反复切除下门牙诱导大鼠颌下腺特异性(LM)蛋白的表达。

C Yagil, T Barka
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引用次数: 12

摘要

长期服用β -肾上腺素能激动剂异丙肾上腺素(IPR)会导致大鼠和小鼠腮腺和下颌骨腺明显增生/肥大,并伴随腺体和唾液成分的变化。在下颌唾液的改变中,显著的是13000 Mr蛋白的出现,称为LM(大移动)蛋白。反复切除下门牙也会引起大鼠大唾液腺肿大。在这项研究中,我们比较了IPR给药或牙齿截肢引起的大鼠下颌骨腺的增大与腺体提取物和唾液中LM蛋白的相对水平。每天2次给予盐酸IPR-HCl (40 mg/kg),连续5天或每周3次切除下门牙,连续3周,导致下颌骨腺重量增加2.2倍。截肢一周后,腺体重量增加1.4倍。对纯化的LM蛋白琼脂抗体进行双重免疫扩散,与知识产权处理大鼠和断牙大鼠的腺体提取物和唾液形成一条单一的沉淀线,表明反应抗原具有免疫学同一性。未处理大鼠腺体提取物或唾液均未见沉淀线。用抗lm抗体染色时,从知识产权处理或牙齿切除的大鼠获得的唾液的免疫印迹显示,sds -聚丙烯酰胺凝胶中具有相同电泳迁移率的单个蛋白带。使用针对纯化LM蛋白的抗体,采用固相酶联免疫吸收法测定腺体提取物和唾液中LM蛋白的相对浓度。(摘要删节250字)
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Induction of a specific (LM) protein in the submandibular gland of the rat by repeated amputation of the lower incisor teeth.

Chronic administration of the beta-adrenergic agonist isoproterenol (IPR) leads to marked hyperplastic/hypertrophic enlargements of the parotid and submandibular glands in rats and mice with concomitant changes in the composition of both the glands and the saliva. Conspicuous among the alterations of the submandibular saliva is the appearance of a 13,000 Mr protein, termed LM (large mobile) protein. Repeated amputation of the lower incisor teeth also causes enlargements of the major salivary glands in rats. In this study, we have compared the enlargements of submandibular glands of rats produced by IPR administration or teeth amputation with respect to the relative levels of the LM protein in gland extracts and saliva. Administration of IPR-HCl (40 mg/kg) twice daily for 5 days or amputation of the lower incisor teeth 3 times a week for 3 weeks resulted in a 2.2-fold increase in the weight of the submandibular gland. Amputation for one week led to a 1.4-fold increase in gland weight. Double immunodiffusion in agar antibodies against the purified LM protein gave a single precipitin line with gland extracts and saliva of IPR-treated and teeth-amputated rats, indicating immunological identity of the reacting antigens. No precipitin lines were seen with gland extracts or saliva of untreated rats. Immunoblots of pooled saliva obtained from IPR-treated or teeth-amputated rats revealed a single protein band of the same electrophoretic mobility in SDS-polyacrylamide gels when stained using anti-LM antibodies. The relative concentrations of LM protein in gland extracts and saliva were measured by a solid-phase enzyme-linked immunoabsorption assay using antibodies against the purified LM protein.(ABSTRACT TRUNCATED AT 250 WORDS)

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