|CSC-DC001918||Panoply™ Human C1QBP Knockdown Stable Cell Line||Inquiry|
|CSC-SC001918||Panoply™ Human C1QBP Over-expressing Stable Cell Line||Inquiry|
|CDCB157590||Human C1QBP ORF clone (BC000435)||Inquiry|
|CDCB169942||Danio rerio C1QBP ORF Clone (NM_001017858)||Inquiry|
|CDCL182963||Mouse C1QBP ORF clone(NM_007573.2)||Inquiry|
|CDCR280217||Human C1QBP ORF Clone(NM_001212.3)||Inquiry|
|CDCR378554||Rat C1qbp ORF Clone(NM_019259.2)||Inquiry|
|CDCS409713||Human C1QBP ORF Clone (BC000435)||Inquiry|
|CDFH002286||Human C1QBP cDNA Clone(NM_001212.3)||Inquiry|
|CDFR011551||Rat C1qbp cDNA Clone(NM_019259.2)||Inquiry|
|MiUTR1H-01284||C1QBP miRNA 3'UTR clone||Inquiry|
|MiUTR1M-02352||C1QBP miRNA 3'UTR clone||Inquiry|
|MiUTR1R-00639||C1QBP miRNA 3'UTR clone||Inquiry|
|SHG120441||shRNA set against Rat C1qbp(NM_019259.2)||Inquiry|
|SHG120517||shRNA set against Mouse C1qbp(NM_007573.2)||Inquiry|
|SHG120553||shRNA set against Human C1QBP(NM_001212.3)||Inquiry|
|SHH250697||shRNA set against Human C1QBP (NM_001212.3)||Inquiry|
|SHH250701||shRNA set against Mouse C1QBP (NM_007573.2)||Inquiry|
|SHH250705||shRNA set against Rat C1QBP (NM_019259.2)||Inquiry|
|SHW008467||shRNA set against Danio rerio C1QBP (NM_001017858)||Inquiry|
Recent Research Progress
Complement component 1q subcomponent binding protein (C1QBP), also known as HABP1, p32 and gC1qR, is a ubiquitously expressed, multi-ligand-binding, multi-compartmental cellular protein involved in various ligand-mediated cellular responses. It is widely distributed in the mitochondria, nucleus, cytoplasm, Golgi apparatus and cell membrane, and can be secreted into the extracellular matrix. According to reports, C1QBP is involved in tumorigenesis and cancer progression in various malignancies.
C1QBP and RCC
Renal cell carcinoma (RCC) is the most common kidney tumor arising from the cells in the lining of the kidney tubules. Early studies have shown that androgen receptor (AR) may play a key role in promoting the progression of RCC; however, the detailed mechanism remains unclear. Recent studies have demonstrated higher the nuclease-sensitive element-binding protein 1 (YBX1) expression with lower C1QBP expression in human RCC clinical tissues, and the intensity of C1QBP was inversely correlated with YBX1 nuclear expression. Mechanism anatomy revealed that C1QBP can interact with YBX1 to inhibit YBX1 activation by altering YBX1 phosphorylation and nuclear translocation in RCC cells. The consequences of such suppression of YBX1 may result in inhibition of RCC cell migration and invasion, which involves altering the AR-regulated MMP9 signals. Interruption of this newly identified C1QBP → YBX1 → AR → MMP9-suppressed RCC cell invasion pathway by targeting YBX1 or AR partially reversed the RCC cell invasion. Importantly, results from in vivo mouse model with orthotopic implantation of RCC OSRC2 cells into the left renal capsule also confirmed in vitro cell line studies showing targeting YBX1 could inhibit RCC cell invasion via regulation of AR/MMP9 signals. Collectively, these data indicate that C1QBP can modulate YBX1 to suppress AR-enhanced RCC cell invasion. This newly discovered C1QBP / YBX1 / AR / MMP9 signaling pathway may provide a new potential therapy to better inhibit RCC metastasis.
C1QBP and HSV-1
As a large double-stranded DNA virus, herpes simplex virus type 1 (HSV-1) assembles a capsid in the nucleus where virus particles exit by budding through the inner membrane. Although many viruses and host proteins are involved, the mechanism of viral export not well understood. Recently, when looking for host interacting proteins of ICP34.5, which is a virulence factor of HSV-1, the scholars identified the cellular protein C1QBP by spectrophotometer analysis. When expressed, ICP34.5 is associated with C1QBP in mammalian cells. After HSV-1 infection, C1QBP is recruited to the inner nuclear membrane by ICP34.5, which is parallel to phosphorylation and rearrangement of the nuclear layer. Knockdown of C1QBP in HSV-1 infected cells significantly reduced the production of cell-free virus, indicating that C1QBP is the mediator of HSV-1 nuclear export. These observations indicate that the interaction between HSV-1 ICP34.5 and C1QBP results in disintegration of the nuclear layer and promotes nuclear export of HSV-1 particles.
C1QBP and Pancreatic cancer
Pancreatic cancer shows a significant preference for hepatic metastasis. C1QBP can mediate growth factor-induced cancer cell chemotaxis and distant metastasis by activating receptor tyrosine kinases. Coincidentally, insulin-like growth factor-1 (IGF-1) derived from the liver and cancer cells itself has been identified as a key inducer of hepatic metastasis. Recent studies have confirmed a significant correlation between C1QBP expression and hepatic metastasis in patients with pancreatic cancer. IGF-1 induces the transfer of C1QBP from the cytoplasm to lipid rafts and further promotes the formation of the CD44 variant 6 (CD44v6)/C1QBP complex in pancreatic cancer cells. C1QBP interacts with CD44v6 in lipid rafts to promote phosphorylation of insulin-like growth factor-1 receptor (IGF-1R), thereby activating downstream phosphoinositide 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) signaling pathways, which mediate the metastatic potential of pancreatic cancer cells, including proliferation, apoptosis, invasion, adhesion and energy metabolism. In addition, C1QBP knockdown inhibited liver metastasis of pancreatic cancer cells in nude mice. Therefore, C1QBP in lipid rafts is considered to be a key regulator of IGF-1 / IGF-1R-induced liver metastasis in pancreatic cancer.
C1QBP and GC
Gastric cancer (GC) remains the fourth largest cancer and the second most deadly cancer in all cancers worldwide. Gao et al. have demonstrated that the expression of C1QBP protein in GC tissues was strongly higher than that in adjacent non-tumor tissues. Increased expression of C1QBP is highly correlated with tumor, node, and metastasis (TNM) stage, depth of invasion, lymph node metastasis, liver metastasis, peritoneal metastasis and poor prognosis, suggesting that C1QBP protein may be an important biomarker for tumor progression and prognosis in patients with GC.
C1QBP and Brain cancer
Recently, some studies have shown that C1QBP in the stimulation of glutamine metabolism by Myc in brain tumors. C1QBP has been shown to be a direct transcriptional target of Myc and its expression contributes to Myc-induced glutamine addiction in cancer cells. C1QBP levels increase in various brain cancers and they are closely related to malignancy grade and Myc expression levels. Attenuation of C1QBP expression in glioma cell lines and patient-derived human glioma cells impairs cell growth in vitro and tumor development in vivo. Taken together, these data provide more mechanistic insight into the reprogramming of glutamine metabolism and how is sustained in the pathogenesis of brain tumors.
C1QBP and BC
Breast cancer (BC) accounts for an estimated 1.38 million of total new cancer cases worldwide, making this disease the most common cancer in the female population. It has been reported that higher C1QBP mRNA levels were observed in tissues from BC patients with lower survival rate and lymph node metastasis. Furthermore, the expression of C1QBP is associated with higher proliferation and motility in BC in vitro. Recently, the C1QBP protein has been shown to be involved in distant metastasis of BC. The same investigator showed that the protein kinase C ξ is an interaction partner of C1QBP that activates the chemotaxis of BC cells.
In conclusion, the abnormal expression of C1QBP is closely related to the progression of various tumors, including RCC, Pancreatic cancer, GC and BC. Therefore, further research on C1QBP is undoubtedly very necessary and valuable.
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