Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-7-13
pubmed:abstractText
A novel supramolecular oligomer, cyclic polylactate (CPL) that was originally discovered in the culture medium of HeLa-S tumor cells, reportedly inhibits the growth of FM3A ascites tumor cells by inhibiting enzymes involved in the glycolytic pathway. We synthesized CPL containing 3- to 13-mers by prolonged heating and rapidly mixing a carbohydrate compound of the L-lactic acid monomer (C(3)H(6)O(3)) under decreased pressure, and studied its effects on the growth of the cloned leukemic cell, TF-1. CPL inhibited the growth of TF-1 cells and induced 7A6 antigen, which is expressed by cells undergoing apoptosis, on the surface of TF-1 cells. In addition, caspase 3, 8 and 9 activities of TF-1 cells were increased after exposure to CPL, indicating that CPL induces apoptotic changes in TF-1. Among the 6 glycolytic enzymes examined in this study, the activities of PFK and HK, induced by CPL, decreased. Interestingly, CPL was detected in conditioned medium of the stromal cell line, LS801, obtained from human bone marrow. This conditioned medium inhibited the growth of TF-1 cells, and induced the expression of 7A6 antigen. These findings suggest that CPL will be a useful chemotherapeutic agent against leukemia.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3, http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9, http://linkedlifedata.com/resource/pubmed/chemical/Caspases, http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned, http://linkedlifedata.com/resource/pubmed/chemical/Enzymes, http://linkedlifedata.com/resource/pubmed/chemical/Glucosephosphate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase, http://linkedlifedata.com/resource/pubmed/chemical/Lactates, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphogluconate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Polymers, http://linkedlifedata.com/resource/pubmed/chemical/antigen 7A6, http://linkedlifedata.com/resource/pubmed/chemical/cyclic polylactate
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1021-335X
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
501-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16012737-Bone Marrow Cells, pubmed-meshheading:16012737-Caspase 3, pubmed-meshheading:16012737-Caspase 9, pubmed-meshheading:16012737-Caspases, pubmed-meshheading:16012737-Cell Line, Tumor, pubmed-meshheading:16012737-Cell Proliferation, pubmed-meshheading:16012737-Chromatography, Liquid, pubmed-meshheading:16012737-Clone Cells, pubmed-meshheading:16012737-Culture Media, Conditioned, pubmed-meshheading:16012737-Dose-Response Relationship, Drug, pubmed-meshheading:16012737-Enzymes, pubmed-meshheading:16012737-Glucosephosphate Dehydrogenase, pubmed-meshheading:16012737-Glycolysis, pubmed-meshheading:16012737-HeLa Cells, pubmed-meshheading:16012737-Hexokinase, pubmed-meshheading:16012737-Humans, pubmed-meshheading:16012737-Lactates, pubmed-meshheading:16012737-Leukemia, pubmed-meshheading:16012737-Mass Spectrometry, pubmed-meshheading:16012737-Membrane Proteins, pubmed-meshheading:16012737-Phosphogluconate Dehydrogenase, pubmed-meshheading:16012737-Polymers, pubmed-meshheading:16012737-Stromal Cells
pubmed:year
2005
pubmed:articleTitle
Cyclic polylactate inhibited growth of cloned leukemic cells through reducing glycolytic enzyme activities.
pubmed:affiliation
Department of Anatomy, Nihon University School of Medicine, 30-1 Ohyaguchi-kami-machi, Itabashi-ku, Tokyo 173-8610, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't