Development of monoclonal antibodies to collagens for assesing host?implant interactions
- 1 December 1989
- journal article
- research article
- Published by Wiley in Journal of Biomedical Materials Research
- Vol. 23 (S14) , 273-283
- https://doi.org/10.1002/jbm.820231403
Abstract
The biologic response to surgical implants is of importance in understanding the host interactions relating to long-term patency of implants. The methodology currently available for the assessment of host—biomaterial interactions is subjective and is limited to identification of inflammatory responses and general histopathological staining procedures associated with these processes. A clearer appraisal of the nature and type of extracellular matrix-components related to the host response to the implanted biomaterials would assist in the development of biomaterials and would allow an earlier means of predicting biocompatibility. The extracellular matrix consists of a range of similar collagen types which are difficult to distinguish using polyclonal antibodies. However, with the advent of hybridoma technology, monoclonal antibodies with the desired specificities can be produced to provide very powerful probes for assessing host—implant interactions. There were several problems associated with the production of these antibodies, mainly arising from collagens being extremely poor immunogens. The present study has examined these problems and has demonstrated that monoclonal antibodies against a range of collagen types can be produced. These antibodies were all highly specific for collagen type, but for a given collagen type, antibodies with different species specificities could be obtained. These antibodies were shown to be suitable for immunohistology of various connective tissue samples and were used to examine collagen-based vascular prostheses (Omniflow Vascular Graft) after retrieval from canine models. These data demonstrated that the monoclonal antibodies to collagens were excellent for the analysis of surgical implants and biomaterials after retrieval.This publication has 19 references indexed in Scilit:
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