Neuron-Specific Enolase Is Produced by Neuroendocrine Tumours

Tapia, Félix J.; Barbosa, A. J. A.; Marangos, Paul J.; Polak, Julia M.; Bloom, Stephen R.; Dermody, C.; Pearse, A. G. E.

doi:10.1016/s0140-6736(81)92682-9

Cited by 458 publications

(137 citation statements)

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“…By immunoassay, the y-enolase subunit was detected in gastric and gut carcinoids (Tapia et al, 1981;Simpson et al, 1984;Nash et al, 1986), and in a cell line from a neuroendocrine tumour of colon (Reeve et al, 1986). In contrast, no y-enolase staining was found in British Journal of Cancer (1997) (Simpson et al, 1984;Vinores et al, 1984;Fukuda et al, 1989), and low levels of reactivity were detected in a cell line from a colon carcinoma (Reeve et al, 1986).…”

Section: Discussionmentioning

confidence: 98%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Durany

Joseph²,

Campo³

et al. 1997

Br J Cancer

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SummaryWe have compared the levels of phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activities and the distribution of their isoenzymes in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinoma, lung squamous cell carcinoma and lung carcinoid. All tumours presented higher phosphoglycerate mutase and enolase activities and lower 2,3-bisphosphoglycerate phosphatase activity than the normal tissues. No changes were observed in the phosphoglycerate mutase isoenzyme patterns analysed by cellulose acetate electrophoresis. All specimens contained mainly type BB isoenzyme, traces of type MB isoenzyme and no type MM isoenzyme. However, the tumours had decreased levels of 2,3-bisphosphoglycerate mutase and 2,3-bisphosphoglycerate mutase-phosphoglycerate mutase hybrid enzyme. Determined by agarose gel electrophoresis, aa-enolase was the isoenzyme predominant in normal lung, colon and liver tissue, although ay-and yy-enolase were also present in all tissues. In colon, liver and non-endocrine lung tumours, the proportions of ay-and yy-enolase decreased. In contrast, in carcinoid tumours of the lung, the proportions of these isoenzymes increased.Keywords: 2,3-bisphosphoglycerate mutase; 2,3-bisphosphoglycerate phosphatase; enolase; phosphoglycerate mutase; isoenzyme; lung, colon and liver adenocarcinoma; lung squamous cell carcinoma; lung carcinoid Phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1, PGM) and enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) are glycolytic enzymes that catalyse consecutive reversible reactions connecting the two ATP-generating reactions in the glycolytic pathway. PGM catalyses the conversion of 3-phosphoglycerate, product of the first ATP-generating reaction, into 2-phosphoglycerate in the presence of the cofactor 2,3-bisphosphoglycerate. Enolase catalyses the conversion of 2-phosphoglycerate into phosphoenolpyruvate, substrate of the second ATP-generating reaction. In addition to the main mutase activity, PGM possesses collateral 2,3-bisphosphoglycerate synthase or 2,3-bisphosphoglycerate mutase activity (BPGM: 1,3-bisphosphoglycerate + 3-phosphoglycerate -> 3-phosphoglycerate + 2,3-bisphosphoglycerate) and 2,3-bisphosphoglycerate phosphatase activity (BPGP: 2,3-bisphosphoglycerate --3-phosphoglycerate + Pi), which is stimulated by 2-phosphoglycolate (for reviews, see Fothergill-Gilmore and Watson, 1989;Wold, 1971).In mammalian tissues, there are three isoenzymes of PGM, which result from the homodimeric and the heterodimeric combinations of two different subunits coded by separate genes and designated M (muscle) and B (brain). In early fetal life, type BB-PGM is the only form present. During myogenesis, the isoenzyme phenotype undergoes transition, type BB-PGM being replaced by the MM-form, through the MB isoenzyme. In skeletal muscle, there is an almost complete transition from the BB-to the MM-PGM, but in heart muscle complete transition does not occur (Omenn and Cheung, Omenn and Hermodson, 1975;Adamson, 1...

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Section: Discussionmentioning

confidence: 98%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Durany

Joseph²,

Campo³

et al. 1997

Br J Cancer

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“…Other general staining markers include pancreatic polypeptide, neuron-specific enolase (NSE), peptide histidine-methionine and human chorionic gonadotrophin subunits (Tapia et al 1981, Hamid et al 1986, Yiangou et al 1987. Chromogranin A (CgA), a secretory granule, is located alongside specific hormones in large dense-core vesicles of neuronal and neuroendocrine cells.…”

Section: General Markers For Neuroendocrine Tumoursmentioning

confidence: 99%

Neuroendocrine tumours.

Barakat¹,

Meeran²,

Bloom³

2004

Endocr Relat Cancer

209

111

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Neuroendocrine tumours are a heterogeneous group including, for example, carcinoid, gastroenteropancreatic neuroendocrine tumours, pituitary tumours, medullary carcinoma of the thyroid and phaeochromocytomas. They have attracted much attention in recent years, both because they are relatively easy to palliate and because they have indicated the chronic effect of the particular hormone elevated. As neuroendocrine phenotypes became better understood, the definition of neuroendocrine cells changed and is now accepted as referring to cells with neurotransmitter, neuromodulator or neuropeptide hormone production, dense-core secretory granules, and the absence of axons and synapses. Neuroendocrine markers, particularly chromogranin A, are invaluable diagnostically. Study of several neuroendocrine tumours has revealed a genetic etiology, and techniques such as genetic screening have allowed risk stratification and prevention of morbidity in patients carrying the particular mutation. Pharmacological therapy for these often slow-growing tumours, e.g. with somatostatin analogues, has dramatically improved symptom control, and radiolabelled somatostatin analogues offer targeted therapy for metastatic or inoperable disease. In this review, the diagnosis and management of patients with carcinoid, gut neuroendocrine tumours, multiple endocrine neoplasia types 1 and 2, and isolated phaeochromocytoma are evaluated.

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“…γ-Enolase isoenzymes have also been detected immunohistochemically in neuroendocrine tumours (22,23), s well s in carcinomas of the lung (3,24,25). Carney and coworkers were the first (4) to use the determination of γ-enolases s a marker for assessing the extent of the disease, and response to therapy of small cell lung cancer.…”

Section: Discussionmentioning

confidence: 99%

Enolase Isoenzymes as Tumour Markers

Kd¹,

Schumacher²,

Arnold³

et al. 1986

Clinical Chemistry and Laboratory Medicine

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Summary: a-and γ-enolase isoenzyme substance concentrations were measured in serum and plasma from healthy subjects and from 174 patients with different solid tumours. While α-enolase was found to be increased in the plasma of patients with tumours of quite different origin, γ-enolase apparently reflected malignancies of the neuroendocrine System. Before the beginning of the cytotoxic therapy γ-enolase was increased above the upper limit of the reference r nge (10 μg/l) in 27/27 patients (100%) suffering from small cell lung cancer. Most patients with squamous cell carcinoma of the lung or with prostatic cancer exhibited normal γ-enolase, while both tumour types produced high plasma substance concentrations of the aisoenzymes of enolase. Wertigkeit der Enolase-Isoenzyme als TumormarkerZusammenfassung: Die Substanzkonzentrationen von a-und γ-Enolase-Isoenzym wurden im Serum und Plasma von Gesunden und 174 Patienten mit unterschiedlichen, soliden Tumoren bestimmt. W hrend sich die α-Enolase-Formen als relativ unspezifisch, d. h. bei unterschiedlichen Tumoren im Plasma erh ht fanden, zeigten die γ-Isoenzyme maligne Erkrankungen des neuroendokrinen Systems relativ spezifisch an. Bei einem Kollektiv von 27 Patienten mit kleinzelligem Lungen-Karzinom fand sich vor der Therapie in 100% der F lle ein Anstieg der γ-Enolase ber den oberen Referenzwert (10 Hg/l). Patienten mit Plattenepithel-Karzinom der Lunge und solche mit Prostata-Karzinomen hatten in der Regel normale γ-Enolase-, dagegen erh hte aEnolase-Substanzkonzentrationen im Plasma. Introdiictionstudied and characterized by Marangos* group (2). Cells related to the amine precursor uptake and de-Recently it was found that small cell lung carcinoma carboxylation (APUD) System (1) share several com-cells also express APUD ceU-specific markers such s mon properties, which include the ability to produce bombesin, L-dopa decarboxylase and γ-enolase (3). and secrete peptides, the presence of storage vesicles The first report by Carney et al. (4) that γ-enolase is and a similar enzyine and isoenzyme pattern. One of elevated to a high degree in the serum of most small the marker proteinsforthis System is the γ-isoenzyme cell lung cancer patients was confirmed by others of enolase (neuron-specific enolase, NSE) extensively (5 -14), but it became evident that patients suffering

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Neuron-Specific Enolase Is Produced by Neuroendocrine Tumours

Cited by 458 publications

References 7 publications

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Neuroendocrine tumours.

Enolase Isoenzymes as Tumour Markers

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