pubmed-article:12075818 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0025202 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0025932 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0035541 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0301869 | lld:lifeskim |
pubmed-article:12075818 | lifeskim:mentions | umls-concept:C0067475 | lld:lifeskim |
pubmed-article:12075818 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12075818 | pubmed:dateCreated | 2002-6-21 | lld:pubmed |
pubmed-article:12075818 | pubmed:abstractText | Recently hydrophilic poly[N-(2-hydroxypropyl)methacrylamide] (PHPMA) was used for BS-RNase modification to prevent its degradation in bloodstream or fast elimination. Polymer-conjugated BS-RNase preparations proved to be cytotoxic after intravenous or intraperitoneal application, whereas native BS-RNase was ineffective. Here RNase A unimer was conjugated with two HPMA polymers (classic and star) and their antitumor effects both in vitro and in vivo were compared with those of BS-RNase polymers. Surprisingly, the antitumor effect of RNase A conjugates was also pronounced. The RNase A conjugates (classic and star) injected intravenously to mice bearing melanoma tumor caused a significant reduction in tumor volume following ten doses of 5 and 1 mg/kg, respectively. Despite the antitumor activity observed in vivo, the in vitro tested cytotoxic activity of RNase A did not differ from that caused by native RNase A while native BS-RNase (50 microg/ml) totally inhibited DNA synthesis in treated cells. The experiments with 125I-labeled preparations demonstrated concentration-dependent internalization of native BS-RNase by tumor cells within an hour, whereas the polymer conjugate (S-BS) was not internalized. On the contrary, the in vivo experiments showed that whereas 40% of S-BS conjugate persisted in bloodstream for 24h after administration, 98% of the native BS-RNase was already eliminated. Improved antitumor activities of PHPMA-modified RNases in vivo might be ascribed to their prolonged retention in bloodstream, better proteolytic stability and resistance to the action of the ribonuclease inhibitor. | lld:pubmed |
pubmed-article:12075818 | pubmed:language | eng | lld:pubmed |
pubmed-article:12075818 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12075818 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12075818 | pubmed:month | May | lld:pubmed |
pubmed-article:12075818 | pubmed:issn | 1061-186X | lld:pubmed |
pubmed-article:12075818 | pubmed:author | pubmed-author:PouckováPP | lld:pubmed |
pubmed-article:12075818 | pubmed:author | pubmed-author:SoucekJJ | lld:pubmed |
pubmed-article:12075818 | pubmed:author | pubmed-author:UlbrichKK | lld:pubmed |
pubmed-article:12075818 | pubmed:author | pubmed-author:StrohalmJJ | lld:pubmed |
pubmed-article:12075818 | pubmed:author | pubmed-author:HlouskováDD | lld:pubmed |
pubmed-article:12075818 | pubmed:author | pubmed-author:ZadinováMM | lld:pubmed |
pubmed-article:12075818 | pubmed:author | pubmed-author:PlocováDD | lld:pubmed |
pubmed-article:12075818 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12075818 | pubmed:volume | 10 | lld:pubmed |
pubmed-article:12075818 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12075818 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12075818 | pubmed:pagination | 175-83 | lld:pubmed |
pubmed-article:12075818 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:12075818 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12075818 | pubmed:articleTitle | Poly[N-(2-hydroxypropyl)methacrylamide] conjugates of bovine pancreatic ribonuclease (RNase A) inhibit growth of human melanoma in nude mice. | lld:pubmed |
pubmed-article:12075818 | pubmed:affiliation | Institute of Hematology and Blood Transfusion, Prague 2, Czech Republic. | lld:pubmed |
pubmed-article:12075818 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12075818 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |