Target Name: GZMB
NCBI ID: G3002
Review Report on GZMB Target / Biomarker Content of Review Report on GZMB Target / Biomarker
GZMB
Other Name(s): Granzyme B (isoform 2) | CSP-B | T-cell serine protease 1-3E | cathepsin G-like 1 | human lymphocyte protein | GRAB_HUMAN | granzyme B | Lymphocyte protease | Fragmentin-2 | CGL-1 | CSPB | C11 | Granzyme B | granzyme B (granzyme 2, cytotoxic T-lymphocyte-associated serine esterase 1) | Granzyme-2 | Cathepsin G-like 1 | CTLA-1 | Granzyme B (granzyme 2, cytotoxic T-lymphocyte-associated serine esterase 1) | Cytotoxic serine protease B | Cytotoxic T-lymphocyte proteinase 2 | Human lymphocyte protein | SECT | Granzyme B, transcript variant 2 | CCPI | Fragmentin 2 | Granzyme B (isoform 1) | HLP | cytotoxic T-lymphocyte proteinase 2 | GZMB variant 1 | cytotoxic serine protease B | CGL1 | CTLA1 | CTSGL1 | fragmentin 2 | GZMB variant 2 | Granzyme B, transcript variant 1

GZMB: A Drug Target / Disease Biomarker

GZMB, or G protein-coupled receptor B subunit, is a protein that is expressed in many different tissues throughout the body. It is a member of the G protein-coupled receptor (GPCR) family, which is a large family of transmembrane proteins that play an important role in cellular signaling. GZMB is one of the subunits of the GPCR family and is expressed in the brain, heart, kidneys, and other tissues.

GZMB is involved in a wide range of physiological processes in the body, including sensory perception, neurotransmitter signaling, and regulation of ion channels. It is also involved in the development and progression of various diseases, including cancer.

Due to its involvement in so many important physiological processes, GZMB has been identified as a potential drug target. Researchers are actively searching for small molecules that can modulate the activity of GZMB and have developed a number of potential lead compounds. These compounds can be tested for their ability to interact with GZMB and have the potential to be used in a variety of therapeutic applications.

One of the challenges in studying GZMB as a drug target is its complex structure. GZMB is a large protein with 1,294 amino acid residues and contains multiple domains, including an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain is involved in cell adhesion and is thought to play a role in the regulation of GZMB activity. The transmembrane domain is responsible for the synthesis and regulation of the protein, while the intracellular domain is involved in the regulation of its stability and function.

In addition to its complex structure, GZMB is also known for its high stability and resistance to inhibition. This is thought to be due to the presence of multiple isoforms of GZMB, which are different forms of the protein that are produced by alternative splicing. These isoforms are able to function as distinct GPCR subunits and can interact with different agonists, making GZMB a versatile target for drug development.

GZMB has also been shown to play a role in the regulation of ion channels, which are responsible for the flow of electrical current through the cell membrane. GZMB is thought to regulate the activity of these channels and is involved in the regulation of muscle and nerve function. This is important for understanding the mechanisms of many neurological and psychiatric disorders, including epilepsy, Parkinson's disease, and schizophrenia.

In addition to its involvement in ion channels, GZMB is also involved in the regulation of neurotransmitter signaling. GZMB is a critical receptor for several neurotransmitters, including dopamine, serotonin, and nitric oxide. These neurotransmitters play important roles in cellular signaling and are involved in a wide range of physiological processes, including mood regulation, pain perception, and learning. The regulation of GZMB activity by these neurotransmitters is important for understanding the mechanisms of many psychiatric and neurological disorders.

GZMB is also involved in the regulation of cell adhesion and cell migration. GZMB is a critical receptor for several adhesion molecules, including cadherin and integrin. These molecules are involved in the formation of tight junctions, which are responsible for the separation of cells in tissues and are important for many physiological processes, including embryonic development and tissue repair. The regulation of GZMB activity by these adhesion molecules is important for understanding the mechanisms of many diseases, including cancer.

In addition to its roles in ion channels, neurotransmission, and cell adhesion, GZMB is also involved in the regulation of inflammation. GZMB is a critical receptor for several pro-inflammatory cytokines, including TNF-alpha and IL-1尾. These cytokines play important roles in the regulation of immune responses and are involved in the development of many inflammatory diseases, including cancer. The regulation

Protein Name: Granzyme B

Functions: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:3262682, PubMed:3263427, PubMed:1985927). It cleaves after Asp (PubMed:8258716, PubMed:1985927). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (PubMed:32188940, PubMed:31953257). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -9 and -10 (CASP3, CASP9 and CASP10, respectively) to give rise to active enzymes mediating apoptosis (PubMed:9852092). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity)

The "GZMB 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 GZMB 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

More Common Targets

GZMH | GZMK | GZMM | H1-0 | H1-1 | H1-10 | H1-10-AS1 | H1-2 | H1-3 | H1-4 | H1-5 | H1-6 | H1-7 | H1-8 | H1-9P | H19 | H19-ICR | H2AB1 | H2AB2 | H2AB3 | H2AC1 | H2AC11 | H2AC12 | H2AC13 | H2AC14 | H2AC15 | H2AC16 | H2AC17 | H2AC18 | H2AC20 | H2AC21 | H2AC25 | H2AC3P | H2AC4 | H2AC6 | H2AC7 | H2AJ | H2AP | H2AX | H2AZ1 | H2AZ1-DT | H2AZ2 | H2AZ2-DT | H2AZP2 | H2BC1 | H2BC10 | H2BC11 | H2BC12 | H2BC12L | H2BC13 | H2BC14 | H2BC15 | H2BC17 | H2BC18 | H2BC20P | H2BC21 | H2BC26 | H2BC27P | H2BC3 | H2BC4 | H2BC5 | H2BC6 | H2BC7 | H2BC8 | H2BC9 | H2BP1 | H2BP2 | H2BP3 | H2BW1 | H2BW2 | H2BW4P | H3-3A | H3-3B | H3-4 | H3-5 | H3-7 | H3C1 | H3C10 | H3C11 | H3C12 | H3C13 | H3C14 | H3C15 | H3C2 | H3C3 | H3C4 | H3C6 | H3C7 | H3C8 | H3P16 | H3P36 | H3P37 | H3P44 | H3P5 | H3P6 | H4C1 | H4C11 | H4C12 | H4C13 | H4C14