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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003772naa a2200481 4500
001oai:DiVA.org:uu-130667
003SwePub
008100910s2010 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1306672 URI
0247 a https://doi.org/10.3892/ijo_000005512 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Göstring, Lovisau Uppsala universitet,Enheten för biomedicinsk strålningsvetenskap4 aut
2451 0a Quantification of internalization of EGFR-binding Affibody molecules :b Methodological aspects
264 1b Spandidos Publications,c 2010
338 a print2 rdacarrier
520 a Tumor cell internalization of targeting agents is of interest, since internalization influences the local retention time of a radionuclide and thereby imaging quality in PET and SPECT and effects of radionuclide therapy. In cases where nuclear methods are not applicable at the cellular level, quantitative fluorescent techniques are useful as described in this article. Two fluorescence-based methods to study cellular internalization were applied: the CypHer and the Alexa488-quenching methods, both utilized in fluorescence microscopy and flow cytometry. Two EGFR-binding Affibody molecules were analyzed in A431 cells: the monomer Z1907 and the dimer (Z1907)2. EGF, cetuximab and non-specific Affibody molecules were used as controls. For comparison, internalization of 111In-labeled Z1907 was studied with the acid wash internalization assay. The Cypher method is straightforward, but requires equal labeling of all compounds for accurate quantification. The Alexa488-quenching method is preferable since it is independent of the dye-to-protein ratio. According to this method, about 45% of EGF and 19-24% of the bound Affibody molecules and cetuximab were internalized within one hour. Similar results were seen with 111In-Z1907 in the acid wash method, while (Z1907)2 was not removed by acid and thus could not be studied this way. The fluorescence-based Alexa488-quenching method is well suited to quantitatively analyze internalization of targeting agents, also those that resist acid wash. The internalized fraction showed that both the monomeric and dimeric Affibody molecules are expected to give good uptake and thereby good retention of metallic radionuclides which will render good tumor to background values.
653 a 111In
653 a A431
653 a Affibody molecule
653 a Alexa488
653 a Cetuximab
653 a CypHer5E
653 a EGFR
653 a Internalization
653 a Radionuclide
653 a Retention
653 a MEDICINE
653 a MEDICIN
7001 a Chew, Ming Tsueyu Uppsala universitet,Enheten för biomedicinsk strålningsvetenskap4 aut
7001 a Orlova, Annau Uppsala universitet,Enheten för biomedicinsk strålningsvetenskap4 aut0 (Swepub:uu)annaorlo
7001 a Höidén-Guthenberg, Ingmarie4 aut
7001 a Wennborg, Anders4 aut
7001 a Carlsson, Jörgenu Uppsala universitet,Enheten för biomedicinsk strålningsvetenskap4 aut0 (Swepub:uu)jorgcarl
7001 a Frejd, Fredrik Y.u Uppsala universitet,Enheten för biomedicinsk strålningsvetenskap4 aut0 (Swepub:uu)freni195
7102 a Uppsala universitetb Enheten för biomedicinsk strålningsvetenskap4 org
7730 t International Journal of Oncologyd : Spandidos Publicationsg 36:4, s. 757-763q 36:4<757-763x 1019-6439x 1791-2423
8564 u https://www.spandidos-publications.com/ijo/36/4/757/download
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-130667
8564 8u https://doi.org/10.3892/ijo_00000551

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