ADSORBED SALIVARY ACIDIC PROLINE-RICH PROTEINS CONTRIBUTE TO THE ADHESION OF STREPTOCOCCUS-MUTANS JBP TO APATITIC SURFACES
ADSORBED SALIVARY ACIDIC PROLINE-RICH PROTEINS CONTRIBUTE TO THE ADHESION OF STREPTOCOCCUS-MUTANS JBP TO APATITIC SURFACES
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DOI：
10.1177/00220345890680090201
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发表时间：
1989-09-01
影响因子：
7.6
通讯作者：
HAY, DI
中科院分区：
文献类型：
--
作者：
GIBBONS, RJ;HAY, DI
与从缓冲液、人血浆或血清制备的薄膜相比，在腮腺或下颌下唾液的羟基磷灰石 (HA) 珠上形成的实验薄膜更能促进变形链球菌 JBP 细胞的粘附。通过在 Trisacryl GF 2000 柱上层析获得的腮腺唾液级分制备薄膜，研究了唾液成分的性质。两组级分促进了生物体的附着。在高分子量粘蛋白级分中迁移的成分是最有效的，但后来洗脱的级分也具有粘附促进活性。后续材料的细分表明粘附促进活性与富含脯氨酸的酸性蛋白（PRP）相关。由 10-20μg/mL 纯 PRP-1 溶液制备的薄膜可有效促进变形链球菌 JBP 细胞的附着。 PRP-3 效果较差，而人唾液富酪蛋白、纤维蛋白原、纤连蛋白、1 型胶原和源自 PRP-1 的氨基末端胰蛋白酶肽则无效。使用放射性标记的蛋白质示踪剂估计了掺入由唾液制备的实验薄膜中的 150 个残基和 106 个残基 PRP 以及富酪蛋白的数量。获得的数据表明这些蛋白质竞争 HA 上的相似结合位点，因此它们在唾液中的比例将影响掺入薄膜中的较大 PRP 的数量。这种竞争可能导致不同唾液样本的粘附促进活性存在差异。
Experimental pellicles formed on hydroxyapatite (HA) beads from parotid or submandibular saliva promoted the adhesion of Streptococcus mutans JBP cells to a greater extent than did pellicles prepared from buffer, human plasma, or serum. The nature of the salivary components responsible was studied by the preparation of pellicles from fractions of parotid saliva obtained by chromatography on Trisacryl GF 2000 columns. Two groups of fractions promoted attachment of the organism. Components migrating in the high-molecular-weight mucin fraction were most effective, but a later-eluting fraction also possessed adhesion-promoting activity. Subfractionation of the later material indicated that the adhesion-promoting activity was associated with the acidic proline-rich proteins (PRPs). Pellicles prepared from 10-20-.mu.g/mL solutions of pure PRP-1 were effective in promoting attachment of S. mutans JBP cells. PRP-3 was less effective, while human salivary statherin, fibrinogen, fibronectin, type 1 collagen and the amino-terminal tryptic peptide derived from PRP-1 were ineffective. The quantities of 150-residue and 106-residue PRPs and of statherin, which become incorporated into experimental pellicles prepared from saliva, were estimated with use of radiolabeled protein tracers. The data obtained suggest that these proteins compete for similar binding sites on HA, and that their ratios in saliva would therefore influence the quantity of the larger PRPs that become incorporated into the pellicle. Such competition may contribute to the variability observed in the adhesion-promoting activities of different saliva samples.