Nieuw Amerongen A V, Bolscher J G, Bloemena E, Veerman E C
Dept. of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), The Netherlands.
Biol Chem. 1998 Jan;379(1):1-18. doi: 10.1515/bchm.1998.379.1.1.
Mucins are widely distributed in mucous secretion fluids or are associated with plasma membranes. Up to now 9 genes of epithelial mucins have been identified, distributed over five chromosomes. Superposed on the genetic diversity, each type of mucin displays heterogeneity in oligosaccharide composition, including the terminal sugar residues. On top of that there is variation between individuals brought about by blood group antigens. Heterogeneity is further incited by the degree of sulfation. This tremendous structural heterogeneity endows mucin molecules with properties suggestive for a multifunctional role. The major biological function assigned to mucins is still the protection of tissues covered by the mucous gel. Current knowledge on the specific biological functions of the sulfate residues is fragmentary and periphrastic. Glycosylation including sulfation appears to be subject to modification under pathological conditions. There is evidence that sulfation rate-limits bacterial degradation of mucins. Moreover, accumulating data focus towards their involvement in recognition phenomena. Sulfate residues on blood group related structures provoke specific epitopes for selective interaction with microorganisms e.g. Helicobacter pylori. A distinct class of mucins acts as ligands for selectins, crucial in cellular recognition processes like cellular homing of lymphocytes. Whereas in earlier days mucins were only seen as water-binding molecules, protecting the underlying mucosa against harmful agents, the current picture of these molecules is characterized by the selective interaction with their environment, including epithelial-, and endothelial cells and microorganisms, thereby regulating a great number of biological processes. However, the specific role of sulfate remains to be further elucidated.
黏蛋白广泛分布于黏液分泌液中或与质膜相关。到目前为止,已鉴定出9种上皮黏蛋白基因,分布在5条染色体上。除了遗传多样性外,每种类型的黏蛋白在寡糖组成上也表现出异质性,包括末端糖残基。除此之外,个体之间还存在由血型抗原引起的差异。硫酸化程度进一步加剧了异质性。这种巨大的结构异质性赋予黏蛋白分子具有多功能作用的特性。赋予黏蛋白的主要生物学功能仍然是保护被黏液凝胶覆盖的组织。目前关于硫酸根残基具体生物学功能的知识是零碎且冗长的。包括硫酸化在内的糖基化似乎在病理条件下会发生改变。有证据表明硫酸化限制了细菌对黏蛋白的降解。此外,越来越多的数据表明它们参与识别现象。血型相关结构上的硫酸根残基引发特定表位,用于与微生物(如幽门螺杆菌)进行选择性相互作用。一类独特的黏蛋白作为选择素的配体,在细胞识别过程(如淋巴细胞的细胞归巢)中起关键作用。在过去,黏蛋白仅被视为结合水的分子,保护下层黏膜免受有害物质侵害,而目前对这些分子的认识特点是它们与周围环境(包括上皮细胞、内皮细胞和微生物)的选择性相互作用,从而调节大量生物学过程。然而,硫酸根的具体作用仍有待进一步阐明。