Search PubMed⌕ Search

Biomedical subjects

P Aula

Publications and source records attributed to P Aula.

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

"Salla disease": a new lysosomal storage disorder.

Severe mental retardation, coarse facial features, clumsiness, and speech failure were common findings in three brothers and one female third-cousin of a family from northern Finland. All the patients had vacuolated lymphocytes in peripheral blood smears, and electron microscopy of fresh skin biopsy specimens showed abundant cytoplasmic inclusions in various types of cells of the skin. Eight lysosomal hydrolases were assayed in peripheral blood lymphocytes and cultured skin fibroblasts, but no enzyme deficiency was detected. Urinary excretion of mucopolysaccharides, amino acids, glycoasparagines, and oligosaccharides was normal. Clinical findings, course of the disease, and the presence of cytoplasmic inclusions, indicating lysosomal storage phenomenon, suggest that the patients suffer from a genetic lysosomal storage disorder not described earlier. The eponym "Salla disease" was introduced, referring to the geographically restricted area where the family resides.

Adult↗
PubMed1978

Prenatal diagnosis of congenital nephrosis in 23 high-risk families.

The efficacy of maternal serum and amniotic fluid alpha-fetoprotein (AFP) estimation for the prenatal detection of congenital nephrosis was assessed in 23 pregnancies of couples with a previously affected child. At 15 to 18 weeks' gestation, amniotic fluid AFP concentration was elevated in seven of 23 cases, and maternal serum AFP level in five of these. Legal abortion was carried out at 18 to 19 weeks in all those cases where he amniotic fluid AFP concentration was abnormally high, and in all cases the fetus was found to be affected. The diagnosis of intrauterine congenital nephrosis was obvious by electron microscopic examination of the fetal kidney, but not by light microscopy. The child was born without congenital nephrosis in all 16 cases where amniotic fluid AFP level was normal, and in 16 of 18 cases (89%) where maternal serum AFP concentration was normal. Thus, the amniotic fluid AFP assay is more reliable and is recommended whenever congenital nephrosis is suspected on the basis of family history.

Abortion, Legal↗
PubMed1978

Incomplete prenatal diagnosis of G-trisomy mosaicism.

Chromosomal mosaicism is difficult to detect in prenatal diagnosis, and it seems even more difficult to predict its significance correctly. We present a case, in which G-trisomy mosaicism was diagnosed prenatally but was not verified in the aborted fetus. A practical approach to suspected fetal mosaicism in prenatal diagnosis is proposed.

Adult↗
PubMed1977

Structure of two glycoasparagines isolated from the urine of patients with aspartylglycosylaminuria (AGU).

The structures of two glycoasparagines composed of one mole each of N-acetylneuraminic acid, galactose, N-acetylglucosamine, and asparagine were determined by periodate oxidation, enzymatic degradation, and methylation analysis. The structures were NANAalpha2 leads to 3Galbeta1 leads to 4GlcNAcbeta leads to Asn and NANAalpha2 leads to 6Galbeta1 leads to 4GlcNAcbeta leads to Asn, respectively.

Asparagine↗
PubMed1977

Morphology of the placenta in fetal I-cell disease.

Placentas were studied from three interrupted pregnancies of a mother whose first liveborn child had I-cell disease (mucolipidosis II). I-cell disease of the fetus was shown by investigation of the amniotic fluid, fetal cells and the aborted fetus in two pregnancies, but in the third case placenta was the only available product of conception. In every placenta extensive vacuolization of the syncytiotrophoblastic layer of the chorionic villi and chorionic mesenchymal cells was found. In electron microscopy the inclusions were identical to those of other tissues in I-cell disease. The importance of histological study of placenta in unexplained spontaneous abortions needs to be emphasized, since this may be the only way of detecing new cases of lysosomal storage diseases.

Abortion, Habitual↗
PubMed1976

Congenital nephrotic syndrome: prenatal diagnosis and genetic counselling by estimation of aminotic-fluid and maternal serum alpha-fetoprotein.

Nine families in which a previous child had had congenital nephrotic syndrome (C.N.) sought genetic counselling and possible antenatal diagnosis of fetal disease. Maternal serum and amniotic-fluid alpha-fetoprotein (A.F.P.) assays were carried out between the 15th and 20th weeks of subsequent pregnancies. Seven women in whom A.F.P. concentrations were normal chose to continue pregnancy, and they were all delivered of a healthy child. Markedly raised amniotic A.F.P. concentrations were found in two cases; in one of these cases maternal serum-A.F.P. was also raised. These pregnancies were terminated, and electron microscopy of the fetal kidneys showed evidence of C.N. in the fetus--i.e., loss of foot processes and an increase in the mesangial matrix of the glomeruli. The outcomes of these at-risk pregnancies indicate that prenatal diagnosis and genetic counselling are possible in families with a history of C.N. The results also stress the importance of carefully examining fetal kidneys whenever amniotic-fluid A.F.P. concentration is raised in the absence of apparent malformations.

Amniotic Fluid↗
PubMed1976

Distribution of spontaneous chromosome breaks in human chromosomes.

Localization of chromosome breaks in human chromosomes was analyzed in 264 peripheral lymphocyte cultures. Three hundred and sixty-nine chromosome breaks could be exactly localized to a chromosome band or region of the Paris Conference nomenclature. The distribution of breaks in the chromosome regions was found to be nonrandom. Chromosome 3 alone had 23% of the breaks and region 3p2 had 13% of the total breaks. Some other chromosome regions, such as 5p1, 9q1, 14q2, and 16q2 also displayed clustering of breaks. Sex chromosomes had less breaks than expected. Spontaneous chromosome breaks were almost exclusively located in the lightly stained G bands.

Chromosome Aberrations↗
PubMed1976

Enzymatic diagnosis and carrier detection of aspartylglucosaminuria using blood samples.

The activity of the glycoprotein degrading lysosomal hydrolase, 4-L-aspartylglycosylamine amido hydrolase (AAD Gase, EC.3.5.1.26), was measured in plasma, buffy coat leukocytes, and separated lymphocytes (Ficoll separation) from 16 patients with aspartylglucosaminuria (AGU), 29 obligate heterozygotes, and 30 control subjects. In lymphocytes the AGU patients had unmeasurable or minimal AAD Gase activity with a mean of 3.9 U. The obligate heterozygotes showed AAD Gase activities ranging from 5 to 69 U with a mean of 34.1 U. Enzyme activities in the control group ranged from 91 to 243 U with a mean of 127.9 U, and were clearly separated from the values of the heterozygotes. In leukocytes the AGU patients had unmeasurable enzyme activity and obligate heterozygotes had enzyme levels closely similar to those in the lymphocytes from the same individuals. The AAD Gase activity in the leukocytes of the control group displayed a much wider variation than in the lymphocytes, ranging from 22 to 132 U with a mean of 70.7 U. In plasma the AGU patients had undetectable AAD Gase activity. The mean enzyme level of obligate heterozygotes was 72.2 U and that of control individuals 107.2 U, but the overlap between the groups was extensive. The results indicate that homozygous deficiency of AAD Gase, i.e., aspartylglucosaminuria can be reliably diagnosed using plasma, leukocytes, or separated lymphocytes. For carrier detection only separated lymphocytes allow a satisfactory differentiation between heterozygous and normal individuals. A group of 31 siblings of verified AGU cases and 11 children of identified carriers, whose spouses had normal AAD Gase activity, were investigated using the lymphocyte assay. The observed and expected frequencies (on the basis of Mendelian probabilities) were closely similar, suggesting that the lymphocyte assay can be used reliably for carrier detection.

Acetylglucosaminidase↗