The topical glucocorticoids (GCs) represent the treatment of choice for many types of inflammatory dermatoses. Despite the extensive use of this class of drugs as first line therapy the mechanism of their action is uncertain. It is clear that the multiplicity of actions of the topical GCs is an important facet of their scope in the treatment of dermal disorders. The aim of this update is to rev...

To assess the potential contribution of the cysteine-rich domain of human platelet glycoprotein (GP) IIIa to the structure of the PlA1 epitope, we used site-directed mutagenesis to substitute alanines for cysteines at key positions potentially involved in PlA1 alloantigen formation. One of these GPIIIa isoforms in which alanine replaced Cys435 reacted normally with a series of well-characterize...

BACKGROUND The PlA1/A2 polymorphism of glycoprotein IIIa (GPIIIa) has been reported to be associated with risk of stroke in some studies, although other studies suggest no such association. This meta-analysis and systematic review was conducted to investigate the hypothesis that carriage of the PlA2 allele is a risk factor for stroke. METHODS Electronic databases (MEDLINE and EMBASE) were sea...

Adenosine induces vasoconstriction of renal afferent arterioles through activation of A1 adenosine receptors (A1AR). A1AR are directly coupled to Gi/Go, resulting in inhibition of adenylate cyclase, but the contribution of this signaling pathway to smooth muscle cell activation is unclear. In perfused afferent arterioles from mouse kidney, adenosine and the A1 agonist N(6)-cyclohexyladenosine, ...

Fenton RA, Shea LG, Doddi C, Dobson JG, Jr. Myocardial adenosine A1-receptor-mediated adenoprotection involves phospholipase C, PKC-ε, and p38 MAPK, but not HSP27. Am J Physiol Heart Circ Physiol 298: H1671–H1678, 2010. First published April 2, 2010; doi:10.1152/ajpheart.01028.2009.—Adenosine via an adenosine A1 receptor (A1R) is a negative feedback inhibitor of adrenergic stimulation in the he...

the activity of phospholipase c in crude enzymatic preparation of melia azadiracht seeds (neem seeds) was studied by the use of lecithin as a substrate in aqueous medium. the enzyme activity was found optimum at ph 2.5 and temperature 35?c. the phospholipase c was found heat labile, being inactivated 88% within 10 minutes at 90°c