Expressions and functions of phosphodiesterase enzymes are different in different region of the rat heart

Date

2016-06-30

Author

Derici, Mehmet Kursat
Sadi, Gökhan
Cenik, Başar
Güray, Nülüfer Tülün
Demirel Yılmaz, Emine

Metadata

Show full item record

Item Usage Stats

135
views

0
downloads

Phosphodiesterase (PDE) enzymes are responsible for the breakdown of cAMP and cGMP and adjust the levels of cyclic nucleotides in heart. Alteration of PDE enzymes expression in different tissues caused conflicts between functional and clinical effects of PDE inhibitors. Therefore the aim of this study was to investigate the functional role and gene/protein expression of PDE enzymes in atrial and ventricular regions of the rat heart. The spontenously beating right atrium and electrically stimulated left papillary muscles from Wistar albino rats were placed in organ bath. The effects of PDE1, 2, 3, 4, 5 inhibitors (Vinpocetine, EHNA, Milrinone, Rolipram Sildenafil) on functions were recorded. The expressions of PDE’s in tissues as well as in enzymatically isolated atrial and ventricular cells were examined by Real Time PCR and Western blot. Right atrial contractions have been increased with Vinpocetine while suppressed by EHNA, Milrinone, Rolipram and Sildenafil. Unlike Milrinone and Sildenafil, Vinpocetine increases the heart rate whereas EHNA and Rolipram have not any significant effect. Left papillary muscle contractions have been increased only with the Vinpocetine while other PDE inhibitors have not been the emergence of a significant effect. The mRNA and protein levels of PDE enzymes were significantly different in atrial and ventricular intact tissues or isolated cells. PDE-1, 2, 3, 4 and 5 enzymes show functional and regional differences in the rat heart. Therefore, these differences should be taken into account in the experimental or therapeutic approaches of the heart.

Subject Keywords

Phosphodiesterases, Right atrium, Papillary muscle

URI

https://hdl.handle.net/11511/87220
https://www.ephar2016.org/post_congress_book.pdf

Conference Name

7th European Congress of Pharmacology (EPHAR2016), 26-30 June 2016

Collections

Department of Biology, Conference / Seminar

Suggestions

OpenMETU
Core

Expression and activity analyses of industrially important extracellular enzymes produced by a bacilysin knock-out mutant of Bacillus Subtilis Aytekin, Samet; Özcengiz, Gülay; Okay, Sezer; Department of Molecular Biology and Genetics (2018) Bacilysin, the smallest peptide antibiotic known to date, is produced non-ribosomally by Bacillus subtilis by the collective actions of seven proteins transcribed from bacABCDEF operon and bacG gene. Bacilysin is a two-amino acid peptide composed of L-alanine and a modified amino acid, L-anticapsin. Bacilysin biosynthesis was shown to be strongly regulated by quorum sensing through the actions of global regulator proteins including Spo0K, Spo0H, Spo0A, ComQ/ComX, ComP/ComA as well as several Phr proteins, O...
Stability of a recombinant plasmid carrying alpha-amylase gene in Bacillus subtilis Gültekin, Güzin Candan; Bayındırlı, Alev (1998-03-01) Plasmid pSB6 is a streptococcal recombinant plasmid carrying the alpha-amylase gene of Bacillus amyloliquefaciens and the chloramphenicol resistance gene. The segregational and structural instabilities of this plasmid were examined under non-selective conditions in Bacillus subtilis. These instabilities were modelled according to a kinetic expression derived from the difference in the growth between plasmid-bearing and plasmid-free cells. This plasmid showed slight segregational instability and much higher ...
Expression of recombinant acid protease (thermopsin) gene from Thermoplasma volcanium Koyuncu, Bilsev; Kocabıyık, Semra; Department of Biology (2006) Acid proteases, commonly known as aspartic proteases are degredative enzymes which catalyze the cleavage reaction of peptide bonds in proteins with a pH optimum in the acidic range (pH 3-4). Acid proteases have crucial roles in metabolism. Moreover, they are used in different fields of industry. Thermophilic microorganisms, especially archaea, gain special interest because of their thermal stability for both fundamental and industrial researches. Thermopsin is an extracellular acid protease and a member of ...
Expression profiling of thermoplasma volcanium GSS1 under stress conditions with specific emphasis on proteasome associated regulatory VAT genes Yılmaz, Tülay; Kocabıyık, Semra; Department of Biology (2013) In this study differential expression of the two proteasome associated VAT genes (TVNO382 and TVN0947) of Thermoplasma volcanium GSS1 (Tpv) cells challenged by extracellular stresses, i.e., pH, heat-shock and hydrogen peroxide were investigated using quantitative RT-PCR and Western blotting/hybridization techniques. We also performed a comprehensive transcriptome analysis of the Tpv as response to environmental stresses by genome-wide expression arrays. Quantitative RT-PCR analyses revealed that VAT genes e...
Determination and metabolic engineering of rate limiting reactions in aromatic amino acid pathway in Bacillus subtilis for L-phenylaianine production Guzide, Calik; Yasemin, Demirci; Pinar, Calik; Ozdamar, Tuncer H. (2007-09-01) Rate limiting reactions in the aromatic-group amino acid pathway (AAAP) in Bacillus subtilis for l-phenylalanine (Phe) production were determined as reported elsewhere (Özçelik-Şenver et al., 2004). The biochemical reactions in the AAAP start with the reaction using phosphoenolpyruvate (PEP) and erythrose 4-phosphate (E4P) synthesised in the glycolysis pathway and the PPP, respectively, leading to the formation of Phe via chorismate by branching at prephenate. The branch-point metabolites E4P supplied in vi...

Citation Formats

M. K. Derici, G. Sadi, B. Cenik, N. T. Güray, and E. Demirel Yılmaz, “Expressions and functions of phosphodiesterase enzymes are different in different region of the rat heart,” presented at the 7th European Congress of Pharmacology (EPHAR2016), 26-30 June 2016, Istanbul, TURKEY, 2016, Accessed: 00, 2021. [Online]. Available: https://hdl.handle.net/11511/87220.