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Results for “ADENOSINE TRIPHOSPHATE”

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At least 883 records · Page 49Linked to original sources
PubMed1992

Magnesium-adenosine triphosphate in the treatment of shock, ischemia, and sepsis.

PURPOSE: To review the rationale for adenosine triphosphate-magnesium chloride (ATP-MgCl2) administration in shock, ischemia, and sepsis; the beneficial effects on cellular and organ functions and survival; and possible mechanisms of these effects. DATA SOURCES: Current literature review. STUDY SELECTION: Articles deemed most pertinent, current, and representative were utilized. DATA SYNTHESIS: Despite apparent, adequate resuscitation of hypovolemic shock and sepsis in experimental animals and patients, persistent cellular and organ dysfunction is apparent. Disturbances in organ microcirculation and tissue hypoxia appear to play an important role. These disturbances occur when the energy needs are increased. Because of the theoretical benefits of ATP-MgCl2 as an energy source, as well as a vasodilator, the administration of ATP-MgCl2 has been investigated extensively, and considerable evidence suggests that ATP-MgCl2 restores the depressed cell and organ functions following ischemia, hypovolemic shock, and sepsis. CONCLUSIONS: ATP-MgCl2 improves cellular and organ function and survival following experimental shock, ischemia, and sepsis. Studies also indicate that ATP-MgCl2 can be administered safely in experimental animals and in normal human volunteers, as well as in patients following various adverse circulatory conditions. Further trials should be undertaken to determine the effects on cell and organ function in patients following traumatic shock and sepsis.

Adenosine Triphosphate↗
PubMed2003

Adenosine triphosphate binding cassette (ABC) transporters are expressed and regulated during terminal keratinocyte differentiation: a potential role for ABCA7 in epidermal lipid reorganization.

Central aspects of the cellular lipid trafficking mechanisms that occur during keratinocyte differentiation are still not well understood. In the past years, evidence has accumulated to suggest that members of the superfamily of adenosine triphosphate binding cassette (ABC) transporters are critically involved in the transmembrane transport of cellular lipids. To test the hypothesis that ABC molecules are potentially involved in the epidermal transport of sphingolipids, glycerophospholipids, cholesterol, and fatty acids, we performed mRNA expression profiling of all currently known ABC molecules during in vitro differentiation of human keratinocytes and HaCaT cells. We identified six ABC molecules that displayed significant regulation during differentiation of these cells. The recently cloned transporter ABCA7 was highly expressed in keratinocytes and HaCaT cells and upregulated during differentiation. Overexpression of ABCA7 in HeLa cells resulted in increased expression of intracellular and cell surface ceramide and elevated intracellular phosphatidylserine levels. Given the observation that during terminal keratinocyte differentiation intracellular and surface ceramide levels are increased, our results render ABCA7 a candidate regulator of ceramide transport in this process. In addition to ABCA7, the cholesterol transporters ABCB1 and ABCG1 and the glutathione/glucuronide sulfate transporters ABCC1, ABCC3, and ABCC4, were strongly upregulated during keratinocyte and HaCaT cell differentiation. These findings support the notion that ABCB1 and ABCG1 are potentially implicated in cholesterol transport, whereas ABCC1, ABCC3, and ABCC4 are candidate regulators of the translocation of sulfated lipids during stratum corneum keratinization. Our results suggest specific biologic functions for members of the ABC transporter family in epidermal lipid reorganization during terminal keratinocyte differentiation.

ATP-Binding Cassette Transporters↗
PubMed1995

Homology of a bovine allergen and the oligomycin sensitivity-conferring protein of the mitochondrial adenosine triphosphate synthase complex.

We have characterized bovine allergens by constructing and analyzing a complementary DNA library from bovine skin. Clones producing proteins that reacted with IgE antibodies from persons with allergy were purified and sequenced. One set of the allergen-coding clones showed an almost complete homology with the bovine oligomycin sensitivity-conferring protein of the mitochondrial adenosine triphosphate synthase complex. The IgE antibodies adsorbed with the recombinant allergen reacted with an 11 kd protein in the cow dander extract. Binding of the IgE from patients allergic to the recombinant allergen expressed in Escherichia coli confirmed the allergen-coding ability of the complementary DNA sequence. The prevalence of the IgE-positive sera among patients with cow allergy and control subjects suggests that the recombinant allergen represents one of the minor allergens in cow dander. This is the first time a mammalian allergen has been identified as a protein with a known function.

Adenosine Triphosphatases↗
PubMed2004

Characteristics of adenosine triphosphate [corrected] release from porcine and human normal bladder.

PURPOSE: Although the sensory and motor roles of the purinergic system in the bladder are well proven in animal species, there is increasing evidence that it may have an important role in humans. In addition, it may be important in the pathophysiology of bladder dysfunction. We established the level of adenosine triphosphate (ATP) release from porcine and normal human bladders. MATERIALS AND METHODS: Bladder strips from patients with a urodynamically proven stable bladder undergoing surgery for stress incontinence and those undergoing cystectomy for cancer with no lower urinary tract symptoms were subjected to varying degrees of stretch (up to 50%) and electric field stimulation (10 to 40 Hz). A luciferase assay was used to quantify ATP release. RESULTS: Significantly increased ATP release over baseline was induced by mechanical and electrical stimulation (each p <0.05). Mean ATP release +/- SE from porcine bladders (38.2 +/- 1.9 pM/gm tissue following stretch and 19.9 +/- 6.5 pM/gm following electrical stimulation) was comparable to the release from human bladders (26.1 +/- 2.4 pM/gm tissue following stretch and 29.9 +/- 1.0 pM/gm following electrical stimulation). The main source of ATP release was the urothelium and not the muscle (p <0.05). This ATP release following stretch was not tetrodotoxin sensitive. CONCLUSIONS: The characteristics of ATP release from porcine and human bladders are similar and, therefore, the pig is a good model for humans. The main source of ATP release is urothelium from predominantly nonneuronal sources. This study supports a sensory role for ATP. An increased role for this purinergic neurotransmission may result in functional motor as well as sensory bladder disorders.

Adenosine Triphosphatases↗
PubMed1985

Rapid methods for counting mycobacteria--comparison of methods for extraction of mycobacterial adenosine triphosphate (ATP) determined by firefly luciferase assay.

A comparison of 5 different methods of extraction of adenosine 5'-triphosphate (ATP) from mycobacterial cells was carried out using Mycobacterium bovis, BCG as a model. ATP was measured using the luciferin-luciferase bioluminescence reaction. Boiling buffer extraction was the best method. The amount of ATP extracted correlated with the number of colony forming units over a wide range of count. Although great sensitivity in terms of number of bacilli detectable was not achieved the method was rapid and appears suitable for drug sensitivity testing of tubercle bacilli.

Adenosine Triphosphate↗