Human osteoclast formation and resorptive function on biomineralized collagen

Biomineralized collagen composite materials pose an intriguing alternative to current synthetic bone graft substitutes by offering a biomimetic composition that closely resembles native bone. We hypothesize that this composite can undergo cellular resorption and remodeling similar to natural bone. W...

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Autores principales:	Daniel de Melo Pereira, Noel Davison, Pamela Habibović
Formato:	article
Lenguaje:	EN
Publicado:	KeAi Communications Co., Ltd. 2022
Materias:	Osteoclastogenesis Osteoclast resorption Biomineralized collagen Intrafibrillar mineral Bone graft substitute Materials of engineering and construction. Mechanics of materials TA401-492 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/ac7b7c1ebc5d49c58c12cc49cdfe62ea
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spelling	oai:doaj.org-article:ac7b7c1ebc5d49c58c12cc49cdfe62ea2021-11-04T04:36:31ZHuman osteoclast formation and resorptive function on biomineralized collagen2452-199X10.1016/j.bioactmat.2021.06.036https://doaj.org/article/ac7b7c1ebc5d49c58c12cc49cdfe62ea2022-02-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2452199X21003376https://doaj.org/toc/2452-199XBiomineralized collagen composite materials pose an intriguing alternative to current synthetic bone graft substitutes by offering a biomimetic composition that closely resembles native bone. We hypothesize that this composite can undergo cellular resorption and remodeling similar to natural bone. We investigate the formation and activity of human osteoclasts cultured on biomineralized collagen and pure collagen membranes in comparison to cortical bone slices. Human monocytes/macrophages from peripheral blood differentiate into multinucleated, tartrate-resistant alkaline phosphatase (TRAP)-positive osteoclast-like cells on all substrates. These cells form clear actin rings on cortical bone, but not on biomineralized collagen or pure collagen membranes. Osteoclasts form resorption pits in cortical bone, resulting in higher calcium ion concentration in cell culture medium; however, osteoclast resorption of biomineralized collagen and collagen membranes does not measurably occur. Activity of osteoclast enzymes – TRAP, carbonic anhydrase II (CA-II), and cathepsin-K (CTS-K) – is similar on all substrates, despite phenotypic differences in actin ring formation and resorption. The mesh-like structure, relatively low stiffness, and lack of RGD-containing binding domains are likely the factors responsible for preventing formation of stable actin rings on and resorption of (biomineralized) collagen membranes. This insight helps to guide further research toward the optimized design of biomineralized collagen composites as a more biomimetic bone-graft substitute.Daniel de Melo PereiraNoel DavisonPamela HabibovićKeAi Communications Co., Ltd.articleOsteoclastogenesisOsteoclast resorptionBiomineralized collagenIntrafibrillar mineralBone graft substituteMaterials of engineering and construction. Mechanics of materialsTA401-492Biology (General)QH301-705.5ENBioactive Materials, Vol 8, Iss , Pp 241-252 (2022)
institution	DOAJ
collection	DOAJ
language	EN
topic	Osteoclastogenesis Osteoclast resorption Biomineralized collagen Intrafibrillar mineral Bone graft substitute Materials of engineering and construction. Mechanics of materials TA401-492 Biology (General) QH301-705.5
spellingShingle	Osteoclastogenesis Osteoclast resorption Biomineralized collagen Intrafibrillar mineral Bone graft substitute Materials of engineering and construction. Mechanics of materials TA401-492 Biology (General) QH301-705.5 Daniel de Melo Pereira Noel Davison Pamela Habibović Human osteoclast formation and resorptive function on biomineralized collagen
description	Biomineralized collagen composite materials pose an intriguing alternative to current synthetic bone graft substitutes by offering a biomimetic composition that closely resembles native bone. We hypothesize that this composite can undergo cellular resorption and remodeling similar to natural bone. We investigate the formation and activity of human osteoclasts cultured on biomineralized collagen and pure collagen membranes in comparison to cortical bone slices. Human monocytes/macrophages from peripheral blood differentiate into multinucleated, tartrate-resistant alkaline phosphatase (TRAP)-positive osteoclast-like cells on all substrates. These cells form clear actin rings on cortical bone, but not on biomineralized collagen or pure collagen membranes. Osteoclasts form resorption pits in cortical bone, resulting in higher calcium ion concentration in cell culture medium; however, osteoclast resorption of biomineralized collagen and collagen membranes does not measurably occur. Activity of osteoclast enzymes – TRAP, carbonic anhydrase II (CA-II), and cathepsin-K (CTS-K) – is similar on all substrates, despite phenotypic differences in actin ring formation and resorption. The mesh-like structure, relatively low stiffness, and lack of RGD-containing binding domains are likely the factors responsible for preventing formation of stable actin rings on and resorption of (biomineralized) collagen membranes. This insight helps to guide further research toward the optimized design of biomineralized collagen composites as a more biomimetic bone-graft substitute.
format	article
author	Daniel de Melo Pereira Noel Davison Pamela Habibović
author_facet	Daniel de Melo Pereira Noel Davison Pamela Habibović
author_sort	Daniel de Melo Pereira
title	Human osteoclast formation and resorptive function on biomineralized collagen
title_short	Human osteoclast formation and resorptive function on biomineralized collagen
title_full	Human osteoclast formation and resorptive function on biomineralized collagen
title_fullStr	Human osteoclast formation and resorptive function on biomineralized collagen
title_full_unstemmed	Human osteoclast formation and resorptive function on biomineralized collagen
title_sort	human osteoclast formation and resorptive function on biomineralized collagen
publisher	KeAi Communications Co., Ltd.
publishDate	2022
url	https://doaj.org/article/ac7b7c1ebc5d49c58c12cc49cdfe62ea
work_keys_str_mv	AT danieldemelopereira humanosteoclastformationandresorptivefunctiononbiomineralizedcollagen AT noeldavison humanosteoclastformationandresorptivefunctiononbiomineralizedcollagen AT pamelahabibovic humanosteoclastformationandresorptivefunctiononbiomineralizedcollagen
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Human osteoclast formation and resorptive function on biomineralized collagen

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