ABSTRACT
A young woman patient had early and extensive familial Mediterranean fever (FMF)-related amyloidosis and pseudoxanthoma elasticum (PXE). She had the novel G1042S mutation in the ATP-binding cassette subfamily C member 6 (ABCC6) gene, responsible for PXE, and the mutation M694I in MEFV, the FMF gene. Both mutations were homozygous, in agreement with consanguinity in the parents. ABCC6 deficiency may have increased the severity of amyloidosis by increasing the deposition in target tissues of heparan sulphate, which colocalizes spatially and temporally with amyloid proteins, and/or by decreasing the therapeutic activity of colchicine.
Subject(s)
Amyloidosis/etiology , Familial Mediterranean Fever/complications , Pseudoxanthoma Elasticum/complications , ATP-Binding Cassette Transporters/genetics , Adult , Amino Acid Sequence , Amyloidosis/genetics , Amyloidosis/pathology , Familial Mediterranean Fever/genetics , Female , Humans , Molecular Sequence Data , Multidrug Resistance-Associated Proteins/genetics , Mutation , Pseudoxanthoma Elasticum/genetics , Pseudoxanthoma Elasticum/pathology , Sequence AlignmentABSTRACT
Polar properties of latex particles containing specific groups with various surface charge densities were examined from contact angle measurements using "old" polar/dispersive models. It was determined that the Fowkes approach is quite sufficient for classifying our functionalized polystyrene latices. The pertinence to our systems of the acid-base approach, which has a more pronounced chemical background, was then investigated, and the strong dependence of the acid-base parameters (gamma plus sign in circle, gammaTheta) on the acid-base scale chosen for the reference liquid (water) was shown. Finally, using the receding angle values revealed the outermost surface buried moieties in the latex particles, which were not seen in the advancing angle measurements. Copyright 1998 Academic Press.
