Document Detail


An investigation into the mechanism ofL-asparaginase resistance in L5178Y murine leukemia cells.
MedLine Citation:
PMID:  24190644     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Resistance of leukemia cells toL-asparaginase is presumed to be due to increased expression of asparagine synthetase activity by resistant cells, so they are no longer dependent on an exogenous source ofL-asparagine for growth. The mechanism by which cells acquire the ability for increased enzyme expression, however, has not been clearly defined. Evidence presented here indicates that genomic alterations in the form of translocations, gene amplification, or increased P-glycoprotein expression, do not account for the phenotypic transformation fromL-asparaginase sensitivity toL-asparaginase resistance. Instead, both sensitive and resistant L5178Y cells contain immunoreactive material detected by Western blotting with an antiserum prepared against bovine pancreatic asparagine synthetase. This suggests that the mechanism of resistance might involve modification of asparagine synthetase inL-asparaginase-resistant cells by an as-yet-unidentified mechanism or by inhibition of enzyme activity in theL-asparaginase-sensitive cells.
Authors:
J K Martin; W Sun; D Moraga-A; S M Schuster; D E Wylie
Related Documents :
24884804 - The role of high cell density in the promotion of neuroendocrine transdifferentiation o...
23911264 - A transfer efficiency model for ultrasound mediated drug/gene transferring into cells.
23022184 - Bex2 regulates cell proliferation and apoptosis in malignant glioma cells via the c-jun...
24399134 - Overexpression of aiolos inhibits cell proliferation and suppresses apoptosis in nalm-6...
20643054 - Bimodal analysis reveals a general scaling law governing nondirected and chemotactic ce...
19688834 - In vivo physiological transdifferentiation of adult adipose cells.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Amino acids     Volume:  5     ISSN:  0939-4451     ISO Abbreviation:  Amino Acids     Publication Date:  1993 Feb 
Date Detail:
Created Date:  2013-11-05     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9200312     Medline TA:  Amino Acids     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  51-69     Citation Subset:  -    
Affiliation:
School of Biological Sciences, University of Nebraska, 319 Manter Hall, 68588-0118, Lincoln, NE, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  A histidine binding protein ofEscherichia coli: a component of cystine binding protein ofEscherichia...
Next Document:  Synthesis of adhesive protein from the vitellaria of the liver flukeFasciola hepatica.