PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7994419

Diaspirin crosslinked hemoglobin (DCLHb) polymerization.

T T Hai·D Nelson·D Pereira·A Srnak
View original source ↗Export metadata ↓

Abstract

By employing proprietary polymerization agents possessing specific binding groups and by completing diaspirin crosslinked hemoglobin (DCLHb) polymerization under specific conditions, we have selectively achieved the following objectives: (1) the P50 was adjusted to the physiologic range or left- or right-shifted; (2) the surface of DCLHb was modified ("decorated"); (3) DCLHb was polymerized but not decorated; (4) DCLHb was polymerized and decorated; or (5) DCLHb was site-specifically modified and polymerized.

Explore related subjects

Amino Acids, DiaminoAspirinBinding SitesBlood SubstitutesCyanobacteria ToxinsHemoglobinsHumansIn Vitro TechniquesIndicators and ReagentsOxygenPolyethylene GlycolsPolymersJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

T T Hai, D Nelson, D Pereira, A Srnak. 1994. Diaspirin crosslinked hemoglobin (DCLHb) polymerization.. https://doi.org/10.3109/10731199409117931

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2006

Down-regulation of glutaredoxin by estrogen receptor antagonist renders female mice susceptible to excitatory amino acid mediated complex I inhibition in CNS.

beta-N-oxalyl-amino-L-alanine, (L-BOAA), an excitatory amino acid, acts as an agonist of the AMPA subtype of glutamate receptors. It inhibits mitochondrial complex I in motor cortex and lumbosacral cord of male mice through oxidation of critical thiol groups, and glutaredoxin, a thiol disulfide oxido-reductase, helps maintain integrity of complex I. Since incidence of neurolathyrism is less common in women, we examined the mechanisms underlying the gender-related effects. Inhibition of complex I activity by L-BOAA was seen in male but not female mice. Pretreatment of female mice with estrogen receptor antagonist ICI 182,780 or tamoxifen sensitizes them to L-BOAA toxicity, indicating that the neuroprotection is mediated by estrogen receptors. L-BOAA triggers glutathione (GSH) loss in male mice but not in female mice, and only a small but significant increase in oxidized glutathione (GSSG) was seen in females. As a consequence, up-regulation of gamma-glutamyl cysteinyl synthase (the rate-limiting enzyme in glutathione synthesis) was seen only in male mouse CNS but not in females. Both glutathione reductase and glutaredoxin that reduce oxidized glutathione and protein glutathione mixed disulfides, respectively, were constitutively expressed at higher levels in females. Furthermore, glutaredoxin activity in female mice was down-regulated by estrogen antagonist indicating its regulation by estrogen receptor. The higher constitutive expression of glutathione reductase and glutaredoxin could potentially confer neuroprotection to female mice.

Amino Acids, Diamino↗
PubMed2006

Beta-N-methylamino-L-alanine enhances neurotoxicity through multiple mechanisms.

The idea that the environmental toxin beta-N-methylamino-l-alanine (BMAA) is involved in neurodegenerative diseases on Guam has risen and fallen over the years. The theory has gained greater interest with recent reports that BMAA is biomagnified, is widely distributed around the planet, and is present in the brains of Alzheimer's patients in Canada. We provide two important new findings. First, we show that BMAA at concentrations as low as 10 muM can potentiate neuronal injury induced by other insults. This is the first evidence that BMAA at concentrations below the mM range can enhance death of cortical neurons and illustrates potential synergistic effects of environmental toxins with underlying neurological conditions. Second, we show that the mechanism of BMAA toxicity is threefold: it is an agonist for NMDA and mGluR5 receptors, and induces oxidative stress. The results provide further support for the hypothesis that BMAA plays a role in neurodegenerative diseases.

Amino Acids, Diamino↗