Either integrin subunit β1 or β3 is involved in mediating monocyte adhesion, IL-1β protein and mRNA expression in response to surfaces functionalized with fibronectin-derived peptides

Either integrin subunit β1 or β3 is involved in mediating monocyte adhesion, IL-1β protein and mRNA expression in response to surfaces functionalized with fibronectin-derived peptides
复制标题

DOI:
10.1163/156856207781034179
复制
发表时间:
2007-06-01
影响因子:
3.6
通讯作者:
Kao, Weiyuan John
Kao, Weiyuan John
中科院分区:
工程技术4区
文献类型:
--
作者:
Chung, Amy S.;Gao, Qiang;Kao, Weiyuan John

文献摘要

被引文献

相似文献

我们合成了以纤维连接蛋白(FN)衍生的多肽固定的明胶基互穿网络(IPN)支架,以评估单核细胞与生物材料的相互作用。将人原代单核细胞接种于经FN或FN衍生多肽预吸附的多肽接枝的IPN或组织培养聚苯乙烯(TCPS)上。在精氨酸-甘氨酸-天冬氨酸(RGD)多肽存在下,TCPS和IPN表面的单核细胞密度都较高。抗整合素β1或β3抗体可降低所有配体修饰的TCP和IPN上的单核细胞密度。改良TCPS上细胞的白介素1β(IL-1β)蛋白水平随时间降低。单核细胞在IPN作用下IL-1β的表达在24 h达到高峰,之后下降至168 h。无论是TCPS还是IPN样品,配体的同一性都不影响IL-1β的表达。经抗整合素β1或β3抗体处理后,TCPS和IPN标本的IL-1β水平均以非配体依赖的方式降低,尤其是在24 h,未经抗体处理的IPN标本的单核细胞IL-1βmRNA表达在2 h达到最高,并随着时间的推移逐渐下降。经抗整合素β1或β3抗体处理的细胞IL-1βmRNA的表达与未经抗体处理的细胞相似,但甲氧基嫁接的IPN样品除外。IL-1βmRNA表达的变化与蛋白表达的变化无相关性。结果表明,单核细胞的黏附受底物、RGD序列和含有整合素受体的β1或β3的影响。含有β1或β3的整合素受体也参与了附着在明胶生物材料表面的单核细胞中IL-1β基因和蛋白的表达。
We synthesized gelatin-based, interpenetrating network (IPN) scaffolds immobilized with fibronectin (FN)-derived peptides to assess monocyte-biomaterial interaction. Human primary monocytes were seeded onto peptide-grafted IPN or tissue-culture polystyrene (TCPS) pre-adsorbed with FN or FN-derived peptides. Monocyte cell density on both TCPS and IPN surfaces was higher in the presence of the arginine-glycine-aspartic acid (RGD) peptide. Pretreatment with anti-integrin beta 1 or beta 3 antibody decreased monocyte density on all ligand-modified TCPS and IPN. Interleukin-1 beta (IL-1 beta) protein levels of cells on modified TCPS decreased over time. IL-1 beta expression of monocytes in the presence of IPNs peaked at 24 h and then decreased through 168 h. Ligand identity did not affect IL-1 beta expression in either TCPS or IPN samples. Pretreatment with anti-integrin beta 1 or beta 3 antibody reduced IL-1 beta levels from both TCPS and IPN samples in a ligand-independent manner, particularly at 24 h. Monocytic IL-1 beta mRNA expression in IPN samples without antibody pretreatment was highest at 2 h and decreased over time. IL-1 beta mRNA expression in cells with anti-integrin beta 1 or beta 3 antibody pretreatment was similar to those without antibody pretreatment, except for methoxygrafted IPN samples. The change in IL-1 beta mRNA expression did not correlate with changes in protein expression. The results indicate that monocyte adhesion was affected by the substrate and the RGD sequence and beta 1 or beta 3 containing integrin receptors. beta 1-or beta 3-containing integrin receptors were also involved in IL-1 beta gene and protein expression in monocytes adhered to gelatin-based biomaterial surfaces.