Investigation of lens glycolytic enzymes: Species distribution and interaction with supramolecular order

Mathur, Rashmi; Reddy, M. Chandra Sekhar; Yee, Shawyin; Imbesi, Rosa; Groth-Vasselli, Barbara; Farnsworth, Patricia N.

doi:10.1016/s0014-4835(05)80215-5

Cited by 13 publications

(9 citation statements)

References 44 publications

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“…For example, ␣-enolase binds to F-actin and tubulin [37] and has been localized to the centrosome in HeLa cells [16,30] and to cell-surface membranes in brain tumor cells [36]. ␣-Enolase is a lens crystallin in several vertebrates [22], undergoes axonal transport in guinea pigs [4], and binds in vitro to single-stranded DNA in Saccharomyces cerevisiae [1]. Recently, a 35-kDa protein (MBP-1) that acts as a transcriptional regu- lator of c-myc in HeLa cells has been identified as a C-terminal fragment of ␣-enolase, and it is an alternative translation product of the ␣-enolase gene [34].…”

Section: Discussionmentioning

confidence: 99%

Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against α‐Enolase

et al. 2003

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Section: Discussionmentioning

confidence: 99%

Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against α‐Enolase

et al. 2003

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“…Enolase has the property of interacting in a concerted fashion with other proteins. For example, it has been shown to be one of the lens proteins in various animals [44]. And, as a case in point here, it has been demonstrated to be part of the degradosome that makes mRNA turnover in E. coli [45].…”

Section: Discussionmentioning

confidence: 99%

Global analysis of genomic texts: The distribution of AGCT tetranucleotides in the Escherichia coli and Bacillus subtilis genomes predicts translational frameshifting and ribosomal hopping in several genes

Hénaut¹,

Lisacek²,

Nitschké³

et al. 1998

Electrophoresis

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Present availability of the genomic text of bacteria allows assignment of biological known functions to many genes (typically, half of the genome's gene content). It is now time to try and predict new unexpected functions, using inductive procedures that allow correlating the content of the genomic text to possible biological functions. We show here that analysis of the genomes of Escherichia coli and Bacillus subtilis for the distribution of AGCT motifs predicts that genes exist for which the mRNA molecule can be translated as several different proteins synthesized after ribosomal frameshifting or hopping. Among these genes we found that several coded for the same function in E. coli and B. subtilis. We analyzed in depth the situation of the infB gene (experimentally known to specify synthesis of several proteins differing in their translation starts), the aceF/pdhC gene, the eno gene, and the rplI gene. In addition, genes specific to E. coli were also studied: ompA, ompFand tolA (predicting epigenetic variation that could help escape infection by phages or colicins).

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“…For instance, enolase binds to F-actin and tubulin (30,31) and has been localized to the centrosome in HeLa cells (32,33) and to cell-surface membranes in brain tumor cells (34). It is a lens crystallin in several vertebrates (35), undergoes axonal transport in guinea pigs (36), is a plasminogen receptor in a monocytoid cell line (37,38), and binds in vitro to single-stranded DNA in Saccharomyces cerevisiae (39). Enolase may also play an isoform-specific role in the stress response of S. cerevisiae (40).…”

Section: Enolase Is An Endothelial Hypoxic Stress Proteinmentioning

confidence: 99%

Non-neuronal Enolase Is an Endothelial Hypoxic Stress Protein

Aaronson

Graven

Tucci

et al. 1995

Journal of Biological Chemistry

137

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The hypoxia-associated proteins (HAPs) are five cellassociated stress proteins (M r 34, 36, 39, 47, and 57) upregulated in cultured vascular endothelial cells (EC) exposed to hypoxia. While hypoxic exposure of other cell types induces heat shock and glucose-regulated proteins, EC preferentially up-regulate HAPs. In order to identify the 47-kDa HAP, protein from hypoxic bovine EC lysates was isolated, digested with trypsin, and sequenced. Significant identity was found with enolase, a glycolytic enzyme. Western analyses confirmed that non-neuronal enolase (NNE) is up-regulated in hypoxic EC. Western analysis of subcellular fractions localized NNE primarily to the cytoplasm and confirmed that it was up-regulated 2.3-fold by hypoxia. Interestingly, NNE also appeared in the nuclear fraction of EC but was unchanged by hypoxia. Northern analyses revealed that NNE mRNA hypoxic up-regulation began at 1-2 h, peaked at 18 h, persisted for 48 h, and returned to base line after return to 21% O 2 for 24 h. Hypoxia maximally up-regulated NNE mRNA levels 3.4-fold. While hypoxic up-regulation of NNE may have a protective effect by augmenting anaerobic metabolism, we speculate that enolase may contribute to EC hypoxia tolerance through one or more of its nonglycolytic functions.Tolerance to acute hypoxia and adaptation to chronic hypoxia are crucial to the survival of cells and the organisms they comprise. Among mammalian cells, vascular endothelial cells (EC) 1 offer an excellent example of adaptation to extreme hypoxia. For example, pulmonary arterial EC normally reside in a pO 2 of 35-40 mm Hg and may be exposed to lower oxygen concentrations in disease states. Yet, we and others have shown that bovine and human EC in culture are extremely tolerant to decreases in ambient oxygen tension (1-8). We have speculated that this tolerance may be, in part, acquired. For instance, although exposure to 0% oxygen for 4 -5 days is lethal to bovine pulmonary artery and aortic EC (BPAEC and BAEC, respectively) not acclimatized to hypoxia, BPAEC and BAEC grown in 3% oxygen and then exposed to 0% oxygen survive, proliferate, and maintain characteristic EC appearance for more than 6 days. 2In studying the EC response to hypoxia, we have previously described the hypoxia associated proteins (HAPs), a unique set of five cell-associated stress proteins (M r 34, 36, 39, 47, and 57) up-regulated in a time and oxygen concentration-dependent manner in EC exposed to hypoxia (1-3). The hypoxic upregulation of HAPs in EC occurs in lieu of the stereotypic hypoxic induction of heat-shock and glucose-regulated proteins seen in more hypoxia-sensitive cells and correlates with the ability of EC to tolerate hypoxia. As part of our efforts to elucidate the function of the HAPs in physiologic and hypoxic conditions, we have previously identified the 36-kDa HAP as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (3). In the current study, we report the isolation and identification of HAP47 as non-neuronal enolase (NNE) and examine its hypoxic r...

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Investigation of lens glycolytic enzymes: Species distribution and interaction with supramolecular order

Cited by 13 publications

References 44 publications

Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against α‐Enolase

Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against α‐Enolase

Global analysis of genomic texts: The distribution of AGCT tetranucleotides in the Escherichia coli and Bacillus subtilis genomes predicts translational frameshifting and ribosomal hopping in several genes

Non-neuronal Enolase Is an Endothelial Hypoxic Stress Protein

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