cDNA cloning and characterization of neuron-specific enolase from chicken

Tanaka, Minoru; Taniguchi, Tomomi; Ohkubo, Tadayasu; Nakashima, Kenichiro

doi:10.1016/s0167-4781(97)00157-7

Cited by 2 publications

(1 citation statement)

References 30 publications

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“…As far as humans and mammals are concerned, there are three independent genetic loci, α, β and γ, that encode three types of subunits for homo-or heterodimeric enzymes (Pancholi, 2001). Enolases from several mammalian species have been purifi ed and their gene structures were determined (Tanaka et al, 1998). Despite the differences found in species, α-enolase is highly conserved.…”

Section: Introductionmentioning

confidence: 99%

Localization of Enolase in the Subfractions of a Breast Cancer Cell Line

Seweryn

Bednarz−Misa

Ceremuga

et al. 2009

Zeitschrift Für Naturforschung C

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Cell fractionationCells were washed twice in cold PBS and then resuspended in hypotonic buffer containing 10 mM Localization of Enolase in the Subfractions of a Breast Cancer Cell LineEwa Seweryn*, Jadwiga Pietkiewicz, Iwona S. Bednarz-Misa, Ireneusz Ceremuga, Jolanta Saczko, Julita Kulbacka, and Andrzej Gamian Enolase detected on the cell surface may be a receptor for certain ligands, especially for plasminogen. It is important for the pathogen invasiveness and in the development of a tumour. Therefore, we sought to preliminarily determine the enolase location and catalytic activity in the subfractions of MCF-7 cells. The latter was done on intact cells and in subfractions of MCF-7 cells. We identifi ed enolase by immunoblotting. The binding of human plasminogen to enolase was performed by immunoblotting using monoclonal antibodies against plasminogen. The intact MCF-7 cells demonstrated activity of enolase. Enolase in postnuclear and perinuclear fractions is catalyticly active too. We identifi ed the enolase protein in immunoblots of these fractions, except for the nuclear subfraction. These results provide evidence that enolase is present on the intact surface of MCF-7 cells and in post-and perinuclear fractions. The surface protein maintained catalytic activity, which suggests that its location in the plasma membrane didn't change the active centre of the enzyme.

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Section: Introductionmentioning

confidence: 99%

Localization of Enolase in the Subfractions of a Breast Cancer Cell Line

Seweryn

Bednarz−Misa

Ceremuga

et al. 2009

Zeitschrift Für Naturforschung C

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Cloning and expression of a novel cDNA encoding shell coat protein, cp4, from the brushtail possum (Trichosurus vulpecula)

Cui

Selwood

2003

Molecular Reproduction Devel

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The marsupial conceptus is enclosed by several egg coats of evolutionary significance and unknown composition, of which the shell coat in mammals occurs only in marsupials and monotremes. Intact coats are vital to marsupial embryonic development. Towards a better understanding of the marsupial coat proteins, a cDNA sequence (cp4) encoding a shell coat protein was cloned from the brushtail possum. A cDNA library of a zygote stage uterus was screened using a deduced oligonucleotide sequence based on a partial amino acid sequence of the coat protein. This study has confirmed a single copy cp4 gene encoding a unique protein of 306 amino acids, although its N-terminus shares high sequence identity with the C-terminal half of the enzyme alpha-enolase. Using Northern blots, the expression of cp4 in adult tissues showed that cp4 transcript is restricted predominantly to the uterus with two stages of expression occurring in the gravid uterus at early cleavage and bilaminar stages, suggesting an important developmental role for CP4. Using RT-PCR, cp4-specific expression as represented by the 3'-end 400 bp was present in heart, liver, oviduct, and uterus. Uterine expression reflected the increase found with Northern blot except that expression was low at unilaminar and bilaminar stages.

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cDNA cloning and characterization of neuron-specific enolase from chicken

Cited by 2 publications

References 30 publications

Localization of Enolase in the Subfractions of a Breast Cancer Cell Line

Localization of Enolase in the Subfractions of a Breast Cancer Cell Line

Cloning and expression of a novel cDNA encoding shell coat protein, cp4, from the brushtail possum (Trichosurus vulpecula)

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