A motif in metallopeptidase inhibitor decreases effectively the activity of macrophage metalloproteinases

IF 0.5 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS Current Proteomics Pub Date : 2022-03-04 DOI:10.2174/1570164619666220304162545

G. Esfandiari, G. Ghasempour, Naser Kakavandi, A. Soleimani, Borhan Rahimi, Elham Bahraini, M. Najafi, M. Khosravi

引用次数: 0

Abstract

The tissue remodeling process and cellular migration relate to the activities of matrix metalloproteinases (MMPs). The aim of this study was to investigate the effects of a predicted motif from TIMPs on the MMP-2 and MMP-9 activities secreted from the differentiated macrophages. The monocytes were isolated from the healthy individuals by RosetteSep kit and were differentiated into macrophages using M-CSF. A 4-amino acid motif (TCAP) was predicted using bioinformatics tools. Zymography technique was applied for the measurement of MMP activities. The docking studies were also investigated between MMPs, tetrapeptide, and Batimastat. The TCAP inhibited significantly the differentiated macrophage MMP-2 and MMP-9 activities (p=0.0001and p=0.01, respectively). The docking results suggested the some MMP amino acids are involved with both tetrapeptide (TCAP), and Batimastat, The data showed that the small motif (TCAP) of TIMPs inhibits effectively the MMP-2 activity.

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金属肽酶抑制剂中的一个基序可以有效地降低巨噬细胞金属蛋白酶的活性

组织重塑过程和细胞迁移与基质金属蛋白酶(MMPs)的活性有关。本研究的目的是研究TIMPs预测基序对分化巨噬细胞分泌的MMP-2和MMP-9活性的影响。使用RosetteSep试剂盒从健康个体中分离单核细胞，并使用M-CSF将其分化为巨噬细胞。利用生物信息学工具预测了一个4氨基酸基序(TCAP)。采用酶谱法测定MMP活性。还研究了MMPs、tetrapeptide和Batimastat之间的对接研究。TCAP显著抑制巨噬细胞MMP-2和MMP-9活性(p=0.0001和p=0.01)。对接结果表明，部分MMP氨基酸同时参与了四肽(TCAP)和Batimastat，数据表明TIMPs的小基序(TCAP)有效抑制了MMP-2的活性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Current Proteomics BIOCHEMICAL RESEARCH METHODS-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

1.60

自引率

0.00%

发文量

审稿时长

>0 weeks

期刊介绍： Research in the emerging field of proteomics is growing at an extremely rapid rate. The principal aim of Current Proteomics is to publish well-timed in-depth/mini review articles in this fast-expanding area on topics relevant and significant to the development of proteomics. Current Proteomics is an essential journal for everyone involved in proteomics and related fields in both academia and industry. Current Proteomics publishes in-depth/mini review articles in all aspects of the fast-expanding field of proteomics. All areas of proteomics are covered together with the methodology, software, databases, technological advances and applications of proteomics, including functional proteomics. Diverse technologies covered include but are not limited to: Protein separation and characterization techniques 2-D gel electrophoresis and image analysis Techniques for protein expression profiling including mass spectrometry-based methods and algorithms for correlative database searching Determination of co-translational and post- translational modification of proteins Protein/peptide microarrays Biomolecular interaction analysis Analysis of protein complexes Yeast two-hybrid projects Protein-protein interaction (protein interactome) pathways and cell signaling networks Systems biology Proteome informatics (bioinformatics) Knowledge integration and management tools High-throughput protein structural studies (using mass spectrometry, nuclear magnetic resonance and X-ray crystallography) High-throughput computational methods for protein 3-D structure as well as function determination Robotics, nanotechnology, and microfluidics.