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Wyświetlanie 1-2 z 2
Tytuł:
p19 detected in the rat retina and pineal gland is a guanylyl cyclase-activating protein (GCAP).
Autorzy:
Dejda, Agnieszka
Matczak, Izabela
Gorczyca, Wojciech
Powiązania:
https://bibliotekanauki.pl/articles/1043693.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
pineal gland
rat
guanylyl cyclase
calcium-binding proteins
guanylyl cyclase-activating proteins
retina
Opis:
The Ca2+-dependent activation of retina-specific guanylyl cyclase (retGC) is mediated by guanylyl cyclase-activating proteins (GCAPs). Here we report for the first time detection of a 19 kDa protein (p19) with GCAP properties in extracts of rat retina and pineal gland. Both extracts stimulate synthesis of cGMP in rod outer segment (ROS) membranes at low (30 nM) but not at high (1 mM) concentrations of Ca2+. At low Ca2+, immunoaffinity purified p19 activates guanylyl cyclase(s) in bovine ROS and rat retinal membranes. Moreover, p19 is recognized by antibodies against bovine GCAP1 and, similarly to other GCAPs, exhibits a Ca2+-dependent electrophoretic mobility shift.
Źródło:
Acta Biochimica Polonica; 2002, 49, 4; 899-905
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Metabolism of cyclic GMP in peritoneal macrophages of rat and guinea pig.
Autorzy:
Kobiałka, Marcin
Witwicka, Hanna
Siednienko, Jakub
Gorczyca, Wojciech
Powiązania:
https://bibliotekanauki.pl/articles/1043463.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
guinea pig
rat
signal transduction
phosphodiesterases
guanylyl cyclases
protein kinases
cyclic nucleotides
macrophages
Opis:
The aim of our studies was to establish which enzymes constitute the "cGMP pathway" in rat and guinea pig peritoneal macrophages (PM). We found that in guinea pig PM synthesis of the nucleotide was significantly enhanced in response to activators of soluble guanylyl cyclase (sGC) and it was only slightly stimulated by specific activators of particulate guanylyl cyclases (pGC). In contrast, rat PM responded strongly to atrial natriuretic peptide (ANP), the activator of pGC type A. The rat cells synthesized about three-fold more cGMP than an equal number of the guinea pig cells. The activity of phosphodiesterases (PDE) hydrolyzing cGMP was apparently regulated by cGMP itself in PM of both species and again it was higher in the rat cells than in those isolated from guinea pig. However, guinea pig PM revealed an activity of Ca2+/calmodulin-dependent PDE1, which was absent in the rat cells. Using Western blotting analysis we were unable to detect the presence of cGMP-dependent protein kinase 1 (PKG1) in PM isolated from either species. In summary, our findings indicate that particulate GC-A is the main active form of GC in the rat PM, while in guinea pig macrophages the sGC activity dominates. Since the profiles of the PDE activities in rat and guinea pig PM are also different, we conclude that the mechanisms regulating cGMP metabolism in PM are species-specific. Moreover, our results suggest that targets for cGMP other than PKG1 should be present in PM of both species.
Źródło:
Acta Biochimica Polonica; 2003, 50, 3; 837-847
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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