Zhai Z, Liu W, Kaur M, Luo Y, Domenico J, Samson J M, Shellman Y G, Norris D A, Dinarello C A, Spritz R A, Fujita M
Department of Dermatology, University of Colorado Denver SOM, Aurora, CO, USA.
Denver Veterans Affairs Medical Center, Denver, CO, USA.
Oncogene. 2017 Jul 6;36(27):3820-3830. doi: 10.1038/onc.2017.26. Epub 2017 Mar 6.
Inflammasomes are mediators of inflammation, and constitutively activated NLRP3 inflammasomes have been linked to interleukin-1β (IL-1β)-mediated tumorigenesis in human melanoma. Whereas NLRP3 regulation of caspase-1 activation requires the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD (caspase recruitment domain)), caspase-1 activation by another danger-signaling sensor NLRP1 does not require ASC because NLRP1 contains a C-terminal CARD domain that facilitates direct caspase-1 activation via CARD-CARD interaction. We hypothesized that NLRP1 has additional biological activities besides IL-1β maturation and investigated its role in melanoma tumorigenesis. NLRP1 expression in melanoma was confirmed by analysis of 216 melanoma tumors and 13 human melanoma cell lines. Unlike monocytic THP-1 cells with prominent nuclear localization of NLRP1, melanoma cells expressed NLRP1 mainly in the cytoplasm. Knocking down NLRP1 revealed a tumor-promoting property of NLRP1 both in vitro and in vivo. Mechanistic studies showed that caspase-1 activity, IL-1β production, IL-1β secretion and nuclear factor-kB activity were reduced by knocking down of NLRP1 in human metastatic melanoma cell lines 1205Lu and HS294T, indicating that NLRP1 inflammasomes are active in metastatic melanoma. However, unlike previous reports showing that NLRP1 enhances pyroptosis in macrophages, NLRP1 in melanoma behaved differently in the context of cell death. Knocking down NLRP1 increased caspase-2, -9 and -3/7 activities and promoted apoptosis in human melanoma cells. Immunoprecipitation revealed interaction of NLRP1 with CARD-containing caspase-2 and -9, whereas NLRP3 lacking a CARD motif did not interact with the caspases. Consistent with these findings, NLRP1 activation but not NLRP3 activation reduced caspase-2, -9 and -3/7 activities and provided protection against apoptosis in human melanoma cells, suggesting a suppressive role of NLRP1 in caspase-3/7 activation and apoptosis via interaction with caspase-2 and -9. In summary, we showed that NLRP1 promotes melanoma growth by enhancing inflammasome activation and suppressing apoptotic pathways. Our study demonstrates a tumor-promoting role of NLRP1 in cancer cells.
炎性小体是炎症的介质,组成性激活的NLRP3炎性小体与人类黑色素瘤中白细胞介素-1β(IL-1β)介导的肿瘤发生有关。虽然NLRP3对caspase-1激活的调节需要接头蛋白ASC(含半胱天冬酶募集结构域(CARD)的凋亡相关斑点样蛋白),但另一种危险信号传感器NLRP1对caspase-1的激活不需要ASC,因为NLRP1含有一个C末端CARD结构域,可通过CARD-CARD相互作用促进caspase-1的直接激活。我们推测NLRP1除了IL-1β成熟外还有其他生物学活性,并研究了其在黑色素瘤肿瘤发生中的作用。通过对216个黑色素瘤肿瘤和13个人类黑色素瘤细胞系的分析,证实了NLRP1在黑色素瘤中的表达。与NLRP1主要定位于细胞核的单核细胞THP-1细胞不同,黑色素瘤细胞中的NLRP1主要在细胞质中表达。敲低NLRP1揭示了其在体外和体内的肿瘤促进特性。机制研究表明,在人转移性黑色素瘤细胞系1205Lu和HS294T中,敲低NLRP1可降低caspase-1活性、IL-1β产生、IL-1β分泌和核因子-κB活性,表明NLRP1炎性小体在转移性黑色素瘤中具有活性。然而,与之前报道NLRP1增强巨噬细胞焦亡不同,黑色素瘤中的NLRP1在细胞死亡方面表现不同。敲低NLRP1可增加人黑色素瘤细胞中caspase-2、-9和-3/7的活性并促进其凋亡。免疫沉淀显示NLRP1与含CARD的caspase-2和-9相互作用,而缺乏CARD基序的NLRP3不与这些半胱天冬酶相互作用。与这些发现一致,NLRP1激活而非NLRP3激活可降低人黑色素瘤细胞中caspase-2、-9和-3/7的活性,并提供抗凋亡保护,提示NLRP1通过与caspase-2和-9相互作用对caspase-3/7激活和凋亡起抑制作用。总之,我们表明NLRP1通过增强炎性小体激活和抑制凋亡途径促进黑色素瘤生长。我们的研究证明了NLRP1在癌细胞中的肿瘤促进作用。