COLLAGEN GENE-EXPRESSION IN HUMAN DENTAL-PULP CELL-CULTURES
COLLAGEN GENE-EXPRESSION IN HUMAN DENTAL-PULP CELL-CULTURES
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DOI：
10.1016/0003-9969(92)90066-h
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发表时间：
1992-11-01
影响因子：
3
通讯作者：
HAHN, LJ
中科院分区：
文献类型：
--
作者：
KUO, MYP;LAN, WH;HAHN, LJ
从人恒磨牙牙髓细胞分离和建立在文化中，40%的碱性磷酸酶染色呈阳性。当与50 μ g/ml的抗坏血酸和10 mM的β-甘油磷酸盐孵育时，细胞形成矿化的细胞外基质;因此，它们有可能在体外分化为成牙本质细胞样细胞。通过SDS间断凝胶电泳、北方印迹和狭缝印迹分析胶原合成：细胞主要产生（约99%）I型胶原，仅产生痕量III型胶原。α 1（I）与α 2（I）前胶原链的比例约为68：32，表明在该系统中没有合成显著量的I型胶原三聚体。α 1（I）、α 2（I）和α 1（III）前胶原mRNA的比例约为61：25：1;这些与相应的前胶原a链的比例一致。此外，一个新的5.8 kb的proalpha 1（III）的mRNA被检测到。这些观察结果表明，在这些培养的牙髓细胞中的胶原蛋白的合成在转录水平上进行调节。
Pulp cells from human permanent molars were isolated and established in culture; 40% showed positive alkaline phosphatase staining. When incubated with 50 mug/ml of ascorbic acid and 10 mM of beta-glycerophosphate, the cells formed a mineralized extracellular matrix; they could thus have the potential to differentiate into odontoblast-like cells in vitro. Collagen synthesis was analysed by SDS interrupted gel electrophoresis, Northern blot and slot blot: the cells produced predominantly (approximately 99%) type I collagen and only trace amount of type III collagen. The ratio of alpha 1(I) to alpha 2(I) procollagen chains was about 68:32, indicating that no significant amount of collagen type I trimer was synthesized in this system. The ratios of alpha 1(I), alpha 2(I) and alpha 1(III) procollagen mRNAs were about 61:25:1; these were compatible with the ratios of corresponding procollagen a chains. In addition, a novel 5.8 kb proalpha 1(III) mRNA was detected. These observations indicate that collagen synthesis in these cultured pulp cells was regulated at the transcriptional level.