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胶原蛋白交联缺陷对移植骨植入的影响。

Effect of Collagen Cross-Link Deficiency on Incorporation of Grafted Bone.

作者信息

Mubarak Suliman, Masako Nagasawa, Al-Omari Farah A, Keisuke Hamaya, Katsumi Uoshima

机构信息

Division of Bio-Prosthodontics, Graduate School of Medical and Dental Sciences, Faculty of Dentistry, Niigata University, 2-5274 Gakkocho-dori, Chuo-ku, Niigata 951-8514, Japan.

出版信息

Dent J (Basel). 2019 May 1;7(2):45. doi: 10.3390/dj7020045.

DOI:10.3390/dj7020045
PMID:31052355
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6630422/
Abstract

Bone matrix collagen, is one of the major contributors to bone quality. No studies have examined how bone quality affects the results of bone transplantation. Collagen cross-links (CCL) are the key factor in collagen properties. The purpose was to investigate the influences of CCL for both grafted bone and recipient site bone on the success of bone augmentation. Four-week-old male Wister rats ( = 54) were divided into control and test groups. Control and test groups equally sub-divided into donors and recipients. An additional six rats were used to characterize bone at day zero. Test groups received 0.2% beta-aminoproperionitrile (BAPN) for 4 weeks as CCL inhibitor. Animals were further divided into donor and recipient groups. The transplanted bone chips integrated with host bone by 25% more in CCL-deficient animals compared to control. However, no difference in cortical thickness among all conditions. CCL-deficient transplanted bone did not show any extra signs of osteocyte apoptosis, while sclerostin expression was comparable to that in control. The host periosteum of CCL-deficient animals showed higher cellular activity, as well as higher bone quantity and osteoclast activity. Collagen cross-links deficiency in host bone might accelerate the incorporation of grafted bone. effect. Incorporation of the bone grafts appears to depend mainly on host condition rather than graft condition.

摘要

骨基质胶原蛋白是骨质量的主要贡献者之一。尚无研究探讨骨质量如何影响骨移植的结果。胶原交联(CCL)是胶原蛋白特性的关键因素。目的是研究CCL对移植骨和受体部位骨在骨增量成功方面的影响。将4周龄雄性Wistar大鼠(n = 54)分为对照组和试验组。对照组和试验组再平均分为供体组和受体组。另外6只大鼠用于在第0天对骨进行表征。试验组接受0.2%β-氨基丙腈(BAPN)作为CCL抑制剂,持续4周。动物进一步分为供体组和受体组。与对照组相比,CCL缺乏的动物中移植的骨碎片与宿主骨的整合度高出25%。然而,所有条件下皮质厚度均无差异。CCL缺乏的移植骨未显示任何骨细胞凋亡的额外迹象,而硬化蛋白表达与对照组相当。CCL缺乏动物的宿主骨膜显示出更高的细胞活性,以及更高的骨量和破骨细胞活性。宿主骨中的胶原交联缺乏可能会加速移植骨的整合。骨移植的整合似乎主要取决于宿主状况而非移植状况。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/5cf9a7f2eeb9/dentistry-07-00045-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/c91551a83e2f/dentistry-07-00045-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/470b29db651c/dentistry-07-00045-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/6043d030c53f/dentistry-07-00045-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/08ef0c04c1c4/dentistry-07-00045-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/4f99b5b1d8c0/dentistry-07-00045-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/564face9bb5d/dentistry-07-00045-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/73cd9a678878/dentistry-07-00045-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/5cf9a7f2eeb9/dentistry-07-00045-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/c91551a83e2f/dentistry-07-00045-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/470b29db651c/dentistry-07-00045-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/6043d030c53f/dentistry-07-00045-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/08ef0c04c1c4/dentistry-07-00045-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/4f99b5b1d8c0/dentistry-07-00045-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/564face9bb5d/dentistry-07-00045-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/73cd9a678878/dentistry-07-00045-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea51/6630422/5cf9a7f2eeb9/dentistry-07-00045-g008.jpg

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本文引用的文献

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Extracellular matrix with defective collagen cross-linking affects the differentiation of bone cells.细胞外基质中胶原交联缺陷会影响骨细胞的分化。
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β-Aminopropionitrile-Induced Reduction in Enzymatic Crosslinking Causes In Vitro Changes in Collagen Morphology and Molecular Composition.β-氨基丙腈诱导的酶交联减少导致胶原蛋白形态和分子组成的体外变化。
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