Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin l
Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 104 times less cellular and in vivo toxicity than ricin that are currently being considered for the construction of anti-cancer conjugates. Here we provide evidence that both RIPs can be used for the construction of conjugat...
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Published in | Cancer letters Vol. 184; no. 1; pp. 29 - 35 |
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Main Authors | , , , , , |
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Language | English |
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08.10.2002
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Abstract | Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 104 times less cellular and in vivo toxicity than ricin that are currently being considered for the construction of anti-cancer conjugates. Here we provide evidence that both RIPs can be used for the construction of conjugates directed to a target such as the transferrin receptor (TfR), which is over-expressed in cancer cells. Nigrin b– and ebulin l–transferrin conjugates were constructed with no substantial reduction in the translational inhibitory molecular activity of either RIPs. Conjugation with transferrin decreased the IC50 of the proteins from 3×10−7M (nigrin b) and 1.5×10−8M (ebulin l) to 3.5×10−10M in HeLa cells. Thus, both conjugates could be considered as useful tools for targeting TfR-over-expressing cancer cells. |
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AbstractList | Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 104times less cellular and in vivo toxicity than ricin that are currently being considered for the construction of anti-cancer conjugates. Here we provide evidence that both RIPs can be used for the construction of conjugates directed to a target such as the transferrin receptor (TfR), which is over-expressed in cancer cells. Nigrin b- and ebulin l-transferrin conjugates were constructed with no substantial reduction in the translational inhibitory molecular activity of either RIPs. Conjugation with transferrin decreased the IC50of the proteins from 3×10-7M (nigrin b) and 1.5×10-8M (ebulin l) to 3.5×10-10M in HeLa cells. Thus, both conjugates could be considered as useful tools for targeting TfR-over-expressing cancer cells. Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 10(4) times less cellular and in vivo toxicity than ricin that are currently being considered for the construction of anti-cancer conjugates. Here we provide evidence that both RIPs can be used for the construction of conjugates directed to a target such as the transferrin receptor (TfR), which is over-expressed in cancer cells. Nigrin b- and ebulin l-transferrin conjugates were constructed with no substantial reduction in the translational inhibitory molecular activity of either RIPs. Conjugation with transferrin decreased the IC(50) of the proteins from 3 x 10(-7)M (nigrin b) and 1.5 x 10(-8)M (ebulin l) to 3.5 x 10(-10)M in HeLa cells. Thus, both conjugates could be considered as useful tools for targeting TfR-over-expressing cancer cells. Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 104 times less cellular and in vivo toxicity than ricin that are currently being considered for the construction of anti-cancer conjugates. Here we provide evidence that both RIPs can be used for the construction of conjugates directed to a target such as the transferrin receptor (TfR), which is over-expressed in cancer cells. Nigrin b– and ebulin l–transferrin conjugates were constructed with no substantial reduction in the translational inhibitory molecular activity of either RIPs. Conjugation with transferrin decreased the IC50 of the proteins from 3×10−7M (nigrin b) and 1.5×10−8M (ebulin l) to 3.5×10−10M in HeLa cells. Thus, both conjugates could be considered as useful tools for targeting TfR-over-expressing cancer cells. |
Author | Benı́tez, Jorge Citores, Lucı́a Muñoz, Raquel Girbés, Tomás Miguel Ferreras, J. Jiménez, Pilar |
Author_xml | – sequence: 1 givenname: Lucı́a surname: Citores fullname: Citores, Lucı́a – sequence: 2 givenname: J. surname: Miguel Ferreras fullname: Miguel Ferreras, J. – sequence: 3 givenname: Raquel surname: Muñoz fullname: Muñoz, Raquel – sequence: 4 givenname: Jorge surname: Benı́tez fullname: Benı́tez, Jorge – sequence: 5 givenname: Pilar surname: Jiménez fullname: Jiménez, Pilar – sequence: 6 givenname: Tomás surname: Girbés fullname: Girbés, Tomás email: girbes@bio.uva.es |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12104045$$D View this record in MEDLINE/PubMed |
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Keywords | SPDP, N-succinimidyl-3-(2-pyridyldithio)propionate Ribosome-inactivating proteins IC50, concentration of inhibitor that gives 50% inhibition of protein synthesis Nigrin b TfR, transferrin receptor MBS, m-maleimido-benzoyl-N-hydroxysuccinimidyl ester HARA, human anti-ricin antibodies Cancer therapy 2-IT, 2-iminothiolane HeLa cells RIP, ribosome-inactivating protein Transferrin conjugates Ebulin l Tf, transferrin |
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Snippet | Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 104 times less cellular and in vivo toxicity than ricin that are currently being... Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 10(4) times less cellular and in vivo toxicity than ricin that are currently being... Nigrin b and ebulin l are type 2 ribosome-inactivating proteins (RIPs) with 104times less cellular and in vivo toxicity than ricin that are currently being... |
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SubjectTerms | Animals Apoptosis Binding sites Cancer Cancer therapies Cancer therapy Chromatography Construction Drug Delivery Systems Ebulin l HeLa cells HeLa Cells - drug effects HeLa Cells - metabolism Humans N-Glycosyl Hydrolases - pharmacology Nigrin b Plant Proteins - pharmacology Polypeptides Protein synthesis Protein Synthesis Inhibitors - pharmacology Proteins Rabbits Receptors, Transferrin - metabolism Ribosome Inactivating Proteins, Type 2 Ribosome-inactivating proteins Studies Transferrin - pharmacology Transferrin conjugates |
Title | Targeting cancer cells with transferrin conjugates containing the non-toxic type 2 ribosome-inactivating proteins nigrin b or ebulin l |
URI | https://dx.doi.org/10.1016/S0304-3835(02)00169-6 https://www.ncbi.nlm.nih.gov/pubmed/12104045 https://www.proquest.com/docview/1505361590 |
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