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Biomedical subjects

G Andria

Publications and source records attributed to G Andria.

At least 127 records · Page 7Linked to original sources
PubMed1979

A two-year-old patient with an atypical expression of GM1-beta-galactosidase deficiency: biochemical, immunological, and cell genetic studies.

Cultured skin fibroblasts from a 2-year-old boy with an atypical form of beta-galactosidase deficiency have been studied. With the artificial substrate 4-methylumbelliferyl-beta-D-galactopyranoside, 5--15% residual activity was found in fibroblasts from this patient. Most of this activity was in the monomeric A form of the enzyme, very little in the multimeric B form. Km value, pH profile, and heat lability of the mutant enzyme were similar to those of beta-galactosidase from control fibroblasts. Immunological studies showed that the mutant enzyme cross-reacted with an antiserum raised against human liver beta-galactosidase, but the catalytic activity per unit antigenic activity was lower than normal. It was demonstrated by somatic cell hybridization that the gene mutation in this patient is different from that in patients with type 1 or type 2 GM1-gangliosidosis. No genetic complementation was found after fusion of fibroblasts from this patient with those from two other clinical variants of GM1-gangliosidosis formerly designated type 3 and adult type 4.

Cells, Cultured↗
PubMed1979

Sanfilippo B syndrome (MPS III B): mild and severe forms within the same sibship.

Clinical heterogeneity for Sanfilippo B syndrome (MPS III B) in the same family has never been reported previously. We describe two clinically severe cases and one clinically mild case of MPS III B in a Neapolitan sibship. We could not detect N-acetyl-alpha-D-glucosaminidase activity in the sera of either the severe or mild cases. Mucopolysacchariduria mainly due to heparan sulfate excretion was consistently high in the severely affected patients and extremely variable in the mildly affected one.

Abnormalities, Multiple↗
PubMed1978

Atypical expression of beta-galactosidase deficiency in a child with Hurler-like features but without neurological abnormalities.

A 28-month-old child was found to have several clinical features of lysosomal storage diseases, including: coarse facies, hepatosplenomegaly, lumbar kyphosis due to hypoplastic beaked L1 and L2 vertebral bodies, vacuolated lymphocytes in blood smears and rare foamy hystiocytes in bone marrow. However, no signs of neurological or ocular abnormalities were detected. A beta-galactosidase deficiency was demonstrated in leukocytes and cultured skin fibroblasts, with a residual activity toward 4-methylumbelliferyl-beta-galactopyranoside ranging between 5 and 15% of the normal mean. Normal activities were found for several other lysosomal acid hydrolases. beta-Galactosidase activities in leukocytes and cultured skin fibroblasts from both parents were within the normal ranges. The patient seems to represent an atypical expression of acid beta-galactosidase deficiency, since his clinical picture does not exaclty correspond to that of either the two classical types of GM1-gangliosidosis or other atypical patients reported in the literature havining beta-galactosidase deficiency.

Eye Abnormalities↗
PubMed1977

Brush border peptidases and arylamidases in the experimental blind loop syndrome of the rat.

Peptidase and arylamidase activities were assessed in purified brush borders from jejunum of rats with surgically created blind loops. The blind loop segment and the jejunum proximal and distal to the blind loop were studied. Comparable jejunal segments from control rats were also studied. The blind loop syndrome was documented by presence of macrocytic anemia. Enzyme activities were determined on purified brush borders. In rats with the blind loop syndromes enzymatic activities hydrolizing sucrose, L-Leucyl-beta-naphthylamide, L-lysyl-beta-naphthylamide, alpha-L-glutamyl-beta-naphthylamide, L-phenylalanyl-alanine and L-leucyl-glycine were significantly reduced as compared to controls (P less than 0.001). After a short course of antibiotic therapy enzymatic activities returned to normal. Our findings suggest a reversible intestinal mucosa damage in the rat with blind loop syndrome.

Aminopeptidases↗
PubMed1976

Partial monosomy 22 as the result of an unbalanced translocation 5:22 in a patient with cri-du-chat syndrome.

A 2-year-old boy with features suggestive of cri-du-chat syndrome had a complex karyotype: 45,XY,--22,5p--,t(5p:22q). Clinical symptoms were catlike cry in early infancy, severe mental and motor retardation, failure to thrive, hypertelorism, antimongoloid slant of the eyes, ptosis of the eyelids, epicanthus, micrognathia, dermatoglyphics abnormalities, and partial syndactyly between 2nd and 3rd toes.

Aneuploidy↗
PubMed1976

Alpha-Glutamyl-beta-naphthylamide hydrolase of rabbit small intestine. Localization in the brush border and separation from other brush border peptidases.

About 70% of the total mucosal enzymatic activity hydrolyzing beta-L-glutamyl-beta-naphthylamide in the rabbit small intestine is present in the brush border; the specific activity in this subcellular fraction is 7 times higher than that of the homogenate. Similar results are obtained for L-leucyl beta-naphthylamide hydrolase. The enzyme activity is efficiently solubilized by papain digestion and is clearly separated from L-leucyl-beta-naphthylamide hydrolase by chromatography on concanavalin A-Sepharose. It probably represents a digestive peptidase, different from the other known peptide hydrolases of the digestive surface of the small intestine.

Aminopeptidases↗
PubMedDate not supplied

Genetic homogeneity of lysinuric protein intolerance.

Lysinuric protein intolerance (LPI) is an autosomal recessive disorder in which transport of the cationic amino acids lysine, arginine and ornithine is defective at the basolateral membrane of the epithelial cells in the intestine and renal tubules. LPI is unusually common in Finland, but patients have been described on all continents. Linkage analysis in Finnish LPI families recently assigned the LPI gene locus to a 10 cM interval between markers D14S72 and MYH7 on the long arm of chromosome 14. In the present study linkage analysis of LPI families from six different non-Finnish populations strongly suggests genetic homogeneity in LPI. Peak lod scores were obtained at the chromosomal area between D14S72 and MYH7 with the same markers as in the Finnish families. The non-Finnish families showed no linkage disequilibrium except in an Italian family cluster, whereas strong allelic association in the Finnish families implies that LPI in Finland is caused by a founder mutation.

Amino Acid Metabolism, Inborn Errors↗