Butler W T
University of Texas Health Science Center, Dental Branch, Dept. of Biological Chemistry, Houston 77225.
Connect Tissue Res. 1989;23(2-3):123-36. doi: 10.3109/03008208909002412.
Osteopontin is an acidic glycoprotein of about 41,500 daltons that has been isolated from rat, human and bovine bone. It is rich in aspartic acid, glutamic acid and serine and contains about 30 monosaccharides, including 10 sialic acids. Several types of data suggest that the carbohydrate is present as 1 N-glycoside and 5-6 O-glycosides while the phosphate is present as 12 phosphoserines and 1 phosphothreonine. The cDNA sequence indicated the presence of a Gly-Arg-Gly-Asp-Ser- (GRGDS) amino acid sequence identical to a cell binding sequence in fibronectin, and suggested that osteopontin might function as a cell attachment factor. This conclusion is supported by a number of studies showing that the protein promotes attachment and spreading of fibroblasts and osteoblasts to substratum, and that this attachment is inhibited by RGD-containing peptides. Despite this evidence that it contains an RGD recognition sequence and probably interacts with the family of receptors known as integrins, it appears that osteopontin does not possess a collagen-binding domain. Osteopontin is synthesized by preosteoblasts, osteoblasts and osteocytes, is secreted into osteoid and is incorporated into bone. The expression at an early developmental stage is an indication that osteopontin is an important component in the formation of bone. The level of synthesis of osteopontin by osteoblasts in culture is increased by treating these cells with 1,25-dihydroxyvitamin D3 and TGF-beta. The effect of these agents is at the transcriptional level. In addition to bone cells, osteopontin is synthesized by extraosseous cells in the inner ear, brain, kidney, and deciduum and placenta. It is also synthesized by odontoblasts, certain bone marrow cells and hypertrophic chondrocytes. Studies with several fibroblast and epithelial-derived cell lines in culture indicate that secretion of osteopontin can be dramatically increased when these cells are treated with phorbol esters, growth factors and hormones. However, osteopontin does not appear to be expressed by mesenchymal cells, fibroblasts, epidermal cells or by most epithelial cells in vivo.
骨桥蛋白是一种分子量约为41,500道尔顿的酸性糖蛋白,已从大鼠、人和牛的骨骼中分离出来。它富含天冬氨酸、谷氨酸和丝氨酸,含有约30种单糖,包括10种唾液酸。几种类型的数据表明,碳水化合物以1个N-糖苷和5-6个O-糖苷的形式存在,而磷酸盐以12个磷酸丝氨酸和1个磷酸苏氨酸的形式存在。cDNA序列显示存在与纤连蛋白中的细胞结合序列相同的甘氨酸-精氨酸-甘氨酸-天冬氨酸-丝氨酸-(GRGDS)氨基酸序列,这表明骨桥蛋白可能作为细胞黏附因子发挥作用。许多研究支持这一结论,这些研究表明该蛋白促进成纤维细胞和成骨细胞附着于基质并铺展,并且这种附着被含RGD的肽所抑制。尽管有证据表明它含有RGD识别序列并且可能与称为整合素的受体家族相互作用,但骨桥蛋白似乎不具有胶原结合结构域。骨桥蛋白由前成骨细胞、成骨细胞和骨细胞合成,分泌到类骨质中并整合到骨中。在发育早期的表达表明骨桥蛋白是骨形成中的重要成分。用1,25-二羟维生素D3和转化生长因子-β处理培养的成骨细胞,可增加其骨桥蛋白的合成水平。这些试剂的作用在转录水平。除了骨细胞外,内耳、脑、肾、蜕膜和胎盘的骨外细胞也合成骨桥蛋白。成牙本质细胞、某些骨髓细胞和肥大软骨细胞也能合成骨桥蛋白。对几种培养的成纤维细胞和上皮来源的细胞系的研究表明,当这些细胞用佛波酯、生长因子和激素处理时,骨桥蛋白的分泌会显著增加。然而,在体内,间充质细胞、成纤维细胞、表皮细胞或大多数上皮细胞似乎不表达骨桥蛋白。