Target Name: LEP
NCBI ID: G3952
Review Report on LEP Target / Biomarker Content of Review Report on LEP Target / Biomarker
LEP
Other Name(s): OB | LEP_HUMAN | Obese protein | obese protein | leptin (obesity homolog, mouse) | obese, mouse, homolog of | Obesity factor | OBS | LEPD | leptin (murine obesity homolog) | leptin | obesity factor | Leptin

LEP-2: Potential Drug Target for Cancer, Neurodegenerative Diseases and Autoimmune Disorders

LEP (Leucine-rich repeat-containing) protein 2 (LEP-2) is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. It is a member of the LEP family, which includes proteins that are characterized by the presence of a leucine repeat in their amino acid sequence.

LEP-2 is a 21-kDa protein that is expressed in the brain, heart, and kidneys. It is characterized by the presence of a leucine repeat in its amino acid sequence. The leucine repeat is a common structural motif that is found in a variety of proteins, including transcription factors, signaling proteins, and structural proteins.

LEP-2 has been shown to play a role in the development and progression of a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. It is also a potential drug target, with researchers studying its potential for use in treating these diseases.

One of the ways that LEP-2 may be involved in the development and progression of cancer is by promoting the growth and survival of cancer cells. LEP-2 has been shown to promote the formation of cancer cell aggregates, which can lead to the development of more invasive and deadly tumors.

Another way that LEP-2 may be involved in the development and progression of neurodegenerative diseases is by contributing to the loss of neural cells. LEP-2 has been shown to interact with the protein PDGF-BB, which is involved in the production of neurons and the maintenance of neural stem cells. The loss of PDGF-BB has been linked to a variety of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease.

LEP-2 may also be involved in the development and progression of autoimmune disorders, as it has been shown to play a role in the regulation of immune cell function. In addition, LEP-2 has been shown to contribute to the development of insulin resistance, a risk factor for a variety of diseases, including type 2 diabetes.

Despite these potential roles in a variety of diseases, LEP-2 is not yet a drug target. Researchers are still studying its potential mechanisms of action and developing strategies for its targeting. In addition, there is a need for further research to determine the safety and effectiveness of targeting LEP-2 as a drug or biomarker.

In conclusion, LEP-2 is a protein that is expressed in various tissues of the body and is known for its role in the development and progression of a variety of diseases. It is currently a drug target and is being studied for its potential use in treating these diseases. Further research is needed to determine its safety and effectiveness as a drug or biomarker.

Protein Name: Leptin

Functions: Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (PubMed:17344214, PubMed:15899045, PubMed:19688109). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity) (PubMed:8589726, PubMed:11460888, PubMed:19688109, PubMed:24340098, PubMed:25060689). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (PubMed:24340098). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity) (PubMed:17344214). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression (PubMed:18242580). Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) (PubMed:11460888). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells (PubMed:12504075). Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (PubMed:15899045, PubMed:19688109). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (PubMed:25060689)

The "LEP 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 LEP 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

LEPR | LEPROT | LEPROTL1 | LERFS | LETM1 | LETM2 | LETMD1 | LETR1 | Leukotriene B4 receptor (LTB4-R) | Leukotriene CysLT receptor | LEUTX | LEXM | LFNG | LGALS1 | LGALS12 | LGALS13 | LGALS14 | LGALS16 | LGALS17A | LGALS2 | LGALS3 | LGALS3BP | LGALS4 | LGALS7 | LGALS7B | LGALS8 | LGALS8-AS1 | LGALS9 | LGALS9B | LGALS9C | LGALSL | LGI1 | LGI2 | LGI3 | LGI4 | LGMN | LGMNP1 | LGR4 | LGR5 | LGR6 | LGSN | LHB | LHCGR | LHFPL1 | LHFPL2 | LHFPL3 | LHFPL3-AS1 | LHFPL3-AS2 | LHFPL4 | LHFPL5 | LHFPL6 | LHFPL7 | LHPP | LHX1 | LHX2 | LHX3 | LHX4 | LHX4-AS1 | LHX5 | LHX6 | LHX8 | LHX9 | LIAS | LIF | LIFR | LIFR-AS1 | LIG1 | LIG3 | LIG4 | LILRA1 | LILRA2 | LILRA3 | LILRA4 | LILRA5 | LILRA6 | LILRB1 | LILRB2 | LILRB3 | LILRB4 | LILRB5 | LILRP1 | LILRP2 | LIM domain kinase (LIMK) | LIM2 | LIMA1 | LIMASI | LIMCH1 | LIMD1 | LIMD1-AS1 | LIMD2 | LIME1 | LIMK1 | LIMK2 | LIMS1 | LIMS2 | LIMS3 | LIMS3-LOC440895 | LIMS4 | LIN28A | LIN28B