Erythrocyte Membrane Damage in Hemolytic Anemias

Author(s):  
Augusta Brovelli
2004 ◽  
Vol 22 (5) ◽  
pp. 287-290 ◽  
Author(s):  
Lülüfer Tamer ◽  
Nehir Sucu ◽  
Bahadır Ercan ◽  
Ali Ünlü ◽  
Mukadder Çalıkoğlu ◽  
...  

Blood ◽  
1975 ◽  
Vol 45 (1) ◽  
pp. 21-27 ◽  
Author(s):  
ER Burka ◽  
SK Ballas ◽  
SM Sabesin

Abstract Exposure of rabbit or human erythrocytes to concentrations of puromycin as low as 7 x 10(-4)M for 2 hr causes damage to the cell membrane, as evidenced by increased susceptibility of the cells to hyposmotic lysis, increased cell rigidity, and ultrastructural changes consistent with severe membrane damage. Puromycin causes a concentration-dependent internalization of the erythrocyte membrane, resulting in vacuolization of the cells, at concentrations between 7 x 10(-4) M and 10(-2) M. Since the erythrocyte does not synthesize protein, the data indicate that puromycin has a direct toxic effect on erythroid cell membranes which is unrelated to its action in inhibiting the synthesis of protein.


2015 ◽  
Vol 174 ◽  
pp. 410-418 ◽  
Author(s):  
Phanuel Saroni Arwa ◽  
Maria Luiza Zeraik ◽  
Valdecir Farias Ximenes ◽  
Luiz Marcos da Fonseca ◽  
Vanderlan da Silva Bolzani ◽  
...  

Blood ◽  
1975 ◽  
Vol 45 (1) ◽  
pp. 21-27
Author(s):  
ER Burka ◽  
SK Ballas ◽  
SM Sabesin

Exposure of rabbit or human erythrocytes to concentrations of puromycin as low as 7 x 10(-4)M for 2 hr causes damage to the cell membrane, as evidenced by increased susceptibility of the cells to hyposmotic lysis, increased cell rigidity, and ultrastructural changes consistent with severe membrane damage. Puromycin causes a concentration-dependent internalization of the erythrocyte membrane, resulting in vacuolization of the cells, at concentrations between 7 x 10(-4) M and 10(-2) M. Since the erythrocyte does not synthesize protein, the data indicate that puromycin has a direct toxic effect on erythroid cell membranes which is unrelated to its action in inhibiting the synthesis of protein.


2008 ◽  
Vol 5 (2) ◽  
pp. 127-130 ◽  
Author(s):  
A. P. Kozlov ◽  
E. A. Krasavin ◽  
A. V. Boreyko ◽  
A. P. Chernyaev ◽  
P. Yu. Alekseeva ◽  
...  

2013 ◽  
Vol 2013 ◽  
pp. 1-11 ◽  
Author(s):  
Lucia Ciccoli ◽  
Claudio De Felice ◽  
Eugenio Paccagnini ◽  
Silvia Leoncini ◽  
Alessandra Pecorelli ◽  
...  

Autism spectrum disorders (ASDs) are a complex group of neurodevelopment disorders steadily rising in frequency and treatment refractory, where the search for biological markers is of paramount importance. Although red blood cells (RBCs) membrane lipidomics and rheological variables have been reported to be altered, with some suggestions indicating an increased lipid peroxidation in the erythrocyte membrane, to date no information exists on how the oxidative membrane damage may affect cytoskeletal membrane proteins and, ultimately, RBCs shape in autism. Here, we investigated RBC morphology by scanning electron microscopy in patients with classical autism, that is, the predominant ASDs phenotype (age range: 6–26 years), nonautistic neurodevelopmental disorders (i.e., “positive controls”), and healthy controls (i.e., “negative controls”). A high percentage of altered RBCs shapes, predominantly elliptocytes, was observed in autistic patients, but not in both control groups. The RBCs altered morphology in autistic subjects was related to increased erythrocyte membrane F2-isoprostanes and 4-hydroxynonenal protein adducts. In addition, an oxidative damage of the erythrocyte membraneβ-actin protein was evidenced. Therefore, the combination of erythrocyte shape abnormalities, erythrocyte membrane oxidative damage, andβ-actin alterations constitutes a previously unrecognized triad in classical autism and provides new biological markers in the diagnostic workup of ASDs.


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