Purification, radioimmuno assay, and distribution of human brain 14-3-2 protein (nervous-system specific enolase) in human tissues

Hullin, David A.; Brown, Keith; Kynoch, Pamela A.M.; Smith, Christine; Thompson, R.J.

doi:10.1016/0304-4165(80)90355-4

Cited by 65 publications

(19 citation statements)

References 24 publications

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“…Endobronchial biopsies from 20 patients (Table I) were taken as part of the usual assessment of those with lung carcinoma. The tissue was immediately fixed in Zamboni fixative (Schmechel et al, 1980 Rabbit anti-NSE and anti-PGP 9.5 were prepared and characterised as described previously (Hullin et al, 1980;Dhillon et al, 1982;Thompson et al, 1983;Doran et al, 1983;Rode et al, 1985). These studies confirmed the specificity of these markers.…”

Section: Tissue Specimensmentioning

confidence: 62%

Neural markers in carcinoma of the lung

Dhillon¹,

Rode²,

Dhillon³

et al. 1985

Br J Cancer

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Summary Small cell carcinoma (SCC) is considered to be of neuroendocrine origin. Neurone specific enolase (NSE) and PGP 9.5 are markers of neural and neuroendocrine differentiation. S-100 protein is a marker of glial differentiation. The expression of these markers in endobronchial biopsy and lung tumour resection specimens was studied to see if any diagnostic, prognostic or therapeutic implications would emerge.Zamboni fixed endobronchial tumour biopsy specimens from 20 patients were examined. Twelve of these were cases of SCC and 8 were non-SCC. Of the 12 SCC, 7 were positive for NSE, 6 for PGP 9.5 and 5 for S-100 protein. Cases which showed a positive reaction for NSE had a mean survival of 9.1 months compared with 3.9 months for those with a negative reaction, but the number of cases is too small to assign any statistical significance. There was no difference in survival times between positive and negative reactors for PGP 9.5 and S-100 protein. All 8 cases of non-SCC showed positive reactions to all three markers.Of 32 formalin fixed lung tumour resection specimens 6 were cases of SCC, 25 non-SCC and a chemodectoma. Three of the 6 cases of SCC showed positive staining for NSE, 3 for PGP 9.5 and 1 for S-100 protein. Of the 25 non-SCC, 10 were positive for NSE, 12 for PGP9.5 ard 6 for S-100 protein. The 1 chemodectoma stained positively for all tihree markers.Neuroendocrine markers are of little value in differentiating SCC from non-SCC. Positive staining for NSE in SCC may be an indicator of prolonged survival but further investigation is required.

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Section: Tissue Specimensmentioning

confidence: 62%

Neural markers in carcinoma of the lung

Dhillon¹,

Rode²,

Dhillon³

et al. 1985

Br J Cancer

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“…It has been shown by immunoassay that the three enolase subunits are present in normal human lung, colon and liver, although the proportion of a subunit is much larger than the proportions of 3 and y subunits (Schmechel et al, 1978;Marangos et al, 1979Marangos et al, , 1980Kato et al, 1983a, b;Taylor et al, 1983;Fujita et al, 1987;Marangos and Schmechel, 1987). Hullin et al (1980) found that yy-enolase determined by ionexchange chromatography represented 0.7%, 1.3% and 0.04% of the total enolase activity in extracts of lung, large intestine and liver respectively. Batandier et al (1987) showed by electrophoretic analysis that aa-enolase was the predominant isoenzyme in human lung.…”

Section: Discussionmentioning

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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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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“…[1][2][3][4][5] NSE (EC 4.2.1.11) is a glycolytic enzyme existing as isoenzyme homodimers (cc and aa), and heterodimers (ac), with the cc and ac dimers being highly abundant in the brain and at low levels in all tissues. 6 Measurement of NSE in the peripheral serum is only expected to occur after both release of intracellular NSE due to structural damage of the cell membrane, and disruption of the blood-brain barrier, although severe damage to internal organs can also result in detectable serum concentrations of NSE. 6,7 Though the half-life (t 1/2 ) of NSE is hypothesized to be between 24 and 48 h, to our knowledge, no actual kinetic studies have been performed.…”

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confidence: 99%

“…6 Measurement of NSE in the peripheral serum is only expected to occur after both release of intracellular NSE due to structural damage of the cell membrane, and disruption of the blood-brain barrier, although severe damage to internal organs can also result in detectable serum concentrations of NSE. 6,7 Though the half-life (t 1/2 ) of NSE is hypothesized to be between 24 and 48 h, to our knowledge, no actual kinetic studies have been performed. 2,4,7 S100B is a 10-kD protein and is a member of a large class of EF hand calcium binding proteins produced and secreted by a variety of glial cells in the central and peripheral nervous systems (CNS and PNS), and is also present in many tissues, including bone, myocardium, and adipose.…”

mentioning

confidence: 99%

Neuron-Specific Enolase, but Not S100B or Myelin Basic Protein, Increases in Peripheral Blood Corresponding to Lesion Volume after Cortical Impact in Piglets

Costine

Quebeda-Clerkin²,

Dodge³

et al. 2012

Journal of Neurotrauma

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A peripheral indicator of the presence and magnitude of brain injury has been a sought-after tool by clinicians. We measured neuron-specific enolase (NSE), myelin basic protein (MBP), and S100B, prior to and after scaled cortical impact in immature pigs, to determine if these purported markers increase after injury, correlate with the resulting lesion volume, and if these relationships vary with maturation. Scaled cortical impact resulted in increased lesion volume with increasing age. Concentrations of NSE, but not S100B or MBP, increased after injury in all age groups. The high variability of S100B concentrations prior to injury may have precluded detection of an increase due to injury. Total serum markers were estimated, accounting for the allometric growth of blood volume, and resulted in a positive correlation of both NSE and S100B with lesion volume. Even with allometric scaling of blood volume and a uniform mechanism of injury, NSE had only a fair to poor predictive value. In a clinical setting, where the types of injuries are varied, more investigation is required to yield a panel of serum markers that can reliably predict the extent of injury. Allometric scaling may improve estimation of serum marker release in pediatric populations.

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Purification, radioimmuno assay, and distribution of human brain 14-3-2 protein (nervous-system specific enolase) in human tissues

Cited by 65 publications

References 24 publications

Neural markers in carcinoma of the lung

Neural markers in carcinoma of the lung

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

Neuron-Specific Enolase, but Not S100B or Myelin Basic Protein, Increases in Peripheral Blood Corresponding to Lesion Volume after Cortical Impact in Piglets

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