癌症轉移是癌症病患致死的主要原因。在沒有辦法有效治療癌症的情況之下，提供一個有效阻斷癌症細胞擴散至全身各處將為病患帶來最大利益。癌細胞上的多聚體纖連蛋白(poly-fibronectin; poly-FN)與肺臟的血管內皮細胞膜上的細胞黏著接受器第四型雙胜肽蛋白水解酶(Dipeptidyl peptidase IV DPPIV; CD26)結合，是造成肺臟之臟器特異性轉移主因之ㄧ。我們試圖以阻斷DPPIV與FN兩個蛋白質的結合作為抑制癌症的策略之ㄧ，期望達到抑制癌細胞轉移的最終目的。之前我們已經在FN的羧基端找到一個保留性胺基酸序列之DPPIV結合位點，並且利用人工合成這段保留性序列，可以阻斷DPPIV與FN的結合並在動物實驗中有效抑制癌症細胞在肺部的轉移聚落。雖然抑制轉移的效果顯著，但是並沒有完全抑制轉移的聚落形成。我們探討眾多不能完全抑制轉移的原因，其中一個是癌細胞表面上FN存在有其他DPPIV的結合位點。的確，在還原狀態(reducing condition) 的Far-western 實驗中，FN 的胺基端水解片段(proteolytic FN) 29kDa[第一至第五個第一型重複區域(FNI(1-5)) ; N-29kDa]與45kDa [第六個第一型、第一個第二個第二型重複性區域及第七個至第九個第一型重複性區域FNI(6)II(1-2)I(7-9) ; N45kDa]的區域中也具有與DPPIV結合的能力。為了找出這些結合位點，我們利用Maltose binding protein (MBP)重組蛋白去表現 FN的N端片段，來篩選出具有DPPIV結合能力之片段。首先我們證實FN重組蛋白與FN水解片段同樣具有與DPPIV的結合能力。由此我們便可利用此系統去縮小FN上可以與DPPIV結合的位點。在實驗結果中顯示，在N-29kDa的區域中，FNI(1)、FNI(2)、FNI(3)、FNI(4)；N-45kDa的區域中，FNI(6)、FNI(7)、FNI(8)可與DPPIV結合。這些DPPIV結合能力全部屬於第一型重複區域。未來的工作乃是一一把這些重複區域中的位點或一個保留性位點序列找出，盼望將來能藉此設計有效藥物來抑制FN的N端、C端與DPPIV的結合，以提供阻斷癌症轉移的新策略。

Most cancer mortality is attributed to metastatic disease rather than the primary tumor. To metastasize successfully, the cancer cells traveling in the circulation must first adhere to blood vessel wall in an organ specific manner. We have demonstrated that Dipeptidyl peptidase IV (DPPIV; CD26) expressed on lung endothelial cells serves as an adhesion receptor of polymeric fibronectin (poly-FN) on the surfaces of metastatic breast cancer cells (MTF7) in a lung-specific rat breast cancer metastasis model. Blocking the binding between DPPIV and FN is an ideal strategy of pulmonary metastasis prevention. We have previously identified a novel consensus DPPIV-binding site (DBS) in the C-terminal of FN, according to the sequence of which a recombinant DPPIV-binding peptide was purified for in vivo breast cancer cell colonization inhibition. Although the inhibitory effect was significant, this peptide did not completely impede the tumor colony formation. One possible explanation for this incompleteness is the existence of other DPPIV-binding regions in FN. The fact that, during testing the DPPIV-binding activity of FN fragments by far-western assay, we accidentally found additional DBS(s) in the N-terminal of the proteolytic FN fragments of 29kDa [FNI(1-5); N-29kDa] and of 45kDa [FNI(6)II(1-2)I(7-9);N45kDa] under reducing condition strengthen the above-mentioned possibility. By conducting additional far-western assay, we were able to narrow down the DBS(s) in the recombinant Maltose-Binding Protein [MBP]-fusion N-terminal FN fragments. We also demonstrated the DPPIV-binding activity of the recombinant FN is similar to that of proteolytic FN. In our results, both the individual fragments of N-29kDa [FNI(1), FNI(2), FNI(3) and FNI(4)] and N-45kDa [FNI(6), FNI(7) and FNI(8) ] can interact with DPPIV. In the future, we determine to find out either various DBS(s) or a consensus motif in these fragments, from which we hope to design specific inhibitors to effectively inhibit cancer metastasis by abolishing the interaction between C,N terminal domain of FN and DPPIV.

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洪婷婷「定位大鼠第四型雙肽蛋白水解酶其細胞外區域中之纖連蛋白及單株抗體6A3的結合位點」，國立成功大學，碩士論文(2007)。