Target Name: ADAM11
NCBI ID: G4185
Review Report on ADAM11 Target / Biomarker Content of Review Report on ADAM11 Target / Biomarker
ADAM11
Other Name(s): ADAM metallopeptidase domain 11, transcript variant 1 | ADAM metallopeptidase domain 11 | Metalloproteinase-like, disintegrin-like, and cysteine-rich protein | metalloproteinase-like, disintegrin-like, and cysteine-rich protein | MDC | ADAM11 variant 1 | ADAM 11 | Disintegrin and metalloproteinase domain-containing protein 11 (isoform 1) | ADA11_HUMAN | Disintegrin and metalloproteinase domain-containing protein 11

ADAM11: A promising drug target and biomarker for cancer treatment

The discovery of ADAM11, a protein known for its role in metastasis and cancer progression, has sparked significant interest in the field of metastasis research. ADAM11 is a member of the ADAM family, which includes several enzymes involved in the regulation of cell signaling pathways. The metastatic potential of cancer cells is a major challenge in cancer treatment, and identifying potential drug targets is a critical step in the development of new therapies. In this article, we will explore the ADAM11 protein, its function in cancer progression, and its potential as a drug target.

Function and Interaction

ADAM11 is a 21-kDa protein that is expressed in various tissues, including breast, ovarian, and colorectal tissues. It is a key regulator of the Wnt/FGF signaling pathway, which is involved in cell proliferation, differentiation, and survival. The Wnt/FGF signaling pathway is a well-established player in cancer development, and alterations in its signaling have been implicated in the development and progression of numerous types of cancer.

ADAM11 functions as a negative regulator of the Wnt/FGF signaling pathway by preventing the activation of the transcription factor SMAD, which is critical for the development of the Wnt/FGF signaling pathway. SMAD is a transcription factor that plays a crucial role in the regulation of stem cell proliferation and the maintenance of stem cell self-renewal. When SMAD is activated, it promotes the transcription of genes involved in stem cell proliferation and differentiation, leading to the development of cancer. On the other hand, when SMAD is inhibited, it prevents the transcription of cancer-promoting genes.

ADAM11's role in the regulation of the Wnt/FGF signaling pathway is critical for the development and progression of cancer. Studies have shown that inhibition of ADAM11 has significant implications for cancer treatment. For example, several studies have shown that inhibition of ADAM11 can lead to the regression of cancer tumors in both preclinical models and human clinical trials. In addition, inhibition of ADAM11 has been shown to be effective in treating various types of cancer, including breast, ovarian, and colorectal cancers.

Potential as a Drug Target

The potential of ADAM11 as a drug target is significant due to its involvement in the regulation of the Wnt/FGF signaling pathway. Drugs that target this pathway, including inhibitors of SMAD, have been shown to be effective in treating various types of cancer. In addition, the inhibition of ADAM11 has been shown to be effective in treating cancer in preclinical models, and clinical trials are underway to evaluate its potential as a drug.

One of the main advantages of targeting ADAM11 is its dual inhibition of SMAD and its role in the regulation of the Wnt/FGF signaling pathway. This means that inhibition of ADAM11 can lead to the inhibition of both SMAD and the Wnt/FGF signaling pathway, which can result in a more comprehensive inhibition of cancer cell proliferation and survival.

Another advantage of targeting ADAM11 is its specificity for cancer cells. Studies have shown that ADAM11 is expressed in various types of cancer cells, including breast, ovarian, and colorectal cells, but not in normal tissues. This makes it a potential target for cancer treatment that is specific for cancer cells, rather than normal cells.

Current Status of Research

Current research on ADAM11 is focused on its potential as a drug target for cancer treatment. Several studies have shown that inhibition of ADAM11 has significant implications for the treatment of various types of cancer, including breast, ovarian, and colorectal cancers. These studies have shown that inhibition of ADAM11 can lead to the regression of cancer tumors in both preclinical models and human clinical trials.

In addition, several companies have developed compounds that target ADAM11 and are in the

Protein Name: ADAM Metallopeptidase Domain 11

Functions: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Required for localization of the potassium channel subunit proteins KCNA1/KV1.1 and KCNA2/KV1.2 at cerebellar cortex basket cell distal terminals, is thereby involved in ephaptic inhibitory synchronization of Purkinje cell firing and response to stress (By similarity). Plays a role in spatial learning and motor coordination (By similarity). Involved in the nociceptive pain response to chemical-derived stimulation (By similarity)

The "ADAM11 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about ADAM11 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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ADAM12 | ADAM15 | ADAM17 | ADAM18 | ADAM19 | ADAM1A | ADAM1B | ADAM2 | ADAM20 | ADAM20P1 | ADAM21 | ADAM21P1 | ADAM22 | ADAM23 | ADAM28 | ADAM29 | ADAM30 | ADAM32 | ADAM33 | ADAM3A | ADAM5 | ADAM6 | ADAM7 | ADAM7-AS1 | ADAM7-AS2 | ADAM8 | ADAM9 | ADAMDEC1 | ADAMTS1 | ADAMTS10 | ADAMTS12 | ADAMTS13 | ADAMTS14 | ADAMTS15 | ADAMTS16 | ADAMTS16-DT | ADAMTS17 | ADAMTS18 | ADAMTS19 | ADAMTS2 | ADAMTS20 | ADAMTS3 | ADAMTS4 | ADAMTS5 | ADAMTS6 | ADAMTS7 | ADAMTS7P1 | ADAMTS7P3 | ADAMTS7P4 | ADAMTS8 | ADAMTS9 | ADAMTS9-AS1 | ADAMTS9-AS2 | ADAMTSL1 | ADAMTSL2 | ADAMTSL3 | ADAMTSL4 | ADAMTSL4-AS1 | ADAMTSL5 | ADAP1 | ADAP2 | Adapter protein complex 5 | Adaptor-related protein complex 1 | Adaptor-related protein complex 2 | Adaptor-Related Protein Complex 3 | Adaptor-related protein complex 4 | ADAR | ADARB1 | ADARB2 | ADARB2-AS1 | ADAT1 | ADAT2 | ADAT3 | ADCK1 | ADCK2 | ADCK5 | ADCY1 | ADCY10 | ADCY10P1 | ADCY2 | ADCY3 | ADCY4 | ADCY5 | ADCY6 | ADCY7 | ADCY8 | ADCY9 | ADCYAP1 | ADCYAP1R1 | ADD1 | ADD2 | ADD3 | ADD3-AS1 | Adducin | Adenosine A2 receptor | Adenosine deaminase | Adenosine receptor | Adenylate Cyclase | ADGB | ADGB-DT