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I 组 p21 激活激酶在白血病细胞黏附纤维连接蛋白中的作用。

Group I p21-activated kinases in leukemia cell adhesion to fibronectin.

机构信息

Department of Proteomics, Institute of Hematology and Blood Transfusion , Prague, Czech Republic.

出版信息

Cell Adh Migr. 2021 Dec;15(1):18-36. doi: 10.1080/19336918.2021.1872760.

DOI:10.1080/19336918.2021.1872760
PMID:33464167
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7834095/
Abstract

P21-activated kinases (PAK) regulate processes associated with cytoskeleton dynamics. PAK expression in leukemia cells was measured on protein and mRNA levels. In functional assays, we analyzed the effect of PAK inhibitors IPA-3 and FRAX597 on cell adhesivity and viability. PAK2 was dominant in cell lines, whereas primary cells also expressed comparable amount of PAK1 transcription isoforms: PAK1-full and PAK1Δ15. PAK1Δ15 and PAK2 levels correlated with surface density of integrins β1 and αVβ3. PAK1-full, but not PAK2, was present in membrane protrusions. IPA-3, which prevents PAK activation, induced cell contraction in semi-adherent HEL cells only. FRAX597, which inhibits PAK kinase activity, increased cell-surface contact area in all leukemia cells. Both inhibitors reduced the stability of cell attachment and induced cell death.

摘要

P21 激活激酶 (PAK) 调节与细胞骨架动态相关的过程。在蛋白质和 mRNA 水平上测量白血病细胞中的 PAK 表达。在功能测定中，我们分析了 PAK 抑制剂 IPA-3 和 FRAX597 对细胞黏附性和活力的影响。PAK2 在细胞系中占优势，而原代细胞也表达相当数量的 PAK1 转录同工型：PAK1-full 和 PAK1Δ15。PAK1Δ15 和 PAK2 水平与整合素β1 和 αVβ3 的表面密度相关。PAK1-full，但不是 PAK2，存在于膜突中。IPA-3 可阻止 PAK 激活，仅在半贴壁 HEL 细胞中诱导细胞收缩。FRAX597 抑制 PAK 激酶活性，增加所有白血病细胞的细胞表面接触面积。两种抑制剂均降低细胞附着的稳定性并诱导细胞死亡。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/04e83b5190fa/KCAM_A_1872760_F0010_OC.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/d87e00df3130/KCAM_A_1872760_F0005_OC.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/d84d8298a171/KCAM_A_1872760_F0008_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/36f153f358c4/KCAM_A_1872760_F0009_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/04e83b5190fa/KCAM_A_1872760_F0010_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/93b4c012c481/KCAM_A_1872760_F0001_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/b4303679eb12/KCAM_A_1872760_F0002_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/a59fe0ce8174/KCAM_A_1872760_F0003_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/a6cd7290ce3b/KCAM_A_1872760_F0004_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/d87e00df3130/KCAM_A_1872760_F0005_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/deecbb9c70dc/KCAM_A_1872760_F0006_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/a3b8228c97a7/KCAM_A_1872760_F0007_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/d84d8298a171/KCAM_A_1872760_F0008_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/36f153f358c4/KCAM_A_1872760_F0009_B.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/65c0/7834095/04e83b5190fa/KCAM_A_1872760_F0010_OC.jpg

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