PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 8561424

[In vitro endothelial dysfunction after cold storage: comparison with various preservative solutions].

F Dagenais·J Buluran·R Cartier
View original source ↗Export metadata ↓

Abstract

Optimal solution for endothelial function preservation during cold storage for organ transplant has not yet been defined. To assess this issue, rat aortic rings (n = 28) were stored for 4 hours at 4 degrees C in different preservation solutions: Krebs Ringer (KR), normal saline (NS), rat blood (RB), and the University of Wisconsin solution (UW). Subsequently, rings were suspended in organ chambers for endothelial and smooth muscle assessment. Endothelial-dependent relaxation responses were tested by exposure to cumulative doses of acetylcholine (ACH), adenosine diphosphate (ADP), and histamine (HIS). Smooth muscle function was evaluated by exposure to norepinephrine (NE) and sodium nitroprusside (SNP). A fifth group not submitted to a storage period was used as control (CTL, n = 7). Results are expressed as maximal relaxation (%) from initial precontraction level. Compared to the CTL group, all storage groups showed a significant decrease in endothelial-dependent relaxations to ACH, ADP and HIS (p < 0.05). Among the stored groups, endothelial-dependent relaxation to ACH was significantly decreased in the NS group when compared to the UW group (p < 0.05). Endothelial-independent relaxation to SNP was comparable for all groups. However significant hypercontractility to NE was observed for all stored groups compared to the control group (p < 0.01). A significant decrease in ADP response was observed with NS and RB storage when compared to KR (p < 0.01). In conclusion, cold storage affects both endothelial and smooth muscle function by decreasing endothelial-dependent responses to ACH, ADP and HIS and increasing smooth muscle reactivity to NE. However, endothelial dysfunction was lessened with UW or KR storage compared to NS or RB.

Explore related subjects

AdenosineAllopurinolAnimalsAorta, ThoracicBloodCold TemperatureEndothelium, VascularGlutathioneIn Vitro TechniquesInsulinIsotonic SolutionsMaleMuscle, Smooth, VascularOrgan Preservation SolutionsRaffinoseRatsRats, Sprague-DawleySodium ChlorideTissue PreservationVasodilationComparative StudyEnglish AbstractJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

F Dagenais, J Buluran, R Cartier. 1995. [In vitro endothelial dysfunction after cold storage: comparison with various preservative solutions].. https://pubmed.ncbi.nlm.nih.gov/8561424/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Solution structure of domain 6 from a self-splicing group II intron ribozyme: a Mg(2+) binding site is located close to the stacked branch adenosine.

Group II intron self-splicing is essential for the correct expression of organellar genes in plants, fungi, and yeast, as well as of bacterial genes. Self-excision of these autocatalytic introns from the primary RNA transcript is achieved in a two-step mechanism that is apparently analogous to that of the eukaryotic spliceosome. The 2'-OH of a conserved adenosine (the branch point) located within domain 6 (D6) acts as the nucleophile in the first step of splicing. Despite the biological importance of group II introns, little is known about their structural organization and usage of metal ions in catalysis. Here we report the first solution structure of a catalytically active D6 construct encompassing the branch point and the neighboring helical regions from the mitochondrial yeast intron ai5gamma. The branch adenosine is the single unpaired nucleotide, and, in contrast to the spliceosomal branch site, resides within the helix, being partially stacked between two flanking GU wobble pairs. We identified a novel prominent Mg(2+) binding site in the major groove of the branch site. Importantly, Mg(2+) addition does not impair the stacking of the branch adenosine, rather it strengthens the interaction with the flanking uridines, as shown by NMR and fluorescence studies. This means that domain 6 presents the branch adenosine in a stacked fashion to the core of group II introns upon folding to the active conformation.

Adenosine↗
PubMed2007

Synthesis and biological evaluation of novel 1-deoxy-1-[6-[((hetero)arylcarbonyl)hydrazino]- 9H-purin-9-yl]-N-ethyl-beta-D-ribofuranuronamide derivatives as useful templates for the development of A2B adenosine receptor agonists.

The lack of molecules endowed with selective and potent agonistic activity toward the hA2B adenosine receptors has limited the studies on this pharmacological target and consequently the evaluation of its therapeutic potential. We report the design and the synthesis of the first potent (EC50 in the nanomolar range) and selective hA2B adenosine receptor agonists consisting of 1-deoxy-1-[6-[((hetero)arylcarbonyl)hydrazino]-9H-purin-9-yl]-N-ethyl-beta-D-ribofuranuronamide derivatives. The concurrent effect of 6-substitution of the purine nucleus with a ((hetero)arylcarbonyl)hydrazino function and a 2-chloro substitution has been investigated in such NECA derivatives.

Adenosine↗
PubMed2007

Enhanced CXCL1 production and angiogenesis in adenosine-mediated lung disease.

Angiogenesis is a feature of chronic lung diseases such as asthma and pulmonary fibrosis; however, the pathways controlling pathological angiogenesis during lung disease are not completely understood. Adenosine is a signaling molecule that has been implicated in the exacerbation of chronic lung disease and in the regulation of angiogenesis; however, the relationship between these factors has not been investigated. The current study utilized adenosine deaminase (ADA)-deficient mice to determine whether chronic elevations in adenosine in vivo result in pulmonary angiogenesis. Results demonstrate substantial angiogenesis in the tracheas of ADA-deficient mice in association with adenosine elevations. ADA replacement enzyme therapy resulted in a lowering of adenosine levels and reversal of tracheal angiogenesis, indicating that the increases in vessel number are dependent on adenosine elevations. Levels of the angiogenic chemokine CXCL1 (mouse functional homologue of human IL-8) were found to be elevated in an adenosine-dependent manner in the lungs of ADA-deficient mice. Neutralization of CXCL1 and its receptor, CXCR2, resulted in the inhibition of angiogenic activity, which suggests that CXCL1 signaling through the CXCR2 receptor mediated the observed increases in angiogenesis. Our findings suggest that adenosine plays an important role, via CXCL1, in the induction of pulmonary angiogenesis.

Adenosine↗