Why Aspirin (as an antipyratic) is contra-indicated in dengue ???

Dengue fever is transmitted by female Aedes Aegypti mosquitoes which acquire the virus while feeding on the blood of an infected person.Dengue occurs in two forms: Dengue fever and dengue haemorrhagic fever.
Dengue fever is marked by the onset of sudden high fever, severe headache and pain behind the eyes, muscles and joints.According to the World Health Organisation, dengue haemorrhagic fever is a potentially deadly complication that is characterised by high fever, often with enlargement of the liver and, in severe cases, circulatory failure.There is no specific treatment for dengue fever but early recognition and symptomatic treatment can save lives.
Use of aspirin during dengue fever is not recommended owing to increased bleeding tendency.Aspirin has an antiplatelet effect by inhibiting the production of thromboxane, which under normal circumstances binds platelet molecules together to create a patch over damage of the walls within blood vessels.

Difference between diclofenac sod. and potessium salt ......

Dilcofenic is a relatively potent NSAID. It is a phenylacetic or benzeneacetic acid derivative with the chemically designation 2-(2,6-dichlorophenyl)amino phenylacetic acid or benzeneacetic acid, monosodium or monopotassium salt. Diclofenac sodium was first synthesised by Ciba-Geigy of Switzerland in 1965 and was launched as Voltaren in 1988.

The sodium salt and potassium salt of diclofenac used are biologically equivalent, with both being protonated by the acid in the stomach. One difference is that diclofenac potassium is slightly more soluble in water than diclofenac sodium.

source-www.drugs.com, www.assistpainrelief.com

How insulin and proinsulin are safe in lysosomal cavity,where they store normally

Insulin is thought to be chemically stabilized within -granules in the crystal form. The other major products of the -granule, proinsulin and C-peptide, by contrast, are not thought able to crystallize. The physico-chemical properties of peptides in soluble or crystalline form are dramatically different. The ability of insulin to crystallize in the -granule might thus explain why this peptide, but not proinsulin/Cpeptide, remains stable even after its introduction into lysosomes as occurs during granulolysis (crinophagy). We have now studied this by exposing proinsulin or insulin to lysosomal proteases in vitro. 125I-insulin in soluble form was found to be degraded at the same rate as 125I-proinsulin. Strikingly, however, when the labelled insulin was crystallized, its rate of degradation was decreased from 1.9 to 0.2 pmol/min. We take these data as confirmation that the insulin crystal is resistant to degradation, thereby possibly accounting for (a) the presence of insulin immunoreactivity within multigranular bodies, and (b) the unusually slow rate of degradation of insulin within B cells compared with that of other hormones in their cells of origin.

source of information
1.Resistance of the insulin crystal to lysosomal proteases: implications for pancreatic B-cell crinophagy
P. A. Halban, R. Mutkoski, G. Dodson and L. Orci