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Biomedical subjects

J Lisiewicz

Publications and source records attributed to J Lisiewicz.

At least 163 records · Page 9Linked to original sources
PubMed1976

Trace elements and immunologic defects. Zinc deficiency and activity of lysosomal acid phosphatase in lymphocyte of mice.

Activity of lysosomal acid phosphatase in peripheral blood lymphocytes of mice fed a low-Zn diet has been studied. The study comprised 40 CBA T6T6 mice, female, aged 8 weeks, with body weight equal to about 18.0 g. The animals were fed during 10 days with a low-Zn diet. This latter diet, as well as the control one contained 0.8 mg% and 11.4 mg% of zinc, respectively; potable water contained 0.06 mg% of this element. Activity of the enzyme was determined semiquantitatively using cytochemical method of Barka and Anderson. Peripheral blood lymphocytes in mice fed a low-Zn diet exhibited statistically significant lowering of the intracellular enzyme activity when compared with control groups. Absolute count of enzyme-positive lymphocytes was also significantly lowered. The Authors discuss the importance of their observations for evaluation of immune reactivity in trace-elements-deficient animals.

Acid Phosphatase↗
PubMed1976

N-acetyl-beta-glucosaminidase of lymphocytes in the premature infant with special reference to the fetal development of the lysosomas apparatus.

N-acetyl-beta-glucosaminidase activity was determined in peripheral blood lymphocytes by means of Hayashi's cytochemical method in 50 premature infants born between the 21st and 37th weeks of gestation. The lymphocytes exhibited three types of enzymatic cytochemical reaction, i.e. granular, diffuse and mixed (both granular and diffuse). The total count of enzyme-positive lymphocytes was significantly lower in the group of premature infants born between the 21st and 28th weeks of gestation as compared with those born later. This difference was due to the smaller numbers of enzyme-positive lymphocytes with granular reaction type in the group of more immature infants. The formation of enzyme-positive lysosomal granules within the lymphocyte cytoplasm during the last months of fetal development has been suggested and the relationship between the enzymatic equipment of lymphocyte lysosomes and immune response discussed.

Acetylglucosaminidase↗
PubMed1976

The lysosomal enzymes of lymphocytes in the premature and the term infant.

Activity of acid phosphatase, beta-glucuronidase, and beta-glucosaminidase was determined in peripheral blood lymphocytes of 29 premature and 20 term infants with the use of cytochemical methods. The results were expressed semiquantitatively and included the total count of enzyme-positive and the enzyme-negative lymphocytes as well as the intracellular content of enzyme-positive and enzyme-negative lysosomal granules. The premature infant exhibited significantly lower activity of all the studied enzymes than the term infants. It thus argues in favour of the opinion that the lysosomal apparatus in lymphocytes undergoes development in the course of fetal maturation of the immune system. Evaluation of the activity of lysosomal enzymes in lymphocytes can serve as an indicator of fetal maturity and immunological status.

Acid Phosphatase↗
PubMed1976

T cells, B cells and intermediate forms in the newborn studied by scanning electron microscopy and phosphatase marker.

Scanning electron microscopic studies of peripheral blood lymphocytes showed that percentage of T cells was lower in four cases of premature infants born between 30th and 34th week of gestation when compared with that in four cases of term infants (18.6% and 39.9% counted from 956 and 1,379 lymphocytes, respectively). The occurence of lymphocytes with intermediate patterns of surface morphology (I cells) was noted in both groups studied. Percentages of B and I cells were higher in the premature than in the term infant (26.3% and 55.1% and 20.0% and 39.1%, respectively). Analogous tendency in the T cell occurence in the premature and the term infant was demonstrated with acid phosphatase as T cell marker.

Acid Phosphatase↗