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- Table of Contents
Facts about C-Jun-amino-terminal kinase-interacting protein 4.
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Human | |
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Gene Name: | SPAG9 |
Uniprot: | O60271 |
Entrez: | 9043 |
Belongs to: |
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JIP scaffold family |
Cancer/testis antigen 89; c-Jun NH2-terminal kinase-associated leucine zipper protein; C-Jun-amino-terminal kinase-interacting protein 4; CT89JIP4; FLJ14006; FLJ26141; FLJ34602; HLC4; HLC-6; HSS; Human lung cancer oncogene 6 protein; JLPPHETSYD1FLJ13450; JNK interacting protein; JNK/SAPK-associated protein; JNK-associated leucine-zipper protein; JNK-interacting protein 4; KIAA0516JIP-4; lung cancer oncogene 4; MAPK8IP4; Max-binding protein; MGC117291; MGC14967; MGC74461; Mitogen-activated protein kinase 8-interacting protein 4; PIG6; proliferation-inducing gene 6; Proliferation-inducing protei
Mass (kDA):
146.205 kDA
Human | |
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Location: | 17q21.33 |
Sequence: | 17; NC_000017.11 (50962174..51120868, complement) |
Isoform 5 is expressed only in testis on the round spermatids of stage I, II and II. Isoform 5 is absent in spermatogonia and spermatocyte. Isoform 3 is expressed in testis. Isoform 4 is expressed in testis and in acute myeloid leukemia (AML) patients.
Cytoplasm. Cytoplasm, perinuclear region. Lysosome membrane. Perinuclear distribution in response to stress signals such as UV radiation.; [Isoform 5]: Cytoplasmic vesicle, secretory vesicle, acrosome. Associated with the plasma membrane of the acrosomal compartment and also localizes in the acrosome matrix.
SPAG9 has emerged as a potential molecular target for cancer treatments. The SPAG9 protein has several applications, ranging from diagnostic markers to therapeutic interventions. Read on to find out the best uses of SPAG9 in lung cancer research. Also known as SPAG9a, SPAG9b is a relatively new gene that may be a promising therapeutic target for cancer patients.
The expression of SPAG9 protein is found in several different types of cancers, including basal cell carcinoma, adenocarcinoma not otherwise specified (ANCT), and polymorphous low-grade adenocarcinoma of SGT. In an IHC study, SPAG9 protein was detected in 80% of cases and in 10% of cells. Control IgG failed to demonstrate immunoreactivity against SPAG9 protein.
In addition, SPAG9 regulates the survival of tumor cells via p38 signaling. This pathway changes epithelial-mesenchymal transition (EMT) proteins and cell cycle proteins, reducing EMT and increasing DNA damage. Additionally, in vivo xenograft studies revealed that SPAG9 shRNA suppressed tumor growth in ovarian cancer patients.
The presence of anti-SPAG9 antibodies was detected in different tumor histotypes. The study also showed that SPAG9 antibody was detected in 60% of ten patients with benign tumors. It was also found in 72% of 18 patients with polymorphous low-grade adenocarcinoma. Statistical significance was not observed, but the findings show that SPAG9 has the potential to be a novel molecular target for novel cancer treatment modalities.
Although SPAG9 is a candidate for new treatments, it does not co-localize with the nuclear envelope. Unlike other proteins, it does not co-localize with the nuclear envelope. The authors note that this may be a significant difference between patients. This may suggest a role for SPAG9 as a biomarker for cancer. However, further study is needed to determine whether SPAG9 is a viable molecular target for novel cancer treatments.
Knockdown of SPAG9 inhibits HCC cell invasion. Inhibition of SPAG9 inhibits migration and invasion in HuH7 and HCCLM3 cells. This finding supports the hypothesis that SPAG9 could be a molecular target for novel cancer treatment modalities. This study is supported by the National Science Foundation of China and the Medicines Health Platform Key Project of Zhejiang Province. The authors declared no conflicts of interest.
Among other variables, tumor size did not significantly affect SPAG9 expression. Furthermore, estrogen receptor status and progesterone receptor status did not influence SPAG9 expression in HepG2 cells. But the results showed that SPAG9 is an upstream target of JNK. This study is important in predicting novel cancer treatment modalities. The study will continue to inform the field.
Previous studies have indicated that SPAG9 is a novel molecular target for the development of new modalities for treating cancer. This research has also led to a reduction in tumor growth and size in a mouse model of ovarian cancer. It has the potential to become an important molecular target in the treatment of liver cancer. So, it is time to develop novel treatment modalities for SPAG9-positive ovarian cancer.
After removing traces of cells, SPAG9 was immunoblotted using a monoclonal antibody against SPAG9. The anti-SPAG9 antibodies were used to detect a variety of protein oligomerizations. The secondary antibodies were donkey anti-rabbit antibody and rabbit anti-PCNA antibody. These antibodies were added to resuspended protein A/G agarose beads.
The present study examined the possibility of SPAG9 as a diagnostic marker for lung cancer by examining the protein expression in a sample from each patient. Twenty patients were enrolled and samples from adjacent non-cancerous tissue were also analyzed. Results revealed that 16 patients (20%) showed positive staining of SPAG9 in lung cancer tissue. The protein is located in the cytoplasm, and there were no positive cells detected in adjacent non-cancerous tissues.
For the present study, we used a reagent kit from RevertAid. The reagents contained cDNA, which was synthesized with the help of RevertAid M-MulV cDNA Synthesis kit. Using Primer 3.0 software, we designed primers specific for SPAG9 to be amplified by PCR. Primer sets of GAPDH were used as internal controls, and their specificity was verified using the SPAG9-specific primers.
In the present study, we showed the feasibility of using SPAG9 as a diagnostic marker for lung cancer by analyzing serial tissue sections from ANCT patients and healthy donors. We found that SPAG9 expression was highly correlated with malignant stage. Hence, SPAG9 is an excellent diagnostic marker for lung cancer. This study is the first of its kind to confirm SPAG9 as a lung cancer diagnostic marker.
Moreover, SPAG9 may have prognostic value for cancer patients, indicating tumor invasiveness. This may be because it increases the size of tumors. However, other studies have linked SPAG9 with TNM staging, which is helpful for determining the tumor's aggressiveness. And, if it can be accurately detected, it will help to improve the diagnostic accuracy of the invasiveness of the disease.
The current study demonstrates that serum SPAG9 IgG antibody levels in lung cancer patients were significantly higher than those in healthy controls. The difference was not related to stage of disease. Treatment-resistant patients had lower levels than healthy controls. In contrast, the patients with lung cancer who were treated with chemotherapy or radiation had higher SPAG9 levels than those without. Therefore, SPAG9 is a new diagnostic marker for lung cancer.
Moreover, SPAG9 induces a robust humoral response in HCC patients. Inhibition of SPAG9 induces increased serum levels of antibodies against SPAG9. This could be helpful in the early detection of lung cancer. These antibodies may also aid in the treatment of patients with SGT. However, further research is needed before this test can be widely used as a diagnostic marker. However, there are currently no definitive tests for SPAG9.
Sperm-associated antigen 9 (SPAG9) is overexpressed in lung cancer tissues. Patients with lung cancer also exhibit elevated levels of SPAG9 autoantibodies. The high SPAG9 levels in lung cancer tissues make it an effective diagnostic marker for lung cancer. This biomarker is highly accurate for early diagnosis of the disease, and it can predict the progression of lung cancer.
A recent study revealed that the expression of SPAG9 in breast cancer cells is related to the hormone receptor status of the cancer cells. The researchers then investigated the expression levels of SPAG9 in various breast cancer cell subtypes using real-time PCR, Western blotting, and indirect immunofluorescence. Finally, they conducted SPAG9 knockdown in triple-negative breast cancer cells to investigate the malignant properties of the protein in vitro.
The researchers used a lipofectamine reagent to transiently transfect MDA-MB-231 cells with control siRNA or SPAG9 siRNA. They also used a digital caliper to measure the diameter of the cells and their volume. The cells were then fixed and embedded in paraffin, and sections were prepared for histological analysis.
There are many challenges facing clinical research regarding breast cancer. This disease is highly prevalent in women and has the highest mortality rate in developing countries. It is characterized by distinct molecular subtypes and is associated with different prognostic factors. To combat this disease, innovative molecular-targeted treatments are needed. With the advancement of technology, it has become easier to fight this disease.
The researchers used a xenograft model of breast cancer to test the effectiveness of this drug. The SPAG9 siRNA plasmid significantly reduced tumor volume and tumor growth compared to the control siRNA-treated tumors. Further, immunohistochemical analysis revealed that SPAG9 siRNA significantly reduced the expression of PCNA, an antigen of breast cancer.
In vitro studies have shown that endogenous SPAG9 expression can be detected in several human breast cancer cell lines. These cell lines include MCF-7 and SK-BR-3 cells, which are ER+/PR+/Her2-associated luminal-A cell subtypes. However, no evidence has been reported for the presence of SPAG9 protein in normal mammary epithelial cells.
Recently, research has shown that SPAG9 is a new and promising target for cancer immunotherapy. It is thought to play a role in the progression and metastatic potential of BC. However, the cellular response to SPAG9 inhibition is highly variable and may depend on the type of cancer. In addition to SPAG9, other novel cancer immunotherapeutics targeting the hsa_circRPPh2_015 have been discovered.
PMID: 12391307 by Lee C.M., et al. JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors.
PMID: 16112646 by Guinn B.-A., et al. Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia.