Electron microscopic localization of neuron-specific enolase in rat and mouse brain.

Vinores, Stanley A.; Herman, Mary M.; Rubinstein, L. J.; Marangos, Paul J.

doi:10.1177/32.12.6389693

Cited by 77 publications

(33 citation statements)

References 16 publications

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“…In addition to cell-surface localization, the enolase antigen is found in plasma (Kato et al, 1983) and a-enolase is a common autoantigen in different forms of vasculitis (Moodie et al, 1993). Furthermore, enolase is membrane associated in certain brain tumors (Vinores et al, 1986). Therefore, mechanisms for release and membrane attachment or direct translocation to the cell membrane must exist for enolase.…”

Section: Discussionmentioning

confidence: 99%

The Role of an Enolase‐Related Molecule in Plasminogen Binding to Cells

Redlitz

Fowler

Plow

et al. 1995

European Journal of Biochemistry

236

226

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The a isoform of enolase is a candidate plasminogen receptor on U937 monocytoid cells [Miles, L. A., Dahlberg, C. L., Plescia, J., Felez, J., Kato, K. & Plow, E. F. (1991) Biochemistry 30, 1682-16911. In the present study, an enolase-related molecule was detected on the surfaces of peripheral blood monocytes and neutrophils by fluorescence-activated cell sorting. A mRNA transcript encoding a unique membrane form of an enolase-related molecule was not detected by Northem-blotting and primer-extension analyses, consistent with the cell-surface protein being authentic a-enolase. Both the a and p isoforms of purified enolase, bound plasminogen with an affinity similar to that of the cell surface. Moreover, immunopurified a-enolase enhanced plasminogen activation by tissue plasminogen activator and blocked the binding of plasminogen to a,-antiplasmin, mimicking functions arising from the association of plasminogen with cells. The interaction of the enolase isoforms with plasminogen was dependent upon recognition of the C-terminal lysyl residue of the enolases by the lysine-binding sites of plasminogen, as the interaction was blocked by (a) peptides with C-terminal lysine residues and (b) an antibody to the Cterminal aspect of enolase. A monoclonal antibody was developed, characterized and utilized to quantify the enolase molecules present on the surface of U937 cells. A substantial number of molecules, 1.8X106/ cell, was present, accounting for approximately 10% of the plasminogen-binding capacity of these cells. These studies clearly establish the role of enolase as a cell-surface plasminogen-binding site with profibrinolytic functions.

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Section: Discussionmentioning

confidence: 99%

The Role of an Enolase‐Related Molecule in Plasminogen Binding to Cells

Redlitz

Fowler

Plow

et al. 1995

European Journal of Biochemistry

236

226

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“…A total of 681 strips (average of 20/case) were stained for albumin, and 474 were stained for AR (an average of 14-15/case). Prior to immunoperoxidase staining, the tissue was treated with 1% sodium borohydride in PBS/CaC1 z for 30 rain at room temperature (60 rain for the retinitis pigmentosa specimen), which has been shown to facilitate immunocytochemical staining in specimens fixed by these protocols (Vinores et al, 1984;Milam & Jacobson, 1990), and washed three times in PBS/CaC12 for a minimum of I h. Tissue to be stained for albumin was then incubated at room temperature for 30 rain in 2% powdered non-fat dry milk in 0.05 M Tris buffered saline, pH 7.6 (TBS), then overnight at 4~ in a 1:500 dilution of rabbit anti-human albumin (Nordik, Capistrano Beach, CA) diluted in 1% powdered milk in TBS. Tissues to be stained for AR were incubated for 30 rain at room temperature in 10% normal goat serum (NGS) in TBS, and then overnight at 4~ in a 1:100 dilution of rabbit anti-rat seminal vesicle AR, provided by Dr R. F. Sorensen (Minneapolis, MN).…”

Section: Methodsmentioning

confidence: 99%

Electron microscopic immunocytochemical demonstration of blood-retinal barrier breakdown in human diabetics and its association with aldose reductase in retinal vascular endothelium and retinal pigment epithelium

et al. 1993

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Light-microscopic immunohistochemical staining for albumin has been used to localize sites of blood-retinal barrier (BRB) breakdown in ocular disorders, but the mechanism for BRB compromise cannot be resolved at this level. Using eyes up to 2 days post-mortem from normal patients or from patients with diabetic retinopathy, or other disorders known to cause BRB failure, electron-microscopic immunocytochemistry reveals focal breakdown of the inner BRB, comprised of the retinal vascular endothelium (RVE), which appears to be mediated by diffuse permeation of the RVE cells and by vesicular transport. Permeation of the retinal pigmented epithelial (RPE) cells that comprise the outer BRB also occurs, but there is no evidence of opening of tight junctions between RVE or RPE in any of the disorders evaluated. Increased aldose reductase (AR) expression in the RVE and RPE cells of diabetics as well as in the perivascular retinal astrocytes, which interact with RVE cells to establish the inner BRB, suggests that AR activity and the subsequent intracellular accumulation of sorbitol in these cell types may impair the function of the BRB in diabetes.

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“…Although the distribution of immunocytochemical positivity and its intracellular localization were very heterogeneous, all the tumours contained some cells that showed both cytoplasmic and membrane staining, whereas the inner nuclear membrane, the interior of nuclei, and the cristae and matrices of mitochondria were consistently negative. Ribosomes and the granular endoplasmic reticulum were occasionally positive, as in normal NSE-positive CNS neurons (Vinores et al 1984b). In some tumour cells, the staining pattern had a linear, tubular appearance, similar to that observed in the processes of some neurons in the rat and mouse brain (Vinores et al 1984b), suggesting an association with microtubules.…”

Section: Discussionmentioning

confidence: 79%

“…By electron microscopy, the enzyme within the tumour cells was not confined to the cytoplasm, as in the case of normal NSE-positive cells (Ghandour et al 1981, Vinores et al 1984b using the same staining technique, but could also be localized on the membranes of the cell surface, the mitochondrial membranes, and the nuclear membranes. Although the distribution of immunocytochemical positivity and its intracellular localization were very heterogeneous, all the tumours contained some cells that showed both cytoplasmic and membrane staining, whereas the inner nuclear membrane, the interior of nuclei, and the cristae and matrices of mitochondria were consistently negative.…”

Section: Discussionmentioning

confidence: 92%

“…The tissue was then fixed by a modification of previously described procedures (Lin, Garbern & Wu 1982, Eldred et al 1983, Vinores et al 1984b. The specimens were placed in freshly prepared fixative consisting of 4% paraformaldehyde with 8.5% sucrose, 0.2% glutaraldehyde and 1 mM CaCI2 in 0.1 M phosphate buffer, pH 7.4, usually within 10min after excision or, in three cases (Cases 4,7 and 12), they were storedin a 36°C humidified incubator with 4% C02 for up to 2 h until the fixative could be prepared, after which the specimens were placed in the solution.…”

Section: Methodsmentioning

confidence: 99%

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Electron‐immunocytochemical localization of neuron‐specific enolase in cytoplasm and on membranes of primary and metastatic cerebral tumours and on glial filaments of glioma cells

1986

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Electron-immunocytochemical localization of neuron-specific enolase in cytoplasm and on membranes of primary and metastatic cerebral tumours and on glial filaments of glioma cells. A series of primary and metastatic human brain tumours was evaluated immunocytochemically for the electron microscopic localization of neuron-specific enolase (NSE). All contained cells which, regardless of the cell type, demonstrated an irregular distribution of NSE in their cytoplasm and on membranes. This was in contrast to the staining pattern in normal central nervous system (CNS) cells which, as previously reported (Vinores el al. 1984b), show only diffuse cytoplasmic staining usually not associated with membranes. In the tumours, the interior of nuclei and the cristae and matrices of mitochondria were consistently negative, as in normal CNS cells. Except in one low-grade fibrillary astrocytoma, the cytoplasmic filaments in neoplastic astrocytes were often, but not invariably, stained for NSE. The fine structural localization of NSE in neoplastic cells suggests that the conversion of 2-Dglycerophosphate to phosphoenolpyruvate by enolase may occur on the membrane and, in the case of astrocytic tumours, on the cytoplasmic filaments as well as in the cytoplasm. When cells which contain only the non-neuronal form of enolase (NNE) transform to neoplastic cells, they may acquire the ability to produce NSE. This presumably enables them to accommodate the increased metabolic demands of neoplasia by allowing them to elude the regulatory controls that are specific for NNE.

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Electron microscopic localization of neuron-specific enolase in rat and mouse brain.

Abstract: (4A0078) cells including their dendrites, and the climbing fibers that formed synapses Materials and Methods Male and female 1295v mice (courtesy of Dr.

Cited by 77 publications

References 16 publications

The Role of an Enolase‐Related Molecule in Plasminogen Binding to Cells

The Role of an Enolase‐Related Molecule in Plasminogen Binding to Cells

Electron microscopic immunocytochemical demonstration of blood-retinal barrier breakdown in human diabetics and its association with aldose reductase in retinal vascular endothelium and retinal pigment epithelium

Electron‐immunocytochemical localization of neuron‐specific enolase in cytoplasm and on membranes of primary and metastatic cerebral tumours and on glial filaments of glioma cells

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