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黏蛋白复合物:下颌下黏液糖蛋白“连接”成分的特性

Mucin complexes: characterization of the "link" component of submandibular mucus glycoprotein.

作者信息

Slomiany A, Tamura S, Grzelinska E, Piotrowski J, Slomiany B L

机构信息

Research Center, University of Medicine and Dentistry of New Jersey, NJDS, Newark 07103-2400.

出版信息

Int J Biochem. 1992 Jun;24(6):1003-15. doi: 10.1016/0020-711x(92)90111-d.

Abstract
  1. Analysis of the submandibular saliva revealed that the secretion consists of mucin complexed with 150 kDa fibronectin fragment and DNA. 2. The kallikreins, secreted by the submandibular gland, appear to be responsible for the fibronectin fragmentation, since an identical peptide was also generated when fibronectin was subjected to incubation with the submandibular saliva or the purified enzyme. 3. The results provide evidence that the 150 kDa glycopeptide so-called salivary mucin "link" component is neither an integral part of the mucin molecule, nor linked to mucin subunits by disulfide bonds, but is a fibronectin fragment which associates with mucin. 4. Using mucin monoclonal antibody (3G12), it was revealed that the nonglycosylated (naked) 8-12 kDa fragment of the mucin molecule is responsible for the interaction of mucin with other components of saliva. 5. Under physiological conditions, the interaction of mucin with fibronectin on the luminal surfaces may be relevant in building mucous barrier and protection of the delicate oral epithelium from damage.
摘要
  1. 对颌下唾液的分析显示,其分泌物由与150 kDa纤连蛋白片段及DNA复合的粘蛋白组成。2. 颌下腺分泌的激肽释放酶似乎是纤连蛋白片段化的原因,因为当纤连蛋白与颌下唾液或纯化的酶一起孵育时,也会产生相同的肽段。3. 结果证明,所谓唾液粘蛋白“连接”成分的150 kDa糖肽既不是粘蛋白分子的组成部分,也不是通过二硫键与粘蛋白亚基相连,而是与粘蛋白结合的纤连蛋白片段。4. 使用粘蛋白单克隆抗体(3G12)发现,粘蛋白分子的非糖基化(裸露)8 - 12 kDa片段负责粘蛋白与唾液其他成分的相互作用。5. 在生理条件下,管腔表面粘蛋白与纤连蛋白的相互作用可能与构建黏液屏障以及保护脆弱的口腔上皮免受损伤有关。

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