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Complement activation on surfaces carrying amino groups.

Complement activation on surfaces carrying amino groups. Research Abstract Details 

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  • Complement activation on surfaces carrying amino groups. Abstract Text:

    mitsuaki todaMitsuaki Toda,takayuki kitazawaTakayuki Kitazawa,isao hirataIsao Hirata,yoshiaki hiranoYoshiaki Hirano,hiroo iwataHiroo Iwata,mitsuaki todaMitsuaki Toda,takayuki kitazawaTakayuki Kitazawa,isao hirataIsao Hirata,yoshiaki hiranoYoshiaki Hirano,hiroo iwataHiroo Iwata,mitsuaki todaMitsuaki Toda,takayuki kitazawaTakayuki Kitazawa,isao hirataIsao Hirata,yoshiaki hiranoYoshiaki Hirano,hiroo iwataHiroo Iwata,

    The complement system is strongly activated by surfaces carrying nucleophilic groups, such as hydroxyl (OH) groups, and triggered by deposition of complement protein fragment, C3b. Surfaces carrying amino groups, the other representative nucleophilic group, are expected to be potential activators of the complement system through the alternative pathway. Few studies thus far have examined the potential of artificial materials carrying amino groups in activating the complement system. In this study, we employed a self-assembled monolayer (SAM) of 11-amino-1-undecanethiol (NH(2)-SAM) and a polyethyleneimine (PEI)-coated surface as model surfaces to study interactions between amino groups and serum complement pathway. SAMs of 11-mercaptoundecanol (OH-SAM) and 1-dodecanethiol (CH(3)-SAM) were used as control surfaces, respectively. Although much protein was adsorbed from serum solutions on the two types of amino surfaces, amounts of C3b deposition were much less than those observed on OH-SAM. Amounts of C3a released on the amino surfaces were same levels as that of CH(3)-SAM, but significantly smaller than that on OH-SAM. These facts suggest that the nucleophilic amino groups on NH(2)-SAM and PEI-coated surfaces do not directly activate the alternative pathway, but the protein adsorbed layers formed on amino surfaces activate it, but to an extent much smaller than that on OH-SAM. In addition, we found no deposition of C1q molecules on the amino surfaces, suggesting that these surfaces fail to activate the classical pathway. However, more careful studies are needed to conclude it, because it is known that C1q is only transiently detected at typical classical activation interfaces.

    Complement activation on surfaces carrying amino groups. Publishing Authors By Initials

    m todaM Toda,t kitazawaT Kitazawa,i hirataI Hirata,y hiranoY Hirano,h iwataH Iwata,m todaM Toda,t kitazawaT Kitazawa,i hirataI Hirata,y hiranoY Hirano,h iwataH Iwata,m todaM Toda,t kitazawaT Kitazawa,i hirataI Hirata,y hiranoY Hirano,h iwataH Iwata,

    For similar abstracts research abstracts see: abstracts research

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    Complement activation on surfaces carrying amino groups. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Biomaterials

    VOLUME: 29

    Page Numbers: 407-17

    Journal Abbreviation: Biomaterials

    ISSN: 0142-9612

    DAY: 24

    MONTH: 10

    YEAR: 2007

    Complement activation on surfaces carrying amino groups. Information

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    LANGUAGE: eng

    NlmUniqueID: 8100316

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    Grant and Affiliation Information for Complement activation on surfaces carrying amino groups.

    AFFILIATION: Advanced Software Technology & Mechatronics Research Institute of Kyoto, 134 Minamimachi Chudoji, Shimogyo-ku, Kyoto 600-8813, Japan; Institute for Frontier Medical Sciences, Kyoto University, 53 Kawara-cho, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: Biomaterials

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