These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: [Effect of adenosine triphosphate on type Ⅰ collagen mineralization in hard tissue]. Author: Kong WJ, Chen CQ, Gu XH. Journal: Zhonghua Kou Qiang Yi Xue Za Zhi; 2019 Jul 09; 54(7):475-480. PubMed ID: 31288328. Abstract: Objective: To observe the effect of adenosine triphosphate (ATP) phosphorylation on type Ⅰ collagen mineralization and explore the role of small molecule compound ATP in biomimetic mineralization. Methods: Fourier transform infrared spectroscopy (FT-IR) was used to analyze the phosphorylation of collagen molecules by different concentrations (0, 25, 50, 100 mmol/L) of ATP. The concentration of 50 mmol/L ATP was chosen to construct the phosphorylated collagen mineralization model. Transmission electron microscopy (TEM) was used to observed the ultrastructure of mineralized collagen and the collagen mineralization rate was further calculated by ImageJ software. The surface morphology of the collagen gel ATP group and the control group was observed by scanning electron microscopy (SEM) and the elemental analysis was performed by using an X-ray energy spectrometer. The artificial demineralized dentin samples were mineralized for 2 days and 4 days to compare the effect of ATP on dentin remineralization by SEM. Results: FT-IR analysis showed that the formation of new peaks at wavenumbers of 642, 818, and 902 cm(-1) indicated that ATP can phosphorylate type Ⅰ collagen. Through TEM and SEM observation, the mineralization degree of type Ⅰ collagen and demineralized dentin pretreated with 50 mmol/L ATP were significantly higher than that of the control group. Compared with the control group [(31.65±1.62)%], the mineralization rate of collagen in the ATP group [(100±0)%] was significantly increased after 2 days of mineralization (P<0.05). Conclusions: ATP phosphorylation can effectively promote the mineralization process of type Ⅰ collagen. 目的: 采用腺苷三磷酸(adenosine triphosphate,ATP)进行Ⅰ型胶原磷酸化,探讨ATP在牙体硬组织Ⅰ型胶原纤维仿生矿化中的作用。 方法: 制备胶原凝胶薄膜,采用傅里叶变换红外光谱(Fourier transform infrared spectrum,FT-IR)分析不同浓度(0、25、50、100 mmol/L)ATP对胶原分子的磷酸化效果。选取浓度为50 mmol/L的ATP水溶液研究磷酸化Ⅰ型胶原的矿化进程。制备单层胶原模型,在矿化0、2 d后从单层胶原ATP组及其对照组(去离子水浸泡)各取样本15个,用透射电镜观察两组胶原超微结构并计算胶原矿化率。用扫描电镜观察三维胶原凝胶,对比矿化0、10 d后三维胶原凝胶ATP组及其对照组(去离子水浸泡)的表面形貌,同时用能量色散X射线谱(X-ray energy dispersive spectrum,EDS)进行元素分析。制备脱矿牙本质模型,用扫描电镜观察磷酸化的牙本质ATP组及其对照组(去离子水浸泡)矿化0、2、4 d后的矿化程度(每个时间点样本量均为10)。 结果: FT-IR显示,25、50、100 mmol/L ATP处理后Ⅰ型胶原在642、818、902 cm(-1)处形成新的吸收峰,表明ATP可使Ⅰ型胶原磷酸化。透射电镜和扫描电镜显示,相同时间矿化处理后,50 mmol/L ATP预处理的Ⅰ型胶原及脱矿牙本质的矿化效果均较相应对照组明显提升,单层胶原ATP组矿化2 d的胶原矿化率[(100±0)%]显著大于相应对照组[(31.65±1.62)%](P<0.05)。 结论: ATP作为磷酸化试剂,可有效促进牙体硬组织Ⅰ型胶原的矿化进程。.[Abstract] [Full Text] [Related] [New Search]