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pleiotrophin 以高度灵活和适应性的方式与糖胺聚糖相互作用。

Pleiotrophin interacts with glycosaminoglycans in a highly flexible and adaptable manner.

机构信息

School of Molecular Sciences, Arizona State University, Tempe, AZ, USA.

出版信息

FEBS Lett. 2021 Apr;595(7):925-941. doi: 10.1002/1873-3468.14052. Epub 2021 Feb 12.

DOI:10.1002/1873-3468.14052
PMID:33529353
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8631008/
Abstract

Pleiotrophin (PTN) is a potent mitogenic cytokine whose activities are controlled by its interactions with glycosaminoglycan (GAG). We examined the specificity of PTN for several types of GAG oligosaccharides. Our data indicate that the interaction of PTN with GAGs is dependent on the sulfation density of GAGs. Surprisingly, an acidic peptide also had similar interactions with PTN as GAGs. This shows that the interaction of PTN with anionic polymers is flexible and adaptable and that the charge density is the main determinant of the interaction. In addition, we show that PTN can compensate for the loss of its termini in interactions with heparin oligosaccharides, allowing it to maintain its affinity for GAGs in the absence of the termini. Taken together, these data provide valuable insight into the interactions of PTN with its proteoglycan receptors.

摘要

多效蛋白(PTN)是一种有效的有丝分裂原细胞因子,其活性受到与糖胺聚糖(GAG)相互作用的控制。我们研究了 PTN 与几种类型的 GAG 寡糖的特异性。我们的数据表明,PTN 与 GAG 的相互作用取决于 GAG 的硫酸化密度。令人惊讶的是,酸性肽也与 GAG 一样与 PTN 相互作用。这表明 PTN 与阴离子聚合物的相互作用是灵活和适应性的,并且电荷密度是相互作用的主要决定因素。此外,我们表明 PTN 可以补偿其与肝素寡糖相互作用时末端的缺失,使其在没有末端的情况下保持与 GAG 的亲和力。总之,这些数据为 PTN 与其蛋白聚糖受体的相互作用提供了有价值的见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/330fa10c0d70/nihms-1756999-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/d495512e7e21/nihms-1756999-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/36068aa00fb7/nihms-1756999-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/f4ab76b19f14/nihms-1756999-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/6cb50d8a2bb8/nihms-1756999-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/5e18bb01b73c/nihms-1756999-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/bbb51a5a231c/nihms-1756999-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/330fa10c0d70/nihms-1756999-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/d495512e7e21/nihms-1756999-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/36068aa00fb7/nihms-1756999-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/f4ab76b19f14/nihms-1756999-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/6cb50d8a2bb8/nihms-1756999-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/5e18bb01b73c/nihms-1756999-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/bbb51a5a231c/nihms-1756999-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c4f4/8631008/330fa10c0d70/nihms-1756999-f0007.jpg

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Methods Enzymol. 2018;607:217-240. doi: 10.1016/bs.mie.2018.05.016. Epub 2018 Jun 30.
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