Search PubMed⌕ Search
Home/Archive/PubMed

PubMed · 1148393

Complement-sensitive red cells in aplastic anemia.

I Ben-Bassat·F Brok-Simoni·B Ramot
View original source ↗Export metadata ↓

Abstract

In view of the clinical association of aplastic anemia (AA) and paroxysmal nocturnal hemoglobinuria (PNH), the complement-dependent lysis of the youngest red cells of AA patients was studied. A complement-sensitive population of young red cells was found in five of six patients with AA. These cells were rapidly cleared from the circulation and were undetectable in the oldest cell fraction. Such cells were not found in normal controls or in a variety of hematologic disorders, with the exception of PNH. This study suggests that in most patients with AA, even without any clinical manifestations of PNH, there is a population of dyserythropoietic, short-lived complement-sensitive cells.

Explore related subjects

AcetylcholinesteraseAdultAgedAnemia, AplasticCell SeparationComplement System ProteinsDensitometryErythrocyte AgingErythrocytesFemaleGlucosephosphate DehydrogenaseHemoglobinuria, ParoxysmalHemolysisHumansMaleMiddle AgedPhthalic AcidsJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

I Ben-Bassat, F Brok-Simoni, B Ramot. 1975. Complement-sensitive red cells in aplastic anemia.. https://pubmed.ncbi.nlm.nih.gov/1148393/

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

KEEP EXPLORING

Related citations

PubMed2002

Transcriptional regulation of gene expression by the coding sequence: An attempt to enhance expression of human AChE.

In a previous report, Morel and Massoulié showed that Bungarus AChE (bBAChE) is produced more efficiently than rat AChE in various expression systems, mainly because the Bungarus coding sequence exerts a stimulatory effect on transcription (Morel and Massoulié, 2000). They reported that a 5' Bungarus fragment could partially transfer this property to a CAT expression vector. This appeared to offer the possibility of increasing the production of recombinant proteins. In the present paper, we show that insertion of this fragment in the transcribed region, before the polyadenylation site, may have either stimulatory or inhibitory effects, depending on the vector and on the reporter gene. Since the stimulatory effect of Bungarus coding region could not be attached to a small number of discrete motifs, we reasoned that it might result from a general feature of the sequence. Therefore it might be possible to partially transfer this property to the very homologous human AChE (hHAChE) coding sequence by modifications based on synonymous codons, which increased nucleotide identity between the 5' fragment (721 nucleotides) of bBAChE and hHAChE from 71% to 85%. The production of human AChE in transfected COS cells was increased nearly 2-fold with this modified construct, but still remained about 4-fold smaller than that of Bungarus AChE. There was no change in expression level in transformed Pichia pastoris. We thus confirm that coding sequences can strongly influence gene expression, but in a manner that depends on the context and cannot yet be predicted.

Acetylcholinesterase↗
PubMed2002

Rapid assessment of organophosphorous/carbamate exposure in the bivalve mollusc Mytilus edulis using combined esterase activities as biomarkers.

Carboxylesterases in bivalve molluscs exhibit greater sensitivity to organophosphorous and carbamate pesticides than acetylcholinesterase and are present at higher levels. The aim of the present study was to combine measurement of both acetylcholinesterase and carboxylesterase activities in the marine bivalve Mytilus edulis in order to detect the effects of pesticide exposure. Spectrophotometric assays in microtitreplate format were optimised for use with M. edulis haemolymph and tissue homogenate samples. This permitted the nature and distribution of the enzymes to be determined. One predominant pharmacological form of activity consistent in its patterns of activation and inhibition with acetylcholinesterase was identified in the haemolymph with an apparent K(m) for acetylthiocholineiodide of 1.33 mM. Carboxylesterase activity in the tissues was characterised by its preferential hydrolysis of the substrate analogue phenylthioacetate. Concentration-dependent inhibition of both activities was demonstrated following in vitro incubation with diisopropylfluorophosphate (DFP), paraoxon and eserine in the range 0.1-3.0 mM. When M. edulis (n=10) were exposed for 24 h to concentrations of eserine or paraoxon of 0.05-1.0 mM, the percentage inhibition of acetylcholinesterase was in each case greater than for carboxylesterase and reached statistical significance at lower concentrations. In all exposures, a proportion of carboxylesterase activity was present which remained resistant to inhibition by either organophosphorous or carbamate compounds. The ecotoxicological significance of these findings for the environmental monitoring of pesticide exposure is discussed.

Acetylcholinesterase↗
PubMed2002

Molecular modeling and enzymatic studies of the interaction of a choline analogue and acetylcholinesterase.

Pivaloyl-choline iodide 1 interactions with acetylcholinesterase (AChE) have been studied by theoretical and enzymatic methods. An integrated computational approach has clearly shown a substrate rather than inhibitory profile for 1. Enzymatic experiments have also supported the same theoretical conclusion indicating that AChE was able to hydrolyze 1 to choline.

Acetylcholinesterase↗