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Human Anti-Gal and Anti-Non-Gal Immune Response to Porcine Tissue Implants
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C3b components bind their corresponding receptors on M1 macrophages and trigger release of matrix metalloproteinases (MMPs), the principal ECM degradative enzyme, mediating dECM graft failure.
“C3b components bind their corresponding receptors on these M1 macrophages and trigger the release of matrix metalloproteinases (MMPs), the principal ECM degradative enzyme, mediating the dECM graft failure [46, 47].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [47]
Interaction between antigens within dECM transplants and produced antibodies further activates the complement cascade and creates a vicious cycle with the output of dECM scaffold failure.
“Interaction between antigens within dECM transplants and produced antibodies further activates the complement cascade and creates a vicious cycle with the output of dECM scaffold failure [47].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [47]
ECM of tissues such as heart valves, bone, tendon, and cartilage contain abundant amounts of proteoglycans (and consequently α-gal epitopes), which may remain even after a vigorous decellularization process and cause graft failure.
“Conversely, ECM of tissues such as heart valves, bone, tendon, and cartilage contain abundant amounts of proteoglycans (and consequently α-gal epitopes), which may remain even after a vigorous decellularization process and cause graft failure [47, 116].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [47]
GA prohibits the release of substantial factors for tissue differentiation, which might compromise its application in sites other than connective tissue.
“However, GA prohibits the release of substantial factors for tissue differentiation, which might compromise its application in sites other than connective tissue [47].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [47]
Following implantation of xenografts, α-gal antibodies peak within two weeks, while anti-non-gal antibodies require one to six months.
“Following implantation of xenografts, α-gal antibodies peak within two weeks, while anti-non-gal antibodies require one [47] to six months [116].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [47]
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Kasravi, M., Ahmadi, A., Babajani, A., Mazloomnejad, R., Hatamnejad, M. R., Shariatzadeh, S., Bahrami, S., & Niknejad, H. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00348-z · Cited by 316
Metadata
- Authors
- Galili, U.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Galili, Uri
- ORCID
- Galili, Uri
- Venue
- Host Response to Biomaterials
- Publisher
- Elsevier
- Published
- 2015
- Pages
- 239-267
- OpenAlex
- W2477705402
- Cited by
- 12
- References
- 2
- Citations by year
- 2024: 3 · 2023: 5 · 2022: 1 · 2021: 1 · 2017: 2
- FWCI
- 9.51
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Elsevier eBooks (publishedVersion)
- Topics
- Health Sciences › Medicine › Surgery › Xenotransplantation and immune response
- Health Sciences › Medicine › Surgery › Tissue Engineering and Regenerative Medicine
- Health Sciences › Medicine › Transplantation › Organ and Tissue Transplantation Research
- Keywords
- anti-Gal antibodies, xenotransplantation, alpha-gal epitope, alpha-galactosidase, complement activation, macrophage recruitment, stem cell recruitment
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