Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P67775 (alpha isoform)
 797 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We report the presence and distribution of alpha (ubiquitous) and gamma (neuron-specific) subunits of the dimeric glycolytic enzyme enolase (2-phospho-D-glycerate hydrolase) in cultured neural cells. The gamma gamma enolase is found in vivo at high levels only in neurons and neuroendocrine cells. Neuronal cells in culture also contain relatively high levels of alpha gamma and gamma gamma enolase. Here we show, by enzymatic and immunological techniques, that the gamma subunit also is expressed in cultured rat astrocytes and meningeal fibroblasts and, as we previously reported, in oligodendrocytes. Both neuron-specific isoforms alpha gamma and gamma gamma are expressed in all these cells, but the alpha alpha isoform accounts for the major part of total enolase activity. The sum of alpha gamma and gamma gamma enolase activities increases with time in culture. i.e. maturation processes, reaching the highest level in oligodendrocytes (40% of total enolase activity) and 15 and 10% of total enzymatic activity in astrocytes and fibroblasts, respectively. The gamma enolase transcripts were found not only in cultured neuronal cells but also in cultured oligodendrocytes astrocytes, and meningeal fibroblasts. Our data indicate that neuron-specific enolase should be used with caution as a specific marker for neuronal cell differentiation.
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PMID:A comparative study of the distribution of alpha- and gamma-enolase subunits in cultured rat neural cells and fibroblasts. 917 37

We examined the expression and localisation of enolase (2-phospho-D-glycerate hydrolase) in differentiating rat spermatogenic cells. We found that enolase is most abundant in mature spermatozoa and in residual cytoplasmic bodies detached from elongating spermatids with little to no enolase detected in meiotic primary spermatocytes and round spermatids. We localised enolase mostly to the tail of mature spermatozoa by immunoblotting and by immunofluorescence. RT-PCR analysis of differentiating spermatogenic cells detected only the alpha isoform of enolase. As several glycolytic enzymes are known to associate with microtubules prepared from brain, we investigated the association of enolase with brain and testis microtubules. We found that only a small fraction of testis and brain-derived cytosolic enolase (4.9% and 11.2%, respectively) co-sediments with microtubules stabilised in the presence of taxol. In the presence of certain nucleotides in excess (3 mM ATP, CTP, GTP and ITP) the association of enolase with microtubules was disrupted, however, this was not the case for UTP. This observation is consistent with the finding that in the presence of 0.5 mM AMP-PNP, a nonhydrolysable analogue of ATP, there is an increased association of enolase with microtubules. We propose that the nucleotide-dependent association of enolase with microtubules regulates enzyme activity by linking energy production to utilisation.
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PMID:The glycolytic enzyme enolase is present in sperm tail and displays nucleotide-dependent association with microtubules. 1072 18