Isozyme pattern of enolase of childhood tumors
- 15 July 1984
- Vol. 54 (2) , 293-296
- https://doi.org/10.1002/1097-0142(19840715)54:2<293::aid-cncr2820540218>3.0.co;2-u
Abstract
Retinoblastoma, neuroblastoma, and medulloblastoma have many common features, clinical as well as histologic; a common embryonic origin has been suggested. The authors studied the electrophoretic pattern of enolase (EC 4.2.1.11) in these tumors. All tumors were characterized by the presence of three types of enolase, designated as αα, αγ and γγ. The latter is supposed to be the neuron-specific enolase. Normal adult brain and adult retina show the same set of isozymes (αα, αγ and γγ). In contrast, gliomas of childhood, tumors originating from the supportive tissue of the central nervous system, are characterized mainly by the presence of the αα dimer and a small amount of the αγ hybrid. The results of this report support the hypothesis of a common embryonic origin of retinoblastoma, neuroblastoma, and medullo-blastoma.This publication has 10 references indexed in Scilit:
- Enolase isoenzyme distribution in the human brain and its tumoursThe Journal of Pathology, 1982
- SERUM NEURON-SPECIFIC ENOLASE: A MARKER FOR DISEASE EXTENT AND RESPONSE TO THERAPY OF SMALL-CELL LUNG CANCERThe Lancet, 1982
- Differentiation of medulloblastomaJournal of Neurosurgery, 1981
- Blood Platelets Contain a Neuron‐Specific Enolase SubunitJournal of Neurochemistry, 1980
- Neurone-specific enolase is a molecular marker for peripheral and central neuroendocrine cellsNature, 1978
- Primitive neuroectodermal tumors of the central nervous system in childrenJournal of Neurosurgery, 1978
- Neuron specific protein (NSP) in neuroblastoma cells: Relation to differentiationBrain Research, 1978
- Brain Enolases as Specific Markers of Neuronal and Glial CellsScience, 1978
- Enolase isoenzymesBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- Isolation and characterization of the nervous system-specific protein 14-3-2 from rat brain. Purification, subunit composition, and comparison to the beef brain protein.Journal of Biological Chemistry, 1975