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  • 1
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  44. Kongress der Deutschen Gesellschaft für Rheumatologie (DGRh); 30. Jahrestagung der Deutschen Gesellschaft für Orthopädische Rheumatologie (DGORh); 26. Jahrestagung der Gesellschaft für Kinder- und Jugendrheumatologie (GKJR); 20160831-20160903; Frankfurt am Main; DOCKR.10 /20160829/
    Publication Date: 2016-08-29
    Keywords: JIA ; Kohortenstudie ; ICON ; inaktive Erkrankung ; Krankheitsaktivität ; Lebensqualität ; ddc: 610
    Language: German
    Type: conferenceObject
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  • 2
    Keywords: CELLS ; EXPRESSION ; tumor ; Germany ; human ; ENZYMES ; PROTEIN ; TISSUE ; TISSUES ; ALPHA ; TRANSPORT ; IDENTIFICATION ; GLUTATHIONE ; resistance ; PLASMA ; MEMBRANE ; SURFACE ; LOCALIZATION ; PLASMA-MEMBRANE ; EPITHELIAL-CELLS ; MULTIDRUG-RESISTANCE ; SMOOTH-MUSCLE ; multidrug resistance ; RECOMBINANT ; CYCLOOXYGENASE-2 ; urinary tract ; plasma membrane ; ENZYME ; immunofluorescence ; membrane transport proteins ; multidrug resistance protein ; SUBFAMILY ; enzymology ; DRUGS ; ABCC4 protein,human ; IMMUNOHISTOCHEMICAL LOCALIZATION ; MRP4 ; PROSTAGLANDIN-E SYNTHASE ; prostaglandins
    Abstract: Purpose: The seminal vesicles are the major source of prostaglandins in seminal fluid. For prostanoid action on cell surfaces they must be released from synthesizing cells. MRP4/ABCC4 (multidrug resistance protein 4 adenosine triphosphate-binding cassette, subfamily C, member 4) is an adenosine triphosphate dependent export pump for organic anions that may mediate prostanoid transport across the plasma membranes. Therefore, we analyzed whether MRP4 is expressed in the seminal vesicles and other tissues of the human urogenital tract, whether MRP4 and prostanoid synthesizing enzymes are co-expressed in the same cell type and whether MRP4 functions as a prostanoid export pump. Materials and Methods: The expression and localization of MRP4 and prostanoid synthesizing enzymes were investigated in several tissues of the male human urogenital tract by immunoblot and immunofluorescence analyses. Prostanoid transport was measured into inside-out membrane vesicles from cells expressing recombinant human MRP4. Results: MRP4 and prostanoid synthesizing enzymes were co-expressed in the epithelial cells of human seminal vesicles. Moreover, MRP4 was localized in the plasma membrane of epithelial cells of the ureter, in the basolateral membrane of glandular epithelial cells of the prostate, and in smooth muscle cells of the bladder and corpus cavernosum. Transport studies established MRP4 as an efflux pump for prostaglandin E-2 (Michaelis constant [K-m] 3.5 mu M), thromboxane 132 (K-m 9.9 mu M) and prostaglandin F-2 alpha (K-m 12.6 mu M). Conclusions: The co-expression of prostanoid synthesizing enzymes and MRP4 in epithelial cells of the human seminal vesicles and the function of MRP4 as a prostanoid efflux pump indicate that MRP4 mediates prostanoid transport from these cells, which are the main prostanoid synthesizing cells in the male urogenital tract
    Type of Publication: Journal article published
    PubMed ID: 16280858
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  • 3
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  42. Kongress der Deutschen Gesellschaft für Rheumatologie (DGRh); 28. Jahrestagung der Deutschen Gesellschaft für Orthopädische Rheumatologie (DGORh); 24. wissenschaftliche Jahrestagung der Gesellschaft für Kinder- und Jugendrheumatologie (GKJR); 20140917-20140920; Düsseldorf; DOC43.07 - KR.31 /20140912/
    Publication Date: 2014-09-13
    Keywords: Juvenile idiopathische Arthritis ; Inzeptionskohorte ; inaktive Erkrankung ; ddc: 610
    Language: German
    Type: conferenceObject
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  • 4
    Keywords: EXPRESSION ; NITRIC-OXIDE ; kidney ; MEMBRANE ; physiology ; SMOOTH-MUSCLE ; CONJUGATE EXPORT PUMP ; CYCLIC-GMP ; MOAT-C ; SILDENAFIL
    Abstract: PURPOSE: The intracellular messenger cyclic guanosine monophosphate (cGMP) has an important role in regulating smooth muscle tone. An increase in intracellular cGMP levels is a prerequisite for penile erection. Inhibition of cGMP degradation by cGMP specific phosphodiesterase 5 has been used for treating erectile dysfunction. In addition to degradation by phosphodiesterase, cGMP is exported from cells by multidrug resistance protein 5 (MRP5), also called ABCC5, which we recently identified as an adenosine triphosphate dependent export pump for cGMP. MRP5 is potently inhibited by substances known as phosphodiesterase inhibitors, including sildenafil and trequinsin. Therefore, we analyzed whether MRP5 is expressed in tissues of the human genitourinary system and whether MRP5 and phosphodiesterase 5 proteins are localized in the same cell types. MATERIALS AND METHODS: Localization of MRP5 and phosphodiesterase 5 was analyzed by immunofluorescence microscopy in cryosections of various tissues of the human genitourinary system. RESULTS: MRP5 and phosphodiesterase 5 were co-expressed in smooth muscle cells of the corpus cavernosum, ureter, urethra and bladder. In addition, MRP5 and phosphodiesterase 5 were localized in epithelial cells of the mucosa in the ureter and urethra, and in blood vessels of the lamina propria. CONCLUSIONS: The co-expression of MRP5 and phosphodiesterase 5 in smooth muscle cells of the genitourinary system indicates 2 distinct pathways for cGMP removal. Thus, MRP5 inhibition represents a new approach for enhancing cGMP levels in smooth muscle cells and developing drugs for erectile dysfunction.
    Type of Publication: Journal article published
    PubMed ID: 11956491
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