Document Detail


Blocking of lymphokine activated killer (LAK) cell mediated cytotoxicity by cell-sized beads bearing tumor cell proteins.
MedLine Citation:
PMID:  2848896     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lymphokine activated killer cells (LAK) have been demonstrated to be cytotoxic for a variety of tumor-derived cells. Little is known of the nature of the cell surface molecules that mediate LAK cell-target cell interactions. Reported here are studies designed to develop the methodology that can lead to the identification and characterization of tumor cell surface molecules recognized by LAK cells. Results from experiments involving the pre-treatment of LAK cells and target cells (51Cr-labeled target cells or cold-blocking cells) with trypsin, neuraminidase, or sodium periodate suggest that proteins on the surface of LAK cells specifically recognized trypsin-sensitive molecules on the tumor cell surface. We extracted tumor cell membranes with detergents, and incorporated membrane proteins together with phospholipids and cholesterol onto the surfaces of cell-sized hydrophobic beads. The resulting "pseudocytes" block LAK mediated killing of 51Cr-labeled targets. Trypsin pretreatment of these pseudocytes significantly reduced their blocking activity. These observations suggested that we have incorporated onto the surface of pseudocytes tumor-membrane derived molecules that are specifically recognized by LAK cells. When membrane proteins from LAK resistant PBMC were incorporated onto beads, the resulting pseudocytes did not block LAK mediated cytotoxicity. It is of interest that beads coated with membrane proteins from one tumor were able to reduce LAK cell lysis of a different tumor target. Our results are consistent with the possibility that each LAK cell is polyspecific or that the LAK cell recognizes a common marker on many tumors. The methodology using pseudocytes should allow the purification and characterization of target acceptor molecule(s) and permit us to distinguish between these possibilities.
Authors:
A S Chong; E M Hersh; W J Grimes
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  141     ISSN:  0022-1767     ISO Abbreviation:  J. Immunol.     Publication Date:  1988 Dec 
Date Detail:
Created Date:  1989-01-18     Completed Date:  1989-01-18     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4418-24     Citation Subset:  AIM; IM    
Affiliation:
Department of Biochemistry, Arizona Cancer Center, Tucson 85721.
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MeSH Terms
Descriptor/Qualifier:
Binding, Competitive*
Cell Line
Cytotoxicity, Immunologic* / drug effects
Humans
Interleukin-2
Killer Cells, Natural / immunology*
Lymphocyte Activation / drug effects
Membrane Proteins / immunology
Microspheres*
Neoplasm Proteins / immunology*
Neuraminidase
Oligosaccharides / physiology
Periodic Acid
Trypsin
Grant Support
ID/Acronym/Agency:
GM34121/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Interleukin-2; 0/Membrane Proteins; 0/Neoplasm Proteins; 0/Oligosaccharides; 10450-60-9/Periodic Acid; 7790-28-5/metaperiodate; EC 3.2.1.18/Neuraminidase; EC 3.4.21.4/Trypsin

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


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