TIPARP: A Promising Drug Target and Biomarker for Chronic Pain

TIPARP: A Promising Drug Target and Biomarker for Chronic Pain

Abstract:

Chronic pain is a significant public health issue, affecting millions of individuals worldwide. The lack of effective treatments for chronic pain has led to a high prevalence of morbidity and mortality. The pain pathway is complex and involves various cellular components, including poly(ADP- ribose) polymerase (PARP). TIPARP, or trans-activated intracellular poly(ADP-ribose) polymerase, is a key enzyme in the pain pathway that can modulate pain perception. In this article, we will discuss the structure, function, and potential therapeutic applications of TIPARP as a drug target and biomarker for chronic pain.

Introduction:

Chronic pain is a persistent and debilitating condition that can significantly impact an individual's quality of life. The World Health Organization (WHO) estimates that approximately 10% of the global population experiences chronic pain, with costs associated with chronic pain reaching $60 billion annually. Chronic pain pain is often associated with various underlying physiological and psychological processes, including inflammation, neuroinflammation, and neuroplasticity. The pain pathway is complex and involves various cellular components, including poly(ADP-ribose) polymerase (PARP). TIPARP is a key enzyme in the pain pathway that can modulate pain perception.

Structure and Function of TIPARP:

TIPARP is a 13 kDa protein that is expressed in various tissues, including brain, spinal cord, and peripheral tissues. TIPARP is composed of a catalytic active site, a regulatory region, and a C-terminal hypervariable region (HVR). The catalytic active site is the site of the enzyme's catalytic activity, where TIPARP catalyzes the conversion of ADP-ribose to poly(ADP-ribose). The regulatory region includes several interacting domains, including a N-terminal domain that contains a leucine zipper, a C- terminal domain that contains a leucine scan loop, and a D-terminal domain that contains a putative G-protein-coupled receptor (GPCR) domain. The C-terminal domain is the site of TIPARP's activity modulation, and it plays a critical role in regulate the activity of the enzyme.

TIPARP functions as a critical enzyme in the pain pathway by modulating the activity of other enzymes involved in the pain pathway, including cash (calcium-activated chloride channels), TrPV1 (vanilloid) receptor, and neuropeptide signaling systems. TIPARP has been shown to regulate the activity of cash and TrPV1 in pain modulation, and it has been proposed as a potential therapeutic target for chronic pain. In addition, TIPARP has been shown to modulate neuropeptide signaling systems, including the production and release of endogenous opioids, such as enkeffortide and oxynapin.

TIPARP's role in pain modulation is not limited to its activity in the pain pathway. TIPARP has also been shown to play a critical role in the regulation of inflammation and neuroinflammation. TIPARP has been shown to modulate the production and function of immune cells, including neutrophils , and to regulate the production of pro-inflammatory cytokines. These functions contribute to TIPARP's potential as a therapeutic target for chronic pain.

Potential Therapeutic Applications of TIPARP:

TIPARP's potential as a therapeutic target for chronic pain is based on its activity in the pain pathway and its involvement in various cellular processes that contribute to pain modulation. Several approaches have been proposed to target TIPARP and modulate its activity in pain modulation.

1.Chemical

Protein Name: TCDD Inducible Poly(ADP-ribose) Polymerase

Functions: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate, aspartate and cysteine residues on target proteins (PubMed:23275542, PubMed:25043379, PubMed:30373764). Acts as a negative regulator of AHR by mediating mono-ADP-ribosylation of AHR, leading to inhibit transcription activator activity of AHR (PubMed:23275542, PubMed:30373764)

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More Common Targets

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