ehrlich cell
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IUBMB Life ◽  
1997 ◽  
Vol 41 (1) ◽  
pp. 75-81
Author(s):  
Luis Rodríguez-Caso ◽  
Daniel Rodríguez-Agudo ◽  
Antonio del Castillo-Olivares ◽  
Javier Márquez ◽  
Ignacio Núñez de Castro ◽  
...  

1996 ◽  
Vol 1313 (2) ◽  
pp. 157-160 ◽  
Author(s):  
Antonio del Castillo-Olivares ◽  
Alicia Esteban del Valle ◽  
Javier Márquez ◽  
Ignacio Núñez de Castro ◽  
Miguel Angel Medina

1996 ◽  
Vol 105 (1) ◽  
pp. 29-32 ◽  
Author(s):  
A.R. Quesada ◽  
M.A. Medina ◽  
I.Nuñez de Castro

1995 ◽  
Vol 27 (6) ◽  
pp. 605-611 ◽  
Author(s):  
Antonio del Castillo-Olivares ◽  
Alicia Esteban del Valle ◽  
Javier Márquez ◽  
Ignacio NÚñez de Castro ◽  
Miguel ángel Medina

1995 ◽  
Vol 311 (3) ◽  
pp. 743-751 ◽  
Author(s):  
J I McCormick ◽  
R M Johnstone

We have previously reported [McCormick and Johnstone (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 7877-7881] the partial purification of the Na(+)-dependent A-system amino acid transporter from Ehrlich cell plasma membranes and have suggested that a 120-130 kDa peptide, a major component of the purified fraction [octyl glucoside (OG) extract], is involved in Na(+)-dependent amino acid transport. In the present study, N-terminal sequence analysis of the 120-130 kDa peptide revealed a sequence similar to that of the alpha 3 subunit of the integrin alpha 3 beta 1. The presence of alpha 3 beta 1 was confirmed by Western blots of the OG extract probed with anti-alpha 3 or -beta 1 antibodies. Western blots also showed that an antibody originally raised against the 120-130 kDa peptide crossreacts with both the alpha 3 and beta 1 integrin subunits. Co-purification of alpha 3 beta 1 and Na(+)-dependent transport activity suggested that the two activities might be associated. Evidence that alpha 3 plays a role in transport is shown by the fact that an antibody against human alpha 3, but not beta 1, removed transport activity (approximately 25% loss) from cholate-solubilized Ehrlich membranes. Further purification of OG extracts using concanavalin A and wheat-germ lectin columns resulted in the separation of transport activity from the bulk (but not all) of alpha 3 beta 1 integrin without loss of the transport activity. These results indicate that the integrin itself is not essential for amino acid transport. Reconstitution of a purified alpha 3 beta 1-depleted protein fraction showed high levels of Na(+)-dependent, alpha-methylaminoisobutyric-acid-inhibitable amino acid transport in proteoliposomes, whereas reconstituted integrin alone showed little transport activity. However, in the integrin-depleted fractions, high amino acid uptake occurred in K+ which compromised the accurate measurement of the Na(+)-dependent component of uptake. The data suggest that alpha 3 may be associated with the A-system transporter and may modulate the activity of this carrier. Moreover, transfection of K562 and RD cells with human alpha 3 and alpha 2 cDNA showed that the former but not the latter increased A-system transport, thus providing more direct evidence that alpha 3 may modulate A-system transport activity.


1994 ◽  
Vol 1190 (1) ◽  
pp. 20-24 ◽  
Author(s):  
Miguel Angel Medina ◽  
Antonio del Castillo-Olivares ◽  
Javier Márquez ◽  
Ignacio Núñez de Castro

1992 ◽  
Vol 47 (11-12) ◽  
pp. 929-931 ◽  
Author(s):  
Antonio del Castillo-Olivares ◽  
Javier Márquez ◽  
Ignacio Núñez de Castro ◽  
Miguel Angel Medina

Ehrlich cell plasma membrane vesicles have a ferricyanide reductase activity that shows two phases. These two phases were kinetically characterized. Evidence is presented for a differential effect of trypsin on both phases


1991 ◽  
Vol 280 (3) ◽  
pp. 825-827 ◽  
Author(s):  
M A Medina ◽  
J L Urdiales ◽  
J M Mates ◽  
I Núñez de Castro ◽  
F Sánchez-Jiménez

1. L-Ornithine transport by plasma-membrane vesicles isolated from Ehrlich cells is Na(+)-independent and shows a saturable and a diffusional component. 2. Putrescine, histamine, 5-hydroxytryptamine and 2,3-diaminopropane at 55 microM concentration significantly inhibit 0.5 mM-L-ornithine transport at least for the first 10 min of incubation. 3. There is a trans-stimulatory effect of putrescine on L-ornithine transport.


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