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J Pilch

Publications and source records attributed to J Pilch.

68 records · Page 4Linked to original sources
PubMedDate not supplied

N-acetyl-beta-glucosaminidase of peripheral blood lymphocytes in patients with cancer of the larynx.

In 20 men, age 35 to 55 years, with cancer of the larynx of N-acetyl-beta-glucosaminidase in peripheral blood lymphocytes was determined cytochemically according to Hayashi's method. Numbers of enzyme-positive cells were counted with regard to the type of cytochemical reaction (granular, granular-diffuse, or diffuse), and to the number of enzyme-positive lysosomal granules within a single cell. In comparison to 20 healthy men, age 20 to 30 years, the following changes were noted in the patients: 1) the decrease of the total count of enzyme-negative lymphocytes; 2) the decrease of the total count of lymphocytes with granular type of reaction; 3) the increase of the counts of lymphocytes with granular-diffuse and diffuse type of reaction. The authors suggest that these changes could be related to the immune reaction of specific tumor antigens.

Adult↗
PubMedDate not supplied

Long-term effect of radiotherapy on the lymphocyte lysosomal enzymes and serum immunoglobulins in patients with cancer of the larynx.

Thirty male patients ranging in age from 40 to 70 years, investigated 6--9 years after radiotherapy for cancer of the larynx, showed various alterations of the lysosomal apparatus of peripheral blood lymphocytes. These changes, consisting of diffusion of the lysosomal enzymes within the cytoplasm and disappearance of normal lysosomal granules, were related to a greater extent to the beta-glucuronidase and N-acetyl-beta-glucosaminidase positive-lysosomes than to the acid phosphatase-positive ones. Determination of the enzymatic activities was achieved by cytochemical techniques. The increased immunological reactivity of the patients was reflected in the frequently elevated immunoglobulin levels, particularly that of IgA, in the serum and an increase of the enzyme-positive lymphocyte count in the blood.

Acetylglucosaminidase↗
PubMedDate not supplied

The enzymatic equipment of neutrophils in patients with precancerous states of the larynx.

Cytochemical investigations performed in 24 men with precancerous states of the larynx, i.e. leukoplakia, papillomas and pachydermia, indicated that the peripheral blood neutrophils from these patients exhibit a significant intracellular deficiency of beta-glucuronidase activity and of total lipids, as well as an increased alkaline phosphatase activity. Acid phosphatase and N-acetyl-beta-glucosaminidase activities did not differ significantly between patients and normal controls. In the authors' opinion, the neutrophil beta-glucuronidase deficiency might be a specific disturbance of neutrophils in the precancerous states and the cancer of the larynx. The possible significance of this disturbance and the subsequent decrease of antitumor immune reactivity are discussed.

Acid Phosphatase↗
PubMedDate not supplied

Lymphocyte lysosomal acid phosphatase in patients with carcinoma of the larynx.

The activity of lysosomal acid phosphatase in the peripheral blood lymphocytes was determined by using the method of Barka and Anderson in 20 men with carcinoma of the larynx, untreated. The results were compared with those in 20 healthy subjects. In the patients a statistically significant decrease of the lymphocyte count exhibiting enzyme-positive lysosomal granules was noted but the number of the lymphocytes with granular and diffuse or only diffuse type of cytochemical reaction was significantly increased. The lack of significant differences in the total lymphocyte count between patients and controls suggests the possibility of lysosome disruption and subsequent release of enzymes into the cytoplasm in the patients studied. The anomalies of the enzyme-positive lymphocyte lysosomal equipment are discussed in the light of the data on immunologic alterations in cancer patients, and of those suggesting that acid phosphatase may serve as marker of T cells.

Acid Phosphatase↗