Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019829 (Hodgkin's disease)
 30,247 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lectins are proteins which have the ability to interact specifically with carbohydrate residues of glycoproteins and other glycoconjugates. The staining patterns of 10 fluorescein conjugated lectins (F-Con A, F-LCA, F-RCA, F-WGA, F-PHA, F-PWM, F-LTA, F-SBA, F-PNA, F-DB) and a protease inhibitor (F-LA) have been studied in histological sections of 11 normal or reactive lymph nodes and 6 nodes and one skin biopsy involved by Hodgkin's disease. On the basis of the patterns of lectin binding, and current knowledge of their saccharide specificities, we found that within germinal centres there is an orderly carbohydrate rich extracellular matrix which contains a higher concentration of GlcNAc and terminal Gal residues than the surface membranes of component cells. This suggests active secretion rather than simple membrane shedding, and it is possible that this pericellular domain plays a part in the regulation of the proliferative response, or controls migration of lymphocytes in and out of the germinal centre. Lectin binding in Reed-Sternberg cells suggests that the huge nucleoli contain glycoconjugates of diverse structure, which may be linked with their failure to undergo cytokinesis.
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PMID:Studies of lectin binding to normal and neoplastic lymphoid tissues. I. Normal nodes and Hodgkin's disease. 618 96

The activity of GlcNAc-ase, GlcUA-ase and Gal-ase was determined in the leukocytes serum and urine of 23 patients with M. M., 11 patients with other neoplasms including 9 with lymphoreticular proliferative processes without associated monoclonal gammapathy. The range of normal enzyme activity was established in the investigations carried out in 45 health subjects. In the group of patients with M. M. without complications. normal activity of GlcNAc-ase, GlcUA-ase and Gal-ase was found in the leukocytes. In the group of patients with white blood cell count below 2.5 g/l and in cases after long-term treatment with Alkeran the activity of GlcNAc-ase and GlcUA-ase in the leukocytes was reduced. In the patients with M. M. the activity of GlcNAc-ase was raised in the serum and urine, and this activity was higher in cases with longer duration of the disease and more advanced pathological process. The patients with M-IgG protein showed a higher GlcNAc-ase activity in the serum and urine than those with protein M-IgA. A higher activity of GlcNAc-ase in the serum and urine than those with protein M-IgGK than in those with M-IgG gamma. In patients with M. M with renal complications the urinary activity of GlcNAc-ase was higher than in patients with M. M. without renal complications. In CLL the activity of GlcNAc-ase was found to be decreased in the leukocytes and raised in the urine. In patients with Hodgkin's disease the activity of the studied enzymes was raised in leukocytes while the results of their determinations in serum and urine were equivocal.
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PMID:N-acetyl-beta-glucosaminidase, beta-glucuronidase and beta-galactosidase in the leukocytes, serum and urine of healthy subjects and patients with immunocytoma. 677 53