THE CYSTEINE-RICH REGION OF DIPEPTIDYL PEPTIDASE-IV (CD 26) IS THE COLLAGEN-BINDING SITE
THE CYSTEINE-RICH REGION OF DIPEPTIDYL PEPTIDASE-IV (CD 26) IS THE COLLAGEN-BINDING SITE
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DOI：
10.1006/bbrc.1995.2782
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发表时间：
1995-12-05
影响因子：
3.1
通讯作者：
REUTTER, W
中科院分区：
文献类型：
--
作者：
LOSTER, K;ZEILINGER, K;REUTTER, W
整合型糖蛋白二肽基肽酶IV(DPP IV，CD26)的一个显著特性是与细胞外基质(ECM)蛋白的亲和力。通过体外结合实验，我们发现DPP IV与胶原蛋白结合；优先与I型和III型胶原蛋白结合，这两种胶原蛋白都以形成大的三螺旋结构域为特征。未观察到DPP IV与层粘连蛋白或纤维连接蛋白的结合。在I型胶原中，α-L(I)链是DPP IV最重要的结合配体。抗DPP IV的单抗(13.4)特异性地抑制了DPP IV与I型胶原的相互作用。多肽图谱和N末端测序表明，相应的表位位于DPP IV的半胱氨酸富集区。因此，我们推测DPP IV的胶原结合部位不同于位于分子C端的含有外肽酶活性的催化部位。(C)1995年学术出版社。
A remarkable property of the integral glycoprotein dipeptidyl peptidase IV (DPP IV, CD 26) is its affinity to proteins of the extracellular matrix (ECM). By in vitro binding assays we have shown that DPP IV binds to collagens; preferentially to the collagens I and III, which are both characterized by the formation of large triplehelical domains. No binding of DPP IV to laminin or fibronectin could be observed. Within collagen I, the alpha l(I) chain was found to be the most prominent binding ligand of DPP IV. A monoclonal anti DPP IV antibody (13.4) specifically inhibited the interaction of DPP IV with collagen I. Peptide mapping and N-terminal sequencing revealed that the corresponding epitope of mAb 13.4 is located in the cysteine-rich domain of DPP IV. We therefore conclude that the putative collagen binding site of DPP IV is different from the region of the catalytic site containing the exopeptidase activity, which is located at the C-terminal portion of the molecule. (C) 1995 Academic Press.