Native Wound-Repair Proteins Retained in Multilayer Placental CAMPs

The human placenta is a complex organ that supports fetal development and is rich in extracellular matrix proteins and growth factors, making it suitable as a biomaterial in wound care. Placenta-derived amnion-only allografts have traditionally been used in the clinic, but they lack the structural and biochemical complexity of the full three-layer placental membrane, which includes the amnion, intermediate, and chorion layers. Advances in tissue engineering have enabled preservation of multiple layers, giving rise to multilayer placental-based Cellular and Acellular Matrix-like Products (CAMPs) such as Full-Thickness (FT; amnion, intermediate, chorion) and ACA (amnion, intermediate, chorion, amnion). Although these advanced CAMPs are increasingly applied clinically, their molecular composition has not been comprehensively defined. This study presents a global proteomic analysis of FT and ACA, complemented by targeted multiplex analysis of soluble proteins and an in vitro angiogenesis assay. Proteomic profiling identified 8908 structural and bioactive components, with 32.5% of proteins associated with tissue repair and remodeling pathways. Multiplex analysis confirmed accessibility of biologically relevant soluble factors. Endothelial tube formation assays further supported biological relevance, demonstrating that soluble proteins in FT and ACA support angiogenesis. These data provide a molecular characterization of multilayer CAMPs and underscore their potential to deliver durable wound coverage while supporting the local microenvironment.

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Publication Details

Journal
International Journal of Molecular Sciences
Published
2025-10-17
DOI
https://doi.org/10.3390/ijms262010121
Primary Topic
Neonatal Respiratory Health Research
Type
article
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article

Native Wound-Repair Proteins Retained in Multilayer Placental CAMPs

Shantanu Guha, Pragya Singh, Joanna Marquez, Shauna Hill et al.
International Journal of Molecular Sciences
Neonatal Respiratory Health Research
article

Native Wound-Repair Proteins Retained in Multilayer Placental CAMPs

Shantanu Guha, Pragya Singh, Joanna Marquez, Shauna Hill, Arthur King, Diego Valdes Cavazos, Odalis Landa
article en

Abstract

The human placenta is a complex organ that supports fetal development and is rich in extracellular matrix proteins and growth factors, making it suitable as a biomaterial in wound care. Placenta-derived amnion-only allografts have traditionally been used in the clinic, but they lack the structural and biochemical complexity of the full three-layer placental membrane, which includes the amnion, intermediate, and chorion layers. Advances in tissue engineering have enabled preservation of multiple layers, giving rise to multilayer placental-based Cellular and Acellular Matrix-like Products (CAMPs) such as Full-Thickness (FT; amnion, intermediate, chorion) and ACA (amnion, intermediate, chorion, amnion). Although these advanced CAMPs are increasingly applied clinically, their molecular composition has not been comprehensively defined. This study presents a global proteomic analysis of FT and ACA, complemented by targeted multiplex analysis of soluble proteins and an in vitro angiogenesis assay. Proteomic profiling identified 8908 structural and bioactive components, with 32.5% of proteins associated with tissue repair and remodeling pathways. Multiplex analysis confirmed accessibility of biologically relevant soluble factors. Endothelial tube formation assays further supported biological relevance, demonstrating that soluble proteins in FT and ACA support angiogenesis. These data provide a molecular characterization of multilayer CAMPs and underscore their potential to deliver durable wound coverage while supporting the local microenvironment.

International Journal of Molecular SciencesVol. 26(20)
Openalex Percentile: Top 58%
Neonatal Respiratory Health Research
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Native Wound-Repair Proteins Retained in Multilayer Placental CAMPs — Shantanu Guha, Pragya Singh, et al. · International Journal of Molecular Sciences (2025) | TGRS Research Map | TGRS