Attenuation of Benzanthrone Toxicity by Ascorbic Acid in Guinea Pigs

1994 ◽  
Vol 22 (3) ◽  
pp. 447-456 ◽  
Author(s):  
M Das
Keyword(s):  
Author(s):  
Marija Bursać-Mitrović ◽  
Dragan R. Milovanović ◽  
Radoslav Mitić ◽  
Danijela Jovanović ◽  
Miroslav Sovrlić ◽  
...  

1977 ◽  
Vol 107 (8) ◽  
pp. 1513-1516 ◽  
Author(s):  
Prakash G. Shilotri
Keyword(s):  

1997 ◽  
Vol 11 (2) ◽  
pp. 134
Author(s):  
Maria Cecília Bueno Jayme Gallani ◽  
José Roberto Moreira Azevedo ◽  
Marilia Mantovani Sampaio Barros ◽  
Rui Errerias Maciel

O presente estudo objetivou avaliar em cobaias (“Cavia porcellus”), fêmeas, com três meses de idade, sedentárias (SED) e treinadas (TRE = natação, 30 min/dia, durante sete semanas) o comportamento da concentração tecidual de histamina muscular e cardíaca, em resposta ao exercício agudo (E = exercício agudo - natação, 30 minutos, R = repouso) e à suplementação de ácido ascórbico (SU = suplementados - 35 mg/kg de peso, NS = não suplementados). Foram constatadas as seguintes diferenças significativas (p < 0,05): a) no grupo sedentário, aumento da histamina muscular e cardíaca tanto nos subgrupos não suplementados como nos suplementados, o mesmo ocorrendo entre os animais treinados-exercitados agudamente somente naqueles suplementados; b) menor aumento de histamina muscular nos animais treinados - não suplementados - exercitados agudamente quando comparados a seus respectivos controles e de histamina cardíaca nos animais sedentários - suplementados - exercitados agudamente, quando comparados aos não suplementados, na mesma condição, e c) diminuição da histamina cardíaca nos animais sedentários, em repouso e suplementados


1938 ◽  
Vol 63 (1) ◽  
pp. 71-76 ◽  
Author(s):  
S. Raffel ◽  
R. R. Madison
Keyword(s):  

1970 ◽  
Vol 119 (3) ◽  
pp. 575-585 ◽  
Author(s):  
M. J. Barnes ◽  
B. J. Constable ◽  
L. F. Morton ◽  
E. Kodicek

1. After the administration of l-[G-3H]proline to guinea pigs deprived of ascorbic acid for increasing periods of time, the specific radioactivities of proline and hydroxyproline in skin collagen and aortic elastin were determined at various time-intervals after administration of the labelled compound with a view to studying the formation and degradation of collagen and elastin both deficient in hydroxyproline. 2. As judged from the incorporation of radioactivity into elastin proline, elastin synthesis was not decreased in the ascorbic acid-deficient animals. There was however, a rapid decline in the specific radioactivity of elastin hydroxyproline. The proline/hydroxyproline specific-radioactivity ratio was approx. 1.5:1 after 6 days and 20:1 after 12 days of ascorbic acid deprivation, in contrast with the ratio of 1:1 in controls. The results suggested that the effect of ascorbic acid deficiency on elastin biosynthesis could be regarded as simply an elimination of hydroxylation of elastin proline with the formation and retention of a polymer increasingly deficient in hydroxyproline. 3. Collagen proline and hydroxyproline specific radioactivities were derived from material that was soluble in hot trichloroacetic acid, non-diffusible and collagenase-degradable. In contrast with elastin, there was a rapid decline in the specific radioactivity of proline as well as hydroxyproline in collagen from the ascorbic acid-deficient animals. However, the proline/hydroxyproline specific-radioactivity ratio in all samples from scorbutic animals was consistently slightly above 1:1. The results suggest the appearance in place of collagen, but in rapidly diminishing amounts, of a partially hydroxylated collagen in which the degree of hydroxylation may be decreased only by approx. 10%. 4. Incorporation of radioactivity into the diffusible hydroxyproline in skin remained relatively high despite the rapid decline in the incorporation of radioactivity into collagen. This observation is interpreted as indicative of an increasing degree of degradation of partially hydroxylated collagen to diffusible peptides. An alternative explanation might be that partially hydroxylated peptides are released to an increasing extent from ribosomes before they attain a length at least sufficient to render them non-diffusible. In either case it implies the accumulation in scurvy of low-molecular-weight peptides enriched in proline and deficient in hydroxyproline and could explain the failure to accumulate a high-molecular-weight collagen deficient in hydroxyproline. 5. It is thought, however, that, in addition, an inhibition of ribosomal amino acid incorporation leading to decreased synthesis of partially hydroxylated collagen may also occur, perhaps secondarily to impaired hydroxylation.


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