ABSTRACT
No abstract available.
Subject(s)
Humans , Basophils/cytology , Flow Cytometry , HLA-DR Antigens/metabolism , Interleukin-3 Receptor alpha Subunit/metabolism , Leukocyte Count , Phosphoric Diester Hydrolases/metabolism , Pyrophosphatases/metabolism , Receptors, CCR3/metabolism , Urticaria/diagnosisABSTRACT
Background: Sudden cardiac death (SCD) is a sudden unexpected event, from a cardiac cause, that occurs in less than one hour after the symptoms onset, in a person without any previous condition that would seem fatal or who was seen without any symptoms 24 hours before found dead. Although it is a relatively frequent event, there are only few reliable data in underdeveloped countries. Objective: We aimed to describe the features of SCD in Ribeirão Preto, Brazil (600,000 residents) according to Coroners’ Office autopsy reports. Methods: We retrospectively reviewed 4501 autopsy reports between 2006 and 2010, to identify cases of SCD. Specific cause of death as well as demographic information, date, location and time of the event, comorbidities and whether cardiopulmonary resuscitation (CPR) was attempted were collected. Results: We identified 899 cases of SCD (20%); the rate was 30/100000 residents per year. The vast majority of cases of SCD involved a coronary artery disease (CAD) (64%) and occurred in men (67%), between the 6th and the 7th decades of life. Most events occurred during the morning in the home setting (53.3%) and CPR was attempted in almost half of victims (49.7%). The most prevalent comorbidity was systemic hypertension (57.3%). Chagas’ disease was present in 49 cases (5.5%). Conclusion: The majority of victims of SCD were men, in their sixties and seventies and the main cause of death was CAD. Chagas’ disease, an important public health problem in Latin America, was found in about 5.5% of the cases. .
Fundamento: Morte súbita cardíaca (MSC) é um evento súbito e inesperado, de causa cardiovascular, que ocorre em menos de uma hora após o início dos sintomas, em indivíduo sem qualquer condição clínica prévia potencialmente fatal ou assintomático nas últimas 24 horas antes do óbito, em caso de morte não testemunhada. Apesar de ser um evento relativamente frequente, há poucos dados confiáveis na literatura sobre países em desenvolvimento. Objetivo: Descrever as características da MSC em Ribeirão Preto (SP 600.000 habitantes) baseando-se nos relatórios de autopsias do Serviço de Verificação de Óbitos do Interior. Métodos: Foram revisados retrospectivamente 4.501 relatórios de autopsias entre 2006 e 2010, para identificar casos de MSC. Foram coletados dados como causa específica do óbito, características demográficas e comorbidades das vítimas, data, local e hora do evento, e se foram realizadas manobras de ressuscitação cardiopulmonar (RCP). Resultados: Foram identificados 899 casos de MSC (20%; razão 30/100.000 habitantes por ano). A principal causa de MSC foi doença arterial coronariana (DAC - 64%), acometendo homens (67%) entre a sexta e a sétima década de vida. A maior parte dos eventos ocorreu durante a manhã, no domicílio (53,3%), e a RCP foi realizada em quase metade das vítimas (49,7%). A comorbidade mais prevalente foi hipertensão arterial sistêmica (57,3%). Doença de Chagas foi detectada em 49 casos (5,5%). Conclusão: A maioria dos casos de MSC ocorreu por DAC em homens entre a sexta e a sétima década de vida. Doença de Chagas, um importante problema de saúde pública na América Latina, foi detectada em 5,5% dos casos. .
Subject(s)
Humans , Drug Evaluation, Preclinical/methods , Enzyme Inhibitors/pharmacology , Oligonucleotides/metabolism , Phosphoric Diester Hydrolases/metabolism , Spectrometry, Fluorescence/methods , Base Sequence , Cost-Benefit Analysis , Drug Evaluation, Preclinical/economics , High-Throughput Screening Assays , Kinetics , Mutation , Oligonucleotides/genetics , Phosphoric Diester Hydrolases/genetics , Spectrometry, Fluorescence/economicsABSTRACT
El presente trabajo involucra el estudio del sistema purinérgico mediante la purinérgico mediante la purificación y la caracterización bioquimica de la ecto-enzima E-NPP3 soluble, la cual modula la activación de los receptores purinérgicos mediante la hidrólisis de los nucleótidos extracelulares. La purificación de esta enzima, expresada en la línea celular CHO-K1, requirió el empleo de diferentes columnas cromatográficas; comprobándose la pureza, mediante la determinación de la actividad enzimática, la cuantificación de las proteínas y la detección de dicha enzima. Los resultados de la caracterización de la E-NPP3 indican que presentan un ph óptimo alcalino y que su actividad depende de la la concentración de los iones calcio y magnesio: mientras que el imidazol y el DDT ejercen acciones inhibidoras sobre su actividad. La purificación de la enzima E-NPP3 soluble representa un primer paso para futuros estudios que permitan su cristalización lo cual, constituirá una herramienta en la elaboración de agonistas y antagonistas selectivos o de anticuerpos monoclonales contra dicha enzima, útiles en el diagnóstico o el tratamiento de condiciones patológicas como el cáncer de colon y la colangiocarcinoma. Adicionalmente, teniendo en cuenta que se ha demostrado la disminución de la expresión de las ecto-nucleotidasas en el uroepitelio de pacientes que padecen cistitis intersticial; el presente trabajo comprende también, el desarrollo de un modelo de órgano aislado, la vejiga urinaria del ratón, para el estudio de la secreción de ATP desde las células uroepiteliales. Dicho modelo permitió demostrar, mediante estudios electrofisiológicos y el uso de diferentes fármacos, la contriución de los receptores purinérgicos sobre la actividad eléctrica del nervio pélvico cuando la vejiga es sometida a distensión mecánica gradual; sugiriendo la importancia de estos receptores en la transducción mecanosensorial de dicho órgano y permitiendo inferir la posible interrelación con los receptores de vaniloides en la detección de los estímulos sensoriales por parte del uroepitelio
Subject(s)
Animals , Mice , Pyrophosphatases/metabolism , Urinary Bladder/cytology , Adenosine Triphosphate/metabolism , Receptors, Purinergic/metabolism , Phosphoric Diester Hydrolases/metabolism , Epithelial Cells/metabolism , Pyrophosphatases/chemistry , Cell Line , Receptors, Purinergic/chemistry , Cholangiocarcinoma/diagnosis , Phosphoric Diester Hydrolases/chemistry , Cystitis, Interstitial/enzymology , Models, Animal , DDT/adverse effectsABSTRACT
Glycerophosphrylocholine (GPC) is a renal medullary compatible organic osmolyte that is derived from choline via phosphatidylcholine, which is catalyzed in part by phospholipase A2 (PLA2) and its degradation by GPC: choline phosphodiesterase (GPC: choline PDE). We found that caffeine elevated intracellular free calcium ([Ca2+]i) and GPC level in cultured MDCK cells, canine kidney epithelial cells, and propose a possible biochemical mechanism. When MDCK cells were incubated for 3 h with 1 to 10 mM caffeine, cellular GPC was elevated in a dose-dependent manner, and this occurred independently of the extracellular osmolality. Caffeine stimulated the rate of [14C]choline incorporation into [14C]GPC and PLA2 activity. Whereas, GPC: choline PDE activity was accompanied by less of increase. These enzyme changes demonstrate the increased net synthesis of MDCK GPC. In order to identify what triggers the PLA2 activation, [Ca2+]i was measured by using a fluorescence dye, Fura-2. Caffeine (10 mM) resulted in a typical transient increase in MDCK [Ca2+]i concentration, and this increase was greatly inhibited by pretreatment of MDCK cells with 10 mM ryanodine for 5 min. Ryanodine (10 mM) also inhibited the caffeine-induced stimulation of PLA2 activity. These findings provide the first evidence that caffeine in MDCK cells causes a ryanodine-inhibitable increase of [Ca2+]i and PLA2 activity, resulting in cellular GPC accumulation.
Subject(s)
Dogs , Animals , Caffeine/pharmacology , Calcium/metabolism , Carbon Radioisotopes , Cell Line , Choline/metabolism , Glycerylphosphorylcholine/metabolism , Kidney/cytology , Phospholipases A/metabolism , Phospholipases A/drug effects , Phospholipases A/antagonists & inhibitors , Phosphoric Diester Hydrolases/metabolism , Phosphoric Diester Hydrolases/drug effects , Ryanodine/pharmacology , Ryanodine/metabolismABSTRACT
Muscle ATPase activity did not show much change with any of the treatments, while hepatic total and Ca(2+)-Mg(2+)-ATPase activities were decreased with low dose of dexamethasone (DXM(L) and enzyme activity in general was increased with both high dose of DXM(H) and corticosterone. Total and Ca(2+)-Mg(2+)-ATPases were increased in testis of corticosterone treated chicks. Acid phosphatase activity of testis was increased with DXM(H) and decreased with DXM(L) while the enzyme activity in all the three tissues was increased with corticosterone. Muscle alkaline phosphatase activity was decreased with DXM treatments while that of testis was decreased with both DXM(H) and corticosterone treatments. Hepatic PDE activity was decreased with DXM and increased with corticosterone while muscle PDE activity was decreased under both DXM(H) and corticosterone treatments. The results suggest that both hypo. and hypercorticalism can induce tissue specific differential alterations in phosphomonoesterases, ATPases and PDE during early phases of post-natal development of chicks.
Subject(s)
Adenosine Triphosphatases/metabolism , Animals , Chickens , Corticosterone/pharmacology , Dexamethasone/pharmacology , Glucocorticoids/pharmacology , Liver/drug effects , Male , Muscle, Skeletal/drug effects , Phosphoric Diester Hydrolases/metabolism , Phosphoric Monoester Hydrolases/metabolism , Testis/drug effectsABSTRACT
Calmodulin-like activity has been reported for the first time in mycobacterial species, namely Mycobacterium tuberculosis BCG and M. smegmatis ATCC 14468. The activity was mainly located in the soluble fraction of the mycobacterial cells, Radioimmunoassay revealed maximum levels of calmodulin in young growing cells (early logarithmic phase of growth). Calmodulin-dependent phosphodiesterase activation assay revealed low activity (22%) of partially purified calmodulin either due to insufficient amount of calmodulin to activate phosphodiesterase or due to the presence of some factors interfering with the assay. Calmodulin antagonists, viz. trifluoperazine and phenothiazine, significantly inhibited the 32Pi incorporation into mycobacterial phospholipids. Similar inhibition was observed when EGTA (which removes calcium) was added to the medium. Significant inhibition of 32Pi incorporation in the presence of calmodulin antagonists suggested the involvement of calmodulin in mycobacterial phospholipid metabolism.
Subject(s)
Calmodulin/antagonists & inhibitors , Cyclic Nucleotide Phosphodiesterases, Type 1 , Mycobacterium/metabolism , Mycobacterium tuberculosis/metabolism , Phosphoric Diester Hydrolases/metabolism , Trifluoperazine/pharmacologyABSTRACT
Goat sperm lysate from cauda epididymis was incubated in the presence of [14C]phosphatidyl-choline, -ethanolamine, -inositol and diphosphatidyl-glycerol. The release of [14C]diacylglycerol from only phosphatidyl inositol confirmed the presence of phosphatidyl inositol specific phospholipase C. The enzyme activity was linear up to 1 hr of incubation at a sperm concentration of 1-10 x 10(9). It had pH optimum of 7.5 in a broad range of pH activity profile (pH 6-9). Maximum activity was observed at 8 mM calcium ion concentration. EDTA and EGTA (5 mM) did not inhibit the activity completely. A comparative study on spermatozoa and fluid from caput, corpus and cauda epididymis revealed 6.5-fold increase of activity in spermatozoa and a 4-fold decrease in case of fluid during the epididymal transit. However, the total protein content remained unchanged in fluid and decreased up to the extent of 2.4-fold in spermatozoa during this process. Thirty five percent of the caudal sperm activity was soluble and the rest was associated with head (44%), mid-piece (10%) and tail (10%).
Subject(s)
Animals , Epididymis , Goats , Male , Phosphatidylinositol Diacylglycerol-Lyase , Phosphoric Diester Hydrolases/metabolism , Sperm Transport , Spermatozoa/enzymologyABSTRACT
Se presenta una revisión sobre la función de la Poli (ADP-ribosa) sintetasa, enzima nuclear que sintetiza monómeros y polímeros a ADP-ribosas a partir de NAD+, mecanismo denominado polirribosilación. Estas moléculas sintetizadas son unidas covalentemente a proteínas, básicamente histonas, modificando, por ende su funcionalidad. Asímismo, se describen actividades enzimáticas que degradan ADP-ribosas. Se plantean también, los roles que el proceso de polirribosilación, podría modular en el núcleo eucariótico
Subject(s)
Humans , Enzyme Activation/physiology , ADP Ribose Transferases/physiology , Eukaryotic Cells/enzymology , Phosphoric Diester Hydrolases/metabolism , Hydrolysis , NAD/metabolism , Proteins/metabolismABSTRACT
Imidazole, a phosphodiesterase stimulator potentiated the responses of rat uterus to 5-HT, without increasing the maximal response. Aminophylline, papaverine and diazoxide significantly inhibited the responses to 5-HT including the maximal response. Imidazole did not affect the inhibitory effect of aminophylline, papaverine and diazoxide. The effect of imidazole on myometrium may be due to its direct effect on membrane permeability resulting in an increased influx of calcium. Phosphodiesterase stimulation if at all seems to play only a minor role.