臺灣博碩士論文加值系統

人類介白素1 (Interleukin-1, IL-1)藉由訊息傳遞活化下游轉錄因子如NF-kappaB，調控眾多基因之表現。IL-1在發炎反應與調控免疫反應中，扮演相當重要的角色。IL-1與IL-1R結合需要IL-1RAcP，過去發現的膜型IL-1RAcP為一個具有570個胺基酸的蛋白 (稱為IL-1RAcP570)。實驗室之前發現另有一個具有687個胺基酸的IL-1RAcP (稱為IL-1RAcP687)，其胺端包含細胞外側免疫球蛋白區域、跨膜區域與細胞內側TIR區域Box 1及Box 2的448個胺基酸與IL-1RAcP570一致，而羧端包含TIR區域Box 3的239個胺基酸為其特有。
IL-1RAcP687如IL-1RAcP570般可與IL-1RI作用，且IL-1beta可促進此交互作用；IL-1RAcP687如IL-1RAcP570般可與Tollip作用，且此作用不需IL-1RI，亦不受IL-1beta影響；IL-1RAcP687和MyD88之作用則和IL-1RAcP570非常不同，IL-1RAcP570和MyD88之交互作用需要IL-1RI，且IL-1beta會大為促進此交互作用，而IL-1RAcP687和MyD88之交互作用則不需要IL-1RI，且IL-1beta亦不會促進此交互作用。另外，與IL-1RI同時表現時，IL-1RAcP687如IL-1RAcP570般，可促進NF-kappaB活化。綜而言之，IL-1RAcP687如IL-1RAcP570般，可以與IL-1訊息傳遞途徑最上游的IL-1RI、Tollip和MyD88有交互作用，也能傳遞訊息、活化轉錄因子NF-kappaB。

Interleukin-1 (IL-1) regulates the expression of many genes by activating transcription factors, such as NF-kappaB. IL-1 plays an important role in inflammation and immune response. IL-1 receptor accessory protein (IL-1RAcP) is essential for IL-1 signaling. Previously, the membrane form of IL-1RAcP was identified as a 570-amino acid protein (named IL-1RAcP570). Interestringly, another membrane form of IL-1RAcP with 687 amino acids (named IL-1RAcP687) was identified by our lab. The N-terminal 448 amino acids of IL-1RAcP687, containing Ig domains, transmembrane domain, and Box 1 and Box 2 of TIR domain, are identical to those of IL-1RAcP570. In constrast, the C-terminal 239 amino acids of IL-1RAcP687, containing Box 3 of TIR domain, are unique.
Similar to IL-1RAcP570, IL-1RAcP687 interacts with IL-1RI, and the interaction between IL-1RAcP687 and IL-1RI can be enhanced by IL-1beta. Like IL-1RAcP570, IL-1RAcP687 also interacts with Tollip, and this interaction does not require IL-1RI. Furthermore, this interaction is not induced by IL-1beta stimulation. The interaction between IL-1RAcP687 and MyD88 is dramatically different from the interaction between IL-1RAcP570 and MyD88. IL-1RI is required for IL-1RAcP570 to interact with MyD88, and this interaction is induced by IL-1beta stimulation. In contrast, IL-1RAcP687 interacts with MyD88 without IL-1RI, and IL-1beta stimulation has no significant effect on the interaction between IL-1RAcP687 and MyD88. Moreover, either IL-1RAcP687 or IL-1RAcP570 co-expressed with IL-1RI activates the transcription factor NF-kappaB. In summary, IL-1RAcP687, like IL-1RAcP570, interacts with the proteins involved in the upstream IL-1 signaling pathway such as IL-1RI, Tollip, and MyD88 and transduces signal to activate transcription factor NF-kappaB.

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