Target Name: LIAS
NCBI ID: G11019
Review Report on LIAS Target / Biomarker Content of Review Report on LIAS Target / Biomarker
LIAS
Other Name(s): LIAS variant 1 | LAS | LIAS variant 4 | Lipoate synthase | Lip-syn | PDHLD | Lipoyl synthase, mitochondrial (isoform 2) | lipoic acid synthetase | Lipoic acid synthetase, transcript variant 2 | LS | Lipoic acid synthase | Lipoic acid synthetase, transcript variant 1 | Lipoyl synthase, mitochondrial (isoform 1) | LIP1 | Lipoyl synthase, mitochondrial (isoform 4) | LIAS variant 2 | HUSSY-01 | LIAS_HUMAN | Lipoyl synthase, mitochondrial | lip-syn | HGCLAS | lipoate synthase | Lipoic acid synthetase, transcript variant 4

LIAS: The Lactate-Induced Increased Absorption Pathway

LIAS, or Lactate-Induced Increased Absorption (LIAS), is a phenomenon that has been observed in the human body where lactate, which is a byproduct of muscle metabolism, increases the absorption of certain medications. This is an interesting finding because it suggests that the body may be using lactate as a signaling molecule to enhance the absorption of certain drugs.

The LIAS pathway is a complex intracellular signaling pathway that has been identified as a potential drug delivery system. The pathway involves the production of lactate from muscle metabolism, which then travels to the endoplasmic reticulum (ER) and increases the absorption of certain drugs.

One of the key proteins involved in the LIAS pathway is the transporter protein known as TG-1. This protein is responsible for transporting lactate across the endbladder membrane and into the bloodstream. TG-1 has been shown to play a crucial role in the regulation of drug absorption by increasing its expression in the body's tissues and organs.

Another key protein involved in the LIAS pathway is the hormone insulin. insulin is a key regulator of muscle metabolism and has been shown to play a role in the production of lactate. Insulin has been shown to increase the production of lactate in muscle tissue and to enhance its effects on drug absorption.

The LIAS pathway has been shown to be involved in the regulation of many different drugs, including many statins, which are used to treat high cholesterol. By increasing the absorption of these drugs, the LIAS pathway can lead to improved treatment outcomes.

The LIAS pathway is also involved in the regulation of other drugs that are used to treat a wide range of conditions, including heart disease, diabetes, and cancer. For example, the LIAS pathway has been shown to be involved in the regulation of the anti-inflammatory drug celecoxib, which is used to treat inflammatory conditions.

In addition to its role in drug regulation, the LIAS pathway is also of interest as a potential drug target. By inhibiting the activity of the transporter protein TG-1, researchers have shown that they can reduce the production of lactate and improve the absorption of drugs. This suggests that targeting TG-1 could be a promising strategy for the development of new treatments for a wide range of conditions.

The LIAS pathway is also of interest as a potential biomarker for drug monitoring. By measuring the production of lactate in the body and the absorption of certain drugs, researchers can monitor the effectiveness of a drug and identify potential drug interactions or side effects.

Overall, the LIAS pathway is a complex intracellular signaling pathway that is involved in the regulation of many different drugs. By targeting the transporter protein TG-1 and the hormone insulin, researchers have shown that they can improve the absorption of these drugs and enhance their therapeutic effects. The LIAS pathway is also of interest as a potential drug target and as a biomarker for drug monitoring. Further research is needed to fully understand the role of the LIAS pathway in drug regulation and its potential as a therapeutic approach.

Protein Name: Lipoic Acid Synthetase

Functions: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives

The "LIAS 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 LIAS 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

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 | LIN28B-AS1 | LIN37 | LIN52 | LIN54 | LIN7A | LIN7B | LIN7C | LIN9 | LINC-PINT | LINC-ROR | LINC00028 | LINC00029 | LINC00032 | LINC00051 | LINC00052 | LINC00092 | LINC00102 | LINC00106 | LINC00111 | LINC00112 | LINC00113 | LINC00114 | LINC00115 | LINC00158 | LINC00159 | LINC00160 | LINC00161 | LINC00163 | LINC00173 | LINC00174 | LINC00184 | LINC00189 | LINC00200 | LINC00205 | LINC00207 | LINC00208 | LINC00210 | LINC00221 | LINC00222 | LINC00226 | LINC00235 | LINC00239 | LINC00240 | LINC00242 | LINC00243 | LINC00244 | LINC00251 | LINC00260 | LINC00261 | LINC00265 | LINC00266-1 | LINC00266-3 | LINC00272 | LINC00273 | LINC00276 | LINC00278 | LINC00293 | LINC00294 | LINC00298 | LINC00299 | LINC00301 | LINC00303 | LINC00304