharmacologique comparant l'effet de la diacerhéine et d'un inhibiteur COX-2 sélectif dans le modèle du granulome induit chez la souris.

    Colville-Nash, P R

    Presse medicale (Paris, France : 1983)

    2002  Volume 31, Issue 39 Pt 2, Page(s) 4S16–7

    Abstract: Unlabelled: ANIMAL MODEL OF DEGENERATIVE JOIN DISEASE: A mouse model of joint disease with an induced granuloma has demonstrated that diacerein inhibits loss of hydroxyproline and proteoglycans in joint cartilage, an effect not observed with ... ...

    Title translation Comparison of the pharmacologic effect of diacerein and a selective COX-2 inhibitor in the mouse induced-granuloma model.
    Abstract Unlabelled: ANIMAL MODEL OF DEGENERATIVE JOIN DISEASE: A mouse model of joint disease with an induced granuloma has demonstrated that diacerein inhibits loss of hydroxyproline and proteoglycans in joint cartilage, an effect not observed with conventional nonsteroidal antiinflammatory drugs (NSAID) or with a specific inhibitor of cyclooxygenase-2 (COX-2). Specific COX-2 inhibitors could thus be beneficially combined with disease modifying osteoarthritis drugs DMOD such as diacerein. ANTIINFLAMMATORY EFFECTS OF COX-2: During the process of inflammation, COX-2 activity appears to occur at two specific time points, with a peak at 2 hours, associated with maximal activity of PGE(2) synthase (proinflammatory prostaglandin) and a second peak after 48 hours, associated with increased levels of PGD(2) and cyclopentenones (anti-inflammatory prostaglandins).
    Therapeutic implications: Treatment with NSAID or selective anti-COX-2 agents appears to have a beneficial effect during acute phases of inflammation but their use in long-term regimens appears to have less favorable effects. Use of long-action symptomatic treatments without any apparent effect on COX-2, for example diacerein, could protect against the potentially deleterious effects of COX-2 inhibition.
    MeSH term(s) Animals ; Anthraquinones/adverse effects ; Anthraquinones/therapeutic use ; Anti-Inflammatory Agents, Non-Steroidal/adverse effects ; Anti-Inflammatory Agents, Non-Steroidal/therapeutic use ; Cyclooxygenase 2 ; Cyclooxygenase 2 Inhibitors ; Cyclooxygenase Inhibitors/adverse effects ; Cyclooxygenase Inhibitors/therapeutic use ; Disease Models, Animal ; Drug Evaluation, Preclinical ; Humans ; Isoenzymes/antagonists & inhibitors ; Membrane Proteins ; Mice ; Osteoarthritis/drug therapy ; Prostaglandin-Endoperoxide Synthases
    Chemical Substances Anthraquinones ; Anti-Inflammatory Agents, Non-Steroidal ; Cyclooxygenase 2 Inhibitors ; Cyclooxygenase Inhibitors ; Isoenzymes ; Membrane Proteins ; diacerein (4HU6J11EL5) ; Cyclooxygenase 2 (EC 1.14.99.1) ; PTGS2 protein, human (EC 1.14.99.1) ; Prostaglandin-Endoperoxide Synthases (EC 1.14.99.1)
    Language French
    Publishing date 2002-12-16
    Publishing country France
    Document type Comparative Study ; Evaluation Study ; Journal Article
    ZDB-ID 120943-7
    ISSN 2213-0276 ; 0755-4982 ; 0032-7867 ; 0301-1518
    ISSN (online) 2213-0276
    ISSN 0755-4982 ; 0032-7867 ; 0301-1518
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  2. Article: Cyclooxygenase enzymes as targets for therapeutic intervention in inflammation.

    Colville-Nash, P R / Gilroy, D W

    Drug news & perspectives

    2003  Volume 13, Issue 10, Page(s) 587–597

    Abstract: The synthesis of bioactive prostanoids is controlled, in part, by the action of the cyclooxygenase (COX; prostaglandin H synthase; prostaglandin endoperoxidase) family of enzymes. Inhibition of these enzymes underlies the therapeutic action of the ... ...

    Abstract The synthesis of bioactive prostanoids is controlled, in part, by the action of the cyclooxygenase (COX; prostaglandin H synthase; prostaglandin endoperoxidase) family of enzymes. Inhibition of these enzymes underlies the therapeutic action of the nonsteroidal antiinflammatory drugs (NSAIDs) and also leads to the adverse side effects, such as gastrointestinal ulceration, associated with these drugs. Interest in the therapeutic targeting of this system as a means of controlling inflammation was further expanded by the demonstration in the early 1990s of the existence of a second, inducible, isoform of COX, COX-2. Originally, it was believed that this isoform was expressed at sites of inflammation but not in noninflamed tissue, where a constitutively expressed isoform, COX-1, was thought to be responsible for the physiological production of eicosanoid mediators. This presented the opportunity to develop novel "super aspirins," which could selectively inhibit the inducible isoform, exert potently antiinflammatory effects and, importantly, be largely devoid of the deleterious side effects of conventional NSAIDs. However, it is now being increasingly accepted that COX-2 is also expressed in chronic inflammatory diseases and is seen during the resolution of inflammatory reactions and in areas undergoing wound healing. Inhibition of this isoform in these situations has revealed potential, previously hidden, pitfalls associated with COX-2 inhibition. This article examines the roles of the COX enzymes in inflammation, with emphasis on the emerging role of COX-2 during inflammatory resolution, as well as discussion of some future directions for antiinflammatory therapy that this research has suggested.
    Language English
    Publishing date 2003-07-23
    Publishing country United States
    Document type Journal Article
    ZDB-ID 885125-6
    ISSN 2013-0139 ; 0214-0934
    ISSN (online) 2013-0139
    ISSN 0214-0934
    DOI 10.1358/dnp.2000.13.10.661378
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  3. Article ; Online: Activation of macrophage peroxisome proliferator-activated receptor-gamma by diclofenac results in the induction of cyclooxygenase-2 protein and the synthesis of anti-inflammatory cytokines.

    Ayoub, Samir S / Botting, Regina M / Joshi, Amrish N / Seed, Michael P / Colville-Nash, Paul R

    Molecular and cellular biochemistry

    2009  Volume 327, Issue 1-2, Page(s) 101–110

    Abstract: Cyclooxygenase-2 (COX-2) is an inducible isoform of the COX family of enzymes central to the synthesis of pro-inflammatory prostaglandins. Induction of COX-2 is mediated by many endogenous and exogenous molecules that include pro-inflammatory cytokines ... ...

    Abstract Cyclooxygenase-2 (COX-2) is an inducible isoform of the COX family of enzymes central to the synthesis of pro-inflammatory prostaglandins. Induction of COX-2 is mediated by many endogenous and exogenous molecules that include pro-inflammatory cytokines and bacterial lipopolysaccharide (LPS). It has been demonstrated that COX-2 can also be induced by diclofenac in cultured J774.2 macrophages. This induction was delayed compared to COX-2 induced by LPS and paracetamol selectively inhibited activity of this protein. The aim of the present study was to determine the transcription factor involved in the production of COX-2 after treatment of J774.2 cells with 500 microM diclofenac. Pre-treatment of cells with the peroxisome proliferator-activated receptor-gamma (PPAR-gamma) antagonists GW9662 (0.1-1 microM) or biphenol A Diglycidyl Ether (100-200 microM) resulted in reduction of the induction of COX-2 by diclofenac, but not by LPS. Induction of COX-2 by the PPAR-gamma agonist 15deoxyDelta(12,14)prostaglandin J(2) was also reduced when the cells were pre-treated with the PPAR-gamma antagonists BADGE or GW9662. On the other hand, pre-treatment of cells with the nuclear factor-kappa-B (NF-kappaB) Super-repressor IkappaBalpha (150-600 nM) reduced the induction of COX-2 by LPS, but not by diclofenac. We, therefore, have identified that PPAR-gamma activation is a requirement for COX-2 induction after diclofenac stimulation of J774.2 cells. These results along with the finding that treatment of J774.2 macrophages with diclofenac resulted in the release of the anti-inflammatory cytokines, interleukin-10 and transforming growth factor-beta suggest that the diclofenac-induced COX-2 protein may possess anti-inflammatory actions.
    MeSH term(s) Animals ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Cyclooxygenase 2/genetics ; Cyclooxygenase 2/metabolism ; Cytokines/biosynthesis ; Diclofenac/pharmacology ; Dose-Response Relationship, Drug ; Inflammation/metabolism ; Lipopolysaccharides/metabolism ; Lipopolysaccharides/pharmacology ; Macrophages/drug effects ; Macrophages/enzymology ; Macrophages/immunology ; Mice ; Mice, Inbred BALB C ; PPAR gamma/metabolism ; Rats ; Rats, Wistar ; Transcription Factors/metabolism
    Chemical Substances Anti-Inflammatory Agents, Non-Steroidal ; Cytokines ; Lipopolysaccharides ; PPAR gamma ; Transcription Factors ; Diclofenac (144O8QL0L1) ; Cyclooxygenase 2 (EC 1.14.99.1)
    Language English
    Publishing date 2009-02-15
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 184833-1
    ISSN 1573-4919 ; 0300-8177
    ISSN (online) 1573-4919
    ISSN 0300-8177
    DOI 10.1007/s11010-009-0048-y
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  4. Article: Potential adverse effects of cyclooxygenase-2 inhibition: evidence from animal models of inflammation.

    Colville-Nash, P R / Gilroy, D W

    BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy

    2001  Volume 15, Issue 1, Page(s) 1–9

    Abstract: Cyclooxygenase (COX; prostaglandin H synthase, prostaglandin endoperoxidase) is the key enzyme in the synthesis of the prostaglandin and thromboxane families of eicosanoid mediators, and is the target for the nonsteroidal anti-inflammatory drugs (NSAIDs). ...

    Abstract Cyclooxygenase (COX; prostaglandin H synthase, prostaglandin endoperoxidase) is the key enzyme in the synthesis of the prostaglandin and thromboxane families of eicosanoid mediators, and is the target for the nonsteroidal anti-inflammatory drugs (NSAIDs). The identification of an inducible COX isoform, COX-2, and the demonstration of its specific expression at sites of inflammation suggested that it may provide a useful therapeutic target for novel anti-inflammatory drugs. Inhibition of an enzyme that is not expressed in most healthy tissues would potentially avoid most of the adverse effects associated with NSAIDs, which target a constitutively expressed isoform, COX-1. The development of novel 'super aspirins' with high selectivity towards the inhibition of COX-2 showed that this hypothesis was well-founded and that high levels of these drugs could be tolerated without these serious adverse effects. The first two of these new generation NSAIDs, celecoxib and rofecoxib, are now in clinical use. More recently, however, concern has been expressed that COX-2 inhibition may in fact have a number of potential, previously hidden, pitfalls. These have arisen from the demonstration that COX-2 induction is not exclusively associated with the onset of an inflammatory reaction, with expression limited to inflammatory sites. In fact, COX-2 is expressed more chronically, and is also seen during the resolution of inflammation and in areas of wound-healing. The application of COX-2-selective inhibitors during these periods has been shown to be deleterious in that resolution of inflammation is delayed, gastric ulcer healing is delayed and, in some patients, ulcers have been shown to progress further to perforation. The suggestion has now been made that, in these situations, COX-2 may help resolve the pathology, perhaps by generating alternative series of prostaglandins such as the cyclopentenone prostaglandins. The finding that these prostaglandins can affect proteins by direct chemical modifications as well as having their own receptor families has rekindled debate on the deleterious and beneficial effects of prostanoids, and the implications of inhibiting the production of these mediators, in the body. Therefore, in this review we discuss the role of COX-2 in inflammation and the potential adverse effects of its inhibition.
    MeSH term(s) Animals ; Cyclooxygenase 2 ; Cyclooxygenase 2 Inhibitors ; Cyclooxygenase Inhibitors/adverse effects ; Humans ; Inflammation/enzymology ; Inflammation/metabolism ; Inflammation/pathology ; Isoenzymes/metabolism ; Membrane Proteins ; Prostaglandin-Endoperoxide Synthases/metabolism
    Chemical Substances Cyclooxygenase 2 Inhibitors ; Cyclooxygenase Inhibitors ; Isoenzymes ; Membrane Proteins ; Cyclooxygenase 2 (EC 1.14.99.1) ; PTGS2 protein, human (EC 1.14.99.1) ; Prostaglandin-Endoperoxide Synthases (EC 1.14.99.1)
    Language English
    Publishing date 2001-04-25
    Publishing country New Zealand
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1364202-9
    ISSN 1179-190X ; 1173-8804
    ISSN (online) 1179-190X
    ISSN 1173-8804
    DOI 10.2165/00063030-200115010-00001
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  5. Article: COX-2 and the cyclopentenone prostaglandins - a new chapter in the book of inflammation?

    Colville-Nash, P R / Gilroy, D W

    Prostaglandins & other lipid mediators

    2000  Volume 62, Issue 1, Page(s) 33–43

    MeSH term(s) Animals ; Cyclooxygenase 2 ; Cyclopentanes/metabolism ; Humans ; Inflammation/metabolism ; Inflammation/physiopathology ; Inflammation Mediators/physiology ; Isoenzymes/metabolism ; Ligands ; Membrane Proteins ; Prostaglandin-Endoperoxide Synthases/metabolism ; Prostaglandins/physiology ; Receptors, Cytoplasmic and Nuclear/metabolism ; Transcription Factors/metabolism
    Chemical Substances Cyclopentanes ; Inflammation Mediators ; Isoenzymes ; Ligands ; Membrane Proteins ; Prostaglandins ; Receptors, Cytoplasmic and Nuclear ; Transcription Factors ; Cyclooxygenase 2 (EC 1.14.99.1) ; PTGS2 protein, human (EC 1.14.99.1) ; Prostaglandin-Endoperoxide Synthases (EC 1.14.99.1) ; cyclopentenone (Q0U2IGF9CK)
    Language English
    Publishing date 2000-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1426962-4
    ISSN 2212-196X ; 1098-8823 ; 0090-6980
    ISSN (online) 2212-196X
    ISSN 1098-8823 ; 0090-6980
    DOI 10.1016/s0090-6980(00)00074-5
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  6. Article: BMP-7 and proximal tubule epithelial cells: activation of multiple signaling pathways reveals a novel anti-fibrotic mechanism.

    Motazed, Reza / Colville-Nash, Paul / Kwan, Jonathan T C / Dockrell, Mark E C

    Pharmaceutical research

    2008  Volume 25, Issue 10, Page(s) 2440–2446

    Abstract: Purpose: Bone morphogenic protein-7 (BMP-7) is a member of the transforming growth factor beta (TGFbeta) superfamily involved in organogenesis. Recent work suggests that BMP-7 can reverse the fibrotic effects of TGFbeta but the underlying mechanism is ... ...

    Abstract Purpose: Bone morphogenic protein-7 (BMP-7) is a member of the transforming growth factor beta (TGFbeta) superfamily involved in organogenesis. Recent work suggests that BMP-7 can reverse the fibrotic effects of TGFbeta but the underlying mechanism is unknown. We sought to determine BMP-7 signaling and its modulation of TGFbeta induced fibrotic outcomes in adult human proximal tubule epithelial cells (PTECs).
    Methods: The effect of BMP-7 on phospho-p38 was assessed by Western blotting, p38 ELISA and Bio-plex phospho-protein assay. Secreted fibronectin (Fn) was measured by ELISA.
    Results: BMP-7 had a concentration-dependent effect on intracellular signaling activating Smad 1/5/8 at higher concentrations and p38 mitogen activated protein (MAP) kinase at lower concentrations in both primary and transformed PTECs; BMP-7 caused phosphorylation of p38 at 2.5 ng/ml and Smads at 200 ng/ml. Similarly, nuclear accumulation of phospho-p38 and Smad were observed at these respective concentrations. These results suggested an inverse relationship between activation of Smads and p38 MAP kinase in this context. Consistent, with this BMP7 at 200 ng/ml reduced TGFbeta-induced p38 MAP activation and the p38-dependent TGFbeta-induced Fn secretion by PTECs.
    Conclusion: We have shown novel p38/Smad signaling along a BMP-7 gradient and demonstrated BMP-7 regulation of TGFbeta MAP kinase signaling and fibrotic outcomes.
    MeSH term(s) Active Transport, Cell Nucleus ; Bone Morphogenetic Protein 7 ; Bone Morphogenetic Proteins/metabolism ; Bone Morphogenetic Proteins/pharmacology ; Cell Line, Transformed ; Dose-Response Relationship, Drug ; Epithelial Cells/drug effects ; Epithelial Cells/enzymology ; Epithelial Cells/metabolism ; Epithelial Cells/pathology ; Fibronectins/metabolism ; Fibrosis ; Humans ; Kidney Tubules, Proximal/drug effects ; Kidney Tubules, Proximal/enzymology ; Kidney Tubules, Proximal/metabolism ; Kidney Tubules, Proximal/pathology ; Phosphorylation ; Signal Transduction/drug effects ; Smad Proteins, Receptor-Regulated/metabolism ; Time Factors ; Transforming Growth Factor beta/metabolism ; Transforming Growth Factor beta/pharmacology ; p38 Mitogen-Activated Protein Kinases/metabolism
    Chemical Substances BMP7 protein, human ; Bone Morphogenetic Protein 7 ; Bone Morphogenetic Proteins ; Fibronectins ; Smad Proteins, Receptor-Regulated ; Transforming Growth Factor beta ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
    Language English
    Publishing date 2008-02-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 843063-9
    ISSN 1573-904X ; 0724-8741 ; 0739-0742
    ISSN (online) 1573-904X
    ISSN 0724-8741 ; 0739-0742
    DOI 10.1007/s11095-008-9551-1
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  7. Article ; Online: Role played by disabled-2 in albumin induced MAP Kinase signalling.

    Diwakar, Ramaswamy / Pearson, Alexander L / Colville-Nash, Paul / Baines, Deborah L / Dockrell, Mark E C

    Biochemical and biophysical research communications

    2008  Volume 366, Issue 3, Page(s) 675–680

    Abstract: Albumin has been shown to activate the mitogen activated protein kinase (MAPK) pathway in proximal tubular cells (PTECs) of the kidney. Megalin, the putative receptor for albumin has potential signalling properties. However, the mechanisms by which ... ...

    Abstract Albumin has been shown to activate the mitogen activated protein kinase (MAPK) pathway in proximal tubular cells (PTECs) of the kidney. Megalin, the putative receptor for albumin has potential signalling properties. However, the mechanisms by which megalin signals are unclear. The adaptor phosphoprotein Disabled-2 (Dab2) is known to interact with the cytoplasmic tail of megalin and may be involved in albumin-mediated MAPK signalling. In this study, we investigated the role of Dab2 in albumin-mediated MAPK signalling and further studied the role of Dab2 in albumin-induced TGFbeta-1 secretion, a MAPK dependent event. We used RNA interference to knockdown Dab2 protein abundance in HKC-8 cells a model of human PTECs. Albumin activated ERK1,2 and Elk-1 in a MEK-1 dependent manner and resulted in secretion of TGFbeta-1. In the absence of albumin, knockdown of Dab2 resulted in a trend towards increase in pERK1,2 consistent with its putative role as an inhibitor of cell proliferation. However albumin-induced ERK1,2 activation was completely abolished by Dab2 knockdown. Dab2 knockdown did not however result in inhibition of albumin-induced TGFbeta-1 secretion. These results suggest that Dab2 is a ligand dependent bi-directional regulator of ERK1,2 activity by demonstrating that in addition to its more traditional role as an inhibitor of ERK1,2 it may also activate ERK1,2.
    MeSH term(s) Cell Line ; Humans ; Kidney/drug effects ; Kidney/metabolism ; Low Density Lipoprotein Receptor-Related Protein-2/metabolism ; MAP Kinase Signaling System/drug effects ; MAP Kinase Signaling System/physiology ; Serum Albumin/administration & dosage ; Transforming Growth Factor beta1/metabolism ; ras GTPase-Activating Proteins/metabolism
    Chemical Substances DAB2IP protein, human ; Low Density Lipoprotein Receptor-Related Protein-2 ; Serum Albumin ; Transforming Growth Factor beta1 ; ras GTPase-Activating Proteins
    Language English
    Publishing date 2008-02-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2007.11.171
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  8. Article: New insights into the role of COX 2 in inflammation.

    Gilroy, D W / Colville-Nash, P R

    Journal of molecular medicine (Berlin, Germany)

    2000  Volume 78, Issue 3, Page(s) 121–129

    Abstract: Cyclo-oxygenase (COX) is responsible for the synthesis of bioactive prostanoids, the inhibition of which serves as the basis for the mode of action of clinically used nonsteroidal anti-inflammatory drugs. While there were suggestions as early as the ... ...

    Abstract Cyclo-oxygenase (COX) is responsible for the synthesis of bioactive prostanoids, the inhibition of which serves as the basis for the mode of action of clinically used nonsteroidal anti-inflammatory drugs. While there were suggestions as early as the 1970s that an inducible isoform of COX exists, it was only in the early 1990s that COX 2 was identified, cloned and sequenced. Not surprisingly, this new isoform was expressed at sites of inflammation and reported to contribute to the inflammatory response. Recently, however, evidence is emerging to suggest that COX 2 also has anti-inflammatory properties. In this review, the two faces of COX 2 are examined, with emphasis on its role in regulating inflammatory resolution, including possible mechanisms of action
    MeSH term(s) Animals ; Anti-Inflammatory Agents/pharmacology ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Cyclooxygenase 1 ; Cyclooxygenase 2 ; Humans ; Inflammation/metabolism ; Isoenzymes/metabolism ; Isoenzymes/physiology ; Membrane Proteins ; Models, Biological ; Prostaglandin-Endoperoxide Synthases/metabolism ; Prostaglandin-Endoperoxide Synthases/physiology ; Prostaglandins/metabolism ; Protein Isoforms ; Stress, Physiological
    Chemical Substances Anti-Inflammatory Agents ; Anti-Inflammatory Agents, Non-Steroidal ; Isoenzymes ; Membrane Proteins ; Prostaglandins ; Protein Isoforms ; Cyclooxygenase 1 (EC 1.14.99.1) ; Cyclooxygenase 2 (EC 1.14.99.1) ; PTGS1 protein, human (EC 1.14.99.1) ; PTGS2 protein, human (EC 1.14.99.1) ; Prostaglandin-Endoperoxide Synthases (EC 1.14.99.1)
    Language English
    Publishing date 2000
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 1223802-8
    ISSN 1432-1440 ; 0946-2716
    ISSN (online) 1432-1440
    ISSN 0946-2716
    DOI 10.1007/s001090000094
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  9. Article: The role played by endocytosis in albumin-induced secretion of TGF-beta1 by proximal tubular epithelial cells.

    Diwakar, Ramaswamy / Pearson, Alex L / Colville-Nash, Paul / Brunskill, Nigel J / Dockrell, Mark E C

    American journal of physiology. Renal physiology

    2007  Volume 292, Issue 5, Page(s) F1464–70

    Abstract: Proteinuria predicts the decline of renal function in chronic kidney disease. Reducing albuminuria has been shown to be associated with a reduction in this rate of decline. Proximal tubular epithelial cells (PTECs), when exposed to albumin produce matrix ...

    Abstract Proteinuria predicts the decline of renal function in chronic kidney disease. Reducing albuminuria has been shown to be associated with a reduction in this rate of decline. Proximal tubular epithelial cells (PTECs), when exposed to albumin produce matrix proteins, proinflammatory and profibrotic cytokines like TGF-beta(1). Some of these effects are dependent on endocytosis of albumin by PTECs. However, conditions like diabetic nephropathy, believed to be associated with reduced albumin endocytosis, are associated with interstitial fibrosis. Moreover, megalin, the putative albumin binding receptor in PTECs, has potential signaling motifs in its cytoplasmic domain, suggesting its ability to signal in response to ligand binding from the apical surface of PTECs. Hence, we looked to see whether albumin-induced secretion of TGF-beta(1) by PTECs is dependent on albumin endocytosis or whether it could occur in the absence of albumin endocytosis. We studied the production of TGF-beta(1) in two accepted models of PTECs, opossum kidney cells and human kidney cell clone-8 cells, with widely varying degrees of endocytosis. We then studied the effect of inhibiting albumin endocytosis with various inhibitors on albumin-induced TGF-beta(1) secretion. Our results indicate that albumin-induced TGF-beta(1) secretion by PTECs does not require albumin endocytosis and therefore the mechanism for the induction of some profibrotic responses by albumin may differ from those required for some of the inflammatory responses. Moreover, we found that albumin-induced TGF-beta(1) secretion by PTECs is not dependent on its interaction with megalin.
    MeSH term(s) Amiloride/analogs & derivatives ; Amiloride/pharmacology ; Animals ; Cell Line ; Clone Cells ; Endocytosis/drug effects ; Endocytosis/physiology ; Epithelial Cells/secretion ; Humans ; Hydroxymethylglutaryl-CoA Reductase Inhibitors/pharmacology ; Kidney Tubules, Proximal/cytology ; Kidney Tubules, Proximal/secretion ; Low Density Lipoprotein Receptor-Related Protein-2/physiology ; Opossums ; Receptors, Transforming Growth Factor beta/physiology ; Serum Albumin/pharmacokinetics ; Serum Albumin/pharmacology ; Simvastatin/pharmacology ; Sodium-Hydrogen Exchangers/antagonists & inhibitors ; Transforming Growth Factor beta1/biosynthesis ; Transforming Growth Factor beta1/secretion
    Chemical Substances Hydroxymethylglutaryl-CoA Reductase Inhibitors ; Low Density Lipoprotein Receptor-Related Protein-2 ; Receptors, Transforming Growth Factor beta ; Serum Albumin ; Sodium-Hydrogen Exchangers ; Transforming Growth Factor beta1 ; Amiloride (7DZO8EB0Z3) ; Simvastatin (AGG2FN16EV) ; ethylisopropylamiloride (VW50CE070T)
    Language English
    Publishing date 2007-05
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 603837-2
    ISSN 1522-1466 ; 1931-857X ; 0363-6127
    ISSN (online) 1522-1466
    ISSN 1931-857X ; 0363-6127
    DOI 10.1152/ajprenal.00069.2006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Growth factors in angiogenesis: current interest and therapeutic potential.

    Colville-Nash, P R / Willoughby, D A

    Molecular medicine today

    1997  Volume 3, Issue 1, Page(s) 14–23

    Abstract: Angiogenesis, the process of new blood vessel development, is an essential component of the body's physiology and contributes to the pathogenesis of a variety of diseases such as benign and malignant neoplasia and rheumatoid arthritis. Failure of this ... ...

    Abstract Angiogenesis, the process of new blood vessel development, is an essential component of the body's physiology and contributes to the pathogenesis of a variety of diseases such as benign and malignant neoplasia and rheumatoid arthritis. Failure of this physiological response is also important in abnormalities of wound healing in diseases such as duodenal ulceration and diabetes. Angiogenesis is controlled by a variety of factors that initiate, control and terminate this complex, multi-stage process. This review covers those factors that are exciting much interest currently and have potential for incorporation into clinical medicine.
    MeSH term(s) Animals ; Forecasting ; Growth Substances/physiology ; Humans ; Neovascularization, Pathologic ; Neovascularization, Physiologic/physiology
    Chemical Substances Growth Substances
    Language English
    Publishing date 1997-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1281487-8
    ISSN 1878-4178 ; 1357-4310
    ISSN (online) 1878-4178
    ISSN 1357-4310
    DOI 10.1016/S1357-4310(96)10048-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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