Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The authors have examined the enzyme histochemical staining of surgically removed human thyroid tissue in an attempt to identify markers that might be useful in the histopathologic diagnosis of thyroid neoplasms. Fresh thyroid glands and other tissues were fixed in cold (4 degrees C) 4% paraformaldehyde and embedded in glycol methacrylate. Forty-two specimens were studied in thin sections, which gave excellent histologic detail and enzyme preservation. Cytologic detail was similar to that in Papanicolaou-stained smears, with good definition of nuclear inclusions and grooves, particularly in cases of papillary carcinoma. The enzyme histochemical reactions studied were as follows: adenosine triphosphatase, alkaline and acid phosphatases, alpha-naphthyl acetate esterase, and 5'-nucleotidase. Thyroid epithelial cells and the benign neoplasms derived from them were typically positive for 5'-nucleotidase, alpha-naphthyl acetate esterase, and acid phosphatase, and negative for adenosine triphosphatase and alkaline phosphatase. Staining for adenosine triphosphatase was present in papillary and follicular carcinomas and was seen in benign glands only under certain circumstances such as Graves' disease. The adenosine triphosphatase reaction therefore appears to be helpful in distinguishing between benign and malignant neoplasms derived from thyroid epithelium in humans and may be a useful adjunct to routine morphology.
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PMID:Enzyme histochemistry and thyroid neoplasia. 301 Jun 99

The adenylate cyclase and 5'-nucleotidase activity was measured biochemically in the thyroid glands from patients with various thyroid diseases in comparison with normal thyroid. The basal adenylate cyclase activity in normal thyroid was 159.3 p-moles cAMP/min./g tissue. The activity was elevated to 230% of basal with 20 mM NaF and 190% of basal with 100 mU/ml TSH. These values in chronic thyroiditis and Graves' disease were not significantly different from the values of normal thyroid. In adenomatous goiter, adenoma and carcinoma, the basal adenylate cyclase activity was significantly higher than that of normal thyroid. Parallel to the biochemical determination of both enzyme activities, the distribution of histochemically demonstrable adenylate cyclase and 5'-nucleotidase activity was described in the follicular cells with normal and various thyroid diseases. The reaction product of adenylate cyclase and 5'-nucleotidase activity was restricted to the plasma membrane of the follicular cells. However, the distribution and intensity of the adenylate cyclase reaction varied in each thyroid disease, except for the absence of reaction product in the basal plasma membrane. The lack of demonstrable adenylate cyclase activity in the basal plasma membrane suggests the possibility that the basal plasma membrane may not play an important role of TSH-reception.
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PMID:Histochemical and biochemical study on adenylate cyclase and 5'-nucleotidase activity in thyroid glands with normal and various thyroid diseases. 631 19