收藏品
肺表面活性物质
促炎细胞因子
先天免疫系统
表面活性蛋白A
炎症
化学
表面活性蛋白D
免疫学
生物
生物化学
免疫系统
细胞生物学
作者
Sadis Matalon,Judy M. Hickman‐Davis,Jo Rae Wright
出处
期刊:Elsevier eBooks
[Elsevier]
日期:2006-01-01
卷期号:: 143-148
被引量:1
标识
DOI:10.1016/b0-12-370879-6/00377-x
摘要
Surfactant protein A (SP-A), the most abundant apoprotein of pulmonary surfactant, is a hydrophilic hybrid molecule that belongs to the Ca2+-dependent animal lectin superfamily termed collectins. Collectins are carbohydrate-binding proteins other than antibodies and enzymes that share the common structural characteristics of an N-terminal collagen-like domain connected to a Ca2+-dependent carbohydrate-recognition domain. SP-A has multiple functions including participating in tubular myelin formation, regulating the recycling of surfactant lipids, and acting synergistically with the two lipophilic surfactant apoproteins to lower surface tension. In addition, SP-A plays a major role in host defense of the lung: it is an essential component of innate immunity and helps to activate acquired immunity. SP-A can act either as a proinflammatory or anti-inflammatory agent, increasing or decreasing production of inflammatory cytokines by inflammatory cells to either enhance pathogen killing or suppress inflammation under basal conditions. Finally, it has been shown that SP-A levels are altered during a number of disease states including adult respiratory distress syndrome (ARDS) and cystic fibrosis. Concomitantly, exposure of SP-A to severe inflammation may cause oxidation or nitration of the protein and result in inactivation. Inactivation of SP-A during disease states may therefore cause increased susceptibility to secondary lung infections.
科研通智能强力驱动
Strongly Powered by AbleSci AI