Enolase Isoenzymes as Tumour Markers

Kd, Gerbitz; Schumacher, Irwin C.; Arnold, HJP; Kraft, Andrea; Mross, Klaus

doi:10.1515/cclm.1986.24.12.1009

Cited by 13 publications

(18 citation statements)

References 20 publications

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“…Only in carcinoid tumours of the lung can the increase in neuron-specific enolase have clinical applications, as already indicated by others (Royds et al, 1985;Schemechel, 1985;Gerbitz et al, 1986;Marangos -and Schmechel, 1987;Kaiser et al, 1989). ABBREVIATIONS BPGM, 2,3-bisphosphoglycerate mutase; BPGP, 2,3-bisphosphoglycerate phosphatase; PGM, phosphoglycerate mutase.…”

Section: Discussionmentioning

confidence: 73%

“…Only one report has been published about PGM isoenzymes in brain tumours (Omenn and Cheung, 1974;Omenn and Hermodson, 1975) and, to our knowledge, no data exist on other tumours. Numerous studies have been published on the distribution of enolase isoenzymes in human tumours (for reviews, see Taylor et al, 1983;Royds et al, 1985;Schmechel, 1985;Gerbitz et al, 1986;Marangos and Schmechel, 1987;Kaiser et al, 1989 (Bergmeyer, 1983), as previously described (Joseph et al, 1996). Enzyme activities were expressed as U g-' wet tissue and as U mg-' protein (1 Unit = 1 [tmol substrate converted per min).…”

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confidence: 99%

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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: 73%

mentioning

confidence: 99%

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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“…NSE is a cytoplasmic glycolytic enzyme of neurons [136][137][138][139]. NSE and S100B serum levels in trauma patients have been found to correlate well to each other and to clinical outcomes and neuroimaging findings of contusion volume and presence of subarachnoid hemorrhage [70,112,121].…”

Section: Time Frame Datamentioning

confidence: 99%

Reliability of S100B in predicting severity of central nervous system injury

et al. 2007

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S100B is a protein biomarker that reflects CNS injury. It can be measured in the CSF or serum with readily available immunoassay kits. The excellent sensitivity of S100B has enabled it to confirm the existence of subtle brain injury in patients with mild head trauma, strokes, and after successful resuscitation from cardiopulmonary arrest. The extent of S100B elevation has been found to be useful in predicting clinical outcome after brain injury. Elevations of S100B above certain threshold levels might be able to reliably predict brain death or mortality. A normal S100B level reliably predicts the absence of significant CNS injury. The specificity of S100B levels as a reflection of CNS injury is compromised by the findings that extra-cranial injuries can lead to elevations in the absence of brain injury. This potential problem can most likely be avoided by measuring serial S100B levels along with other biomarkers and carefully noting peripheral injuries. Serum markers GFAP and NSE are both more specific for CNS injury and have little to no extra-cranial sources. Sustained elevations of S100B over 24 h along with elevations of GFAP and NSE can more reliably predict the extent of brain injury and clinical outcomes. In the future, S100B measurements might reliably predict secondary brain injury and enable physicians to initiate therapeutic interventions in a timelier manner. S100B levels have been shown to rise hours to days before changes in ICP, neurological examinations, and neuroimaging tests. S100B levels may also be used to monitor the efficacy of treatments.

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“…The ␥-subunit, also 47 kDa, is found in the ␥␥ and ␣␥ dimers known collectively as NSE (16,17). Neuronspecific enolase is expressed mainly in normal and neoplastic cells of neuronal and neuroendocrine origin (18,19), but has been found in diverse mammalian cell types (20,21). Neuronspecific enolase has not been found in EC (21) nor has it previously been studied during exposure to hypoxia.…”

Section: Enolase Is An Endothelial Hypoxic Stress Proteinmentioning

confidence: 99%

Non-neuronal Enolase Is an Endothelial Hypoxic Stress Protein

Aaronson

Graven

Tucci

et al. 1995

Journal of Biological Chemistry

137

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The hypoxia-associated proteins (HAPs) are five cellassociated stress proteins (M r 34, 36, 39, 47, and 57) upregulated in cultured vascular endothelial cells (EC) exposed to hypoxia. While hypoxic exposure of other cell types induces heat shock and glucose-regulated proteins, EC preferentially up-regulate HAPs. In order to identify the 47-kDa HAP, protein from hypoxic bovine EC lysates was isolated, digested with trypsin, and sequenced. Significant identity was found with enolase, a glycolytic enzyme. Western analyses confirmed that non-neuronal enolase (NNE) is up-regulated in hypoxic EC. Western analysis of subcellular fractions localized NNE primarily to the cytoplasm and confirmed that it was up-regulated 2.3-fold by hypoxia. Interestingly, NNE also appeared in the nuclear fraction of EC but was unchanged by hypoxia. Northern analyses revealed that NNE mRNA hypoxic up-regulation began at 1-2 h, peaked at 18 h, persisted for 48 h, and returned to base line after return to 21% O 2 for 24 h. Hypoxia maximally up-regulated NNE mRNA levels 3.4-fold. While hypoxic up-regulation of NNE may have a protective effect by augmenting anaerobic metabolism, we speculate that enolase may contribute to EC hypoxia tolerance through one or more of its nonglycolytic functions.Tolerance to acute hypoxia and adaptation to chronic hypoxia are crucial to the survival of cells and the organisms they comprise. Among mammalian cells, vascular endothelial cells (EC) 1 offer an excellent example of adaptation to extreme hypoxia. For example, pulmonary arterial EC normally reside in a pO 2 of 35-40 mm Hg and may be exposed to lower oxygen concentrations in disease states. Yet, we and others have shown that bovine and human EC in culture are extremely tolerant to decreases in ambient oxygen tension (1-8). We have speculated that this tolerance may be, in part, acquired. For instance, although exposure to 0% oxygen for 4 -5 days is lethal to bovine pulmonary artery and aortic EC (BPAEC and BAEC, respectively) not acclimatized to hypoxia, BPAEC and BAEC grown in 3% oxygen and then exposed to 0% oxygen survive, proliferate, and maintain characteristic EC appearance for more than 6 days. 2In studying the EC response to hypoxia, we have previously described the hypoxia associated proteins (HAPs), a unique set of five cell-associated stress proteins (M r 34, 36, 39, 47, and 57) up-regulated in a time and oxygen concentration-dependent manner in EC exposed to hypoxia (1-3). The hypoxic upregulation of HAPs in EC occurs in lieu of the stereotypic hypoxic induction of heat-shock and glucose-regulated proteins seen in more hypoxia-sensitive cells and correlates with the ability of EC to tolerate hypoxia. As part of our efforts to elucidate the function of the HAPs in physiologic and hypoxic conditions, we have previously identified the 36-kDa HAP as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (3). In the current study, we report the isolation and identification of HAP47 as non-neuronal enolase (NNE) and examine its hypoxic r...

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Enolase Isoenzymes as Tumour Markers

Cited by 13 publications

References 20 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

Reliability of S100B in predicting severity of central nervous system injury

Non-neuronal Enolase Is an Endothelial Hypoxic Stress Protein

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