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牙本质的细胞外基质蛋白

Extracellular matrix proteins of dentine.

作者信息

Butler W T, Ritchie H H, Bronckers A L

机构信息

Department of Basic Sciences, University of Texas-Houston Health Science Center 77030, USA.

出版信息

Ciba Found Symp. 1997;205:107-15; discussion 115-7. doi: 10.1002/9780470515303.ch8.

Abstract

Bone and dentine extracellular matrix proteins are similar, consisting primarily of type I collagen, acidic proteins and proteoglycans. Although collagen forms the lattice for deposition of calcium and phosphate for formation of carbonate apatite, the non-collagenous proteins are believed to control initiation and growth of the crystals. Despite this similarity, dentine contains three unique proteins apparently absent from bone and other tissue: dentine phosphophoryn (DPP), dentine matrix protein 1 (DMP1) and dentine sialoprotein (DSP). DPP and DMP1 are acidic phosphoproteins probably involved in the control of mineralization processes. DPP may localize in gap regions of collagen and initiate apatite crystal formation by binding large quantities of calcium in a conformation that promotes this process. Extensive studies have been conducted in our laboratory on the nature, biosynthesis, localization and gene structure of DSP. Immunolocalization studies showed that rat DSP, a 53 kDa sialic acid-rich glycoprotein, was synthesized by young and mature odontoblasts, and by dental pulp cells and pre-ameloblasts, but not by ameloblasts, osteoblasts, chondrocytes or other cell types. The cDNA sequence indicated that DSP was a 366-residue protein with several potential N-glycosylation sites, as well as phosphorylation sites, but that the amino acid sequence was dissimilar to that of other known proteins. Northern blot analysis detected several mRNA species near 4.6 and 1.5 kb, indicative of alternative splicing events. Evidence for two DSP genes was obtained, further complicating this picture. Recent in situ hybridization studies utilizing rat and mouse molars and incisors indicated that DSP mRNA was expressed by young odontoblasts and odontoblasts in animals of all ages. Transcripts were also observed in pre-ameloblasts. The expression of DSP mRNA ceased when these cells matured to become secretory ameloblasts. DSP transcripts were not detected in osteoblasts or other cell types. The transient expression in pre-ameloblasts suggests a role of epithelial-mesenchymal interactions in the formation of the tooth.

摘要

骨和牙本质的细胞外基质蛋白相似,主要由I型胶原蛋白、酸性蛋白和蛋白聚糖组成。虽然胶原蛋白形成了用于沉积钙和磷酸盐以形成碳酸磷灰石的晶格,但非胶原蛋白被认为控制着晶体的起始和生长。尽管存在这种相似性,但牙本质含有三种显然在骨和其他组织中不存在的独特蛋白质:牙本质磷蛋白(DPP)、牙本质基质蛋白1(DMP1)和牙本质涎蛋白(DSP)。DPP和DMP1是酸性磷蛋白,可能参与矿化过程的控制。DPP可能定位于胶原蛋白的间隙区域,并通过以促进该过程的构象结合大量钙来启动磷灰石晶体形成。我们实验室对DSP的性质、生物合成、定位和基因结构进行了广泛研究。免疫定位研究表明,大鼠DSP是一种53 kDa富含唾液酸的糖蛋白,由年轻和成熟的成牙本质细胞、牙髓细胞和前成釉细胞合成,但成釉细胞、成骨细胞、软骨细胞或其他细胞类型不合成。cDNA序列表明DSP是一种366个残基的蛋白质,有几个潜在的N-糖基化位点以及磷酸化位点,但氨基酸序列与其他已知蛋白质不同。Northern印迹分析检测到4.6和1.5 kb附近的几种mRNA种类,表明存在可变剪接事件。获得了两个DSP基因的证据,使情况更加复杂。最近利用大鼠和小鼠磨牙及切牙进行的原位杂交研究表明,DSP mRNA在所有年龄段动物的年轻成牙本质细胞和成牙本质细胞中表达。在前成釉细胞中也观察到转录本。当这些细胞成熟为分泌性成釉细胞时,DSP mRNA的表达停止。在成骨细胞或其他细胞类型中未检测到DSP转录本。在前成釉细胞中的瞬时表达表明上皮-间充质相互作用在牙齿形成中起作用。

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