C B Taylor

Enolase isoenzymes: III. Chromatographic and immunological characteristics of rat brain enolase

1. The chromatography of rat brain enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) reveals three distinet components. One of these appears to be isoenzyme 1 (alpha alpha) but isoenzymes 2 (alpha beta) and 3 (beta beta) are absent. 2. The most acidic form of brain enolase was partially purified and an antiserum raised against it in the chicken. 3. a combination of chromatographic and immunological studies showed that a third type of subunit (gamma) is present in the brain giving rise to two further isoenzymes (alpha gamma and gamma gamma). 4. Developmental studies on the brain enzyme show an increase in total enolase activity from foetal life to maturity and a concurrent rise in the proportion of brain specific dimers. 5. It is therefore concluded that there are three genetic loci alpha, beta and gamma, coding for the enolase isoenzymes of rat tissues.

Enolase isoenzymes in the cerebrospinal fluid of patients with diseases of the nervous system.

Alpha and gamma enolase isoenzymes have been studied in 212 patients with a variety of neurological diseases. The results show that these proteins are sensitive markers of tissue damage which enable a distinction to be made between the involvement of glial and neuronal components.

Levels of enolase and other enzymes in the cerebrospinal fluid as indices of pathological change

The activities of enolase, aldolase, pyruvate kinase, lactate dehydrogenase and creatine phosphokinase were measured in cerebrospinal fluid of 121 patients presenting with a range of disorders of the central nervous system. The results from 41 patients undergoing myelography were used as controls. An assessment was made of the relative merits of these five enzymes as markers of brain damage with special reference to brain tumours. Enolase was the most sensitive marker of pathological change and was the only enzyme raised in the CSF of patients with low grade astrocytomas.

THE NATURE OF THE TWO PROTEINS OF BRAIN SPECIFIC ANTIGEN 14-3-2

The three isoenzymes of rat brain enolase (2‐phospho d‐glycerate hydrolase EC 4.2.1.11.) χχ, χγ and γγ were separated by ion‐exchange chromatography and were tested for reaction with an antiserum against brain specific antigen 14‐3‐2. This monospecific antiserum affects the enolase activity of only the χγ and γγ isoenzymes.

An Immunohistochemical Study of Glial and Neuronal Markers in Primary Neoplasms of the Central Nervous System

SummaryParaffin-embedded tissues from 56 primary neoplasms of the central nervous system and seven cases of non-neoplastic reactive astrocytosis were examined by immunoperoxidase techniques on serial sections using monoclonal antibodies to glial fibrillary acidic protein (GFAP) and the 68 kDa neurofilament subunit and monospecific polyclonal antibodies to α-and γ-enolase. γ-Enolase was present in all neoplasms of neuronal origin, but was also present in anaplastic gliomas (particularly in giant cells), in some well-differentiated astrocytomas and reactive astrocytes. The cells containing γ-enolase in these cases appeared morphologically identical to those containing α-enolase and GFAP in adjacent serial sections. No relationship was found between γ-enolase immunoreactivity and cellular anaplasia in the gliomas studied. Subependymal neoplasms from patients with tuberose sclerosis exhibited evidence of both astrocytic and neuronal differentiation, sometimes in morphologically distinct cell populations, consistent with their suggested origin from a primitive cell line.

Stromal cells in cerebellar haemangioblastomas: an immunocytochemical study.

The nature of the stromal cells in formalin‐fixed paraffin‐embedded material from 23 cerebellar haemangioblastomas was investigated using antisera to intermediate filaments (glial fibrillary acidic protein, vimentin and desmin), histiocytic markers (α1‐antitrypsin, α1‐antichymotrypsin and lysozyme), glycolytic enzymes (alpha and gamma enolase and aldolase C4) and the endothelial markers, factor VIII related antigen and Ulex europaeus I lectin. Most stromal cells stained positively for vimentin and the glycolytic enzymes. Occasional process‐bearing cells within the stroma stained strongly for glial fibrillary acidic protein, α1‐antitrypsin and α1‐antichymotrypsin. No stromal cell staining for desmin, lysozyme or the endothelial markers was observed, although the latter stained the vascular endothelium within all neoplasms. The findings do not support previous suggestions of an endothelial or histiocytic origin for the stromal cells. They appear to be a heterogeneous population including entrapped reactive astrocytes and locally‐derived non‐angiogenic cells of neuroectodermal (pial) origin.

Serum aldolase isoenzymes in benign and malignant liver disease

Using a radio-immunoassay, aldolase A and B isoenzyme concentrations have been measured in the sera of patients in order to assess their specificity and sensitivity in a variety of hepatic disorders. Serum aldolase A has been confirmed to be elevated in some patients with malignant infiltration of the liver, but its sensitivity is not sufficient to be of clinical value. Aldolase B is a sensitive marker of liver cell damage which correlates closely with conventional biochemical markers of inflammation. It appears to distinguish successfully between hepatic and cardiac damage.

Carcinoid tumour arising in a recurrent intradural spinal teratoma

Carcinoid tumour arising in a recurrent intradural spinal teratoma