Study on PDE1C and Its Role in Disease Progression (G5137)

Target Name: PDE1C

NCBI ID: G5137

PDE1C

Other Name(s): cam-PDE 1C | dual specificity Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C | Human 3',5' cyclic nucleotide phosphodiesterase (HSPDE1C1A) | Calcium/calmodulin-dependent 3',

Study on PDE1C and Its Role in Disease Progression

The identification of potential drug targets and biomarkers is a crucial step in the development of new pharmaceuticals. One of the most promising areas of research is the study of protein-protein interactions (PPIs) and their role in disease progression. One of the key protein-protein interactions that has garnered a lot of attention in recent years is the interaction between the protein known as PDE1C and its partner protein, PDE1B. This interaction is known as the cam-PDE1C interaction, and it is a crucial component of the protein signaling pathway in many organisms, including humans.

In this article, we will explore the biology of PDE1C and its role in disease progression. We will discuss the current state of research on the cam-PDE1C interaction and its potential as a drug target. We will also examine the potential clinical applications of a drug that targets the cam-PDE1C interaction, such as the development of new treatments for neurodegenerative diseases.

The Biology of PDE1C

PDE1C is a protein that is expressed in many different tissues throughout the body, including the brain, pancreas, and heart. It is a member of the superfamily of prolyl hydroxylase enzymes (PHAs), which are a group of enzymes that play a critical role in the regulation of protein structure and function. PDE1C is characterized by a catalytic active site that is optimized for the hydrolysis of the amino acid Asp, which is a key structural component of many proteins.

The cam-PDE1C interaction

The cam-PDE1C interaction is a critical component of the protein signaling pathway in many organisms. It is a protein-protein interaction that is formed when the amino acid Asp114 of PDE1C binds to the amino acid Asp112 of PDE1B. This interaction allows PDE1C to regulate the activity of PDE1B and to play a role in the regulation of cellular processes such as cell signaling, migration, and invasion.

The cam-PDE1C interaction is regulated by a variety of factors, including the concentration of both PDE1C and PDE1B, the pH of the environment, and the presence of other proteins that can interact with PDE1C. It is also influenced by the genetic context, as changes in the expression or activity of PDE1C can have a significant impact on the behavior of the cell.

Current state of research

The cam-PDE1C interaction is a topic of active research, with a number of studies having investigated its role in different cellular processes. One of the most significant findings of these studies is that the cam-PDE1C interaction is critical for the regulation of cell signaling and for the development of cancer.

For example, studies have shown that changes in the cam-PDE1C interaction can have a significant impact on the growth and survival of cancer cells. In addition, the cam-PDE1C interaction has also been implicated in the regulation of neural networks and the development of neurodegenerative diseases.

Potential clinical applications

The cam-PDE1C interaction is a promising area of research with potential clinical applications. One of the most promising applications is the development of new treatments for neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. These conditions are characterized by the progressive loss of brain cells and can cause a range of symptoms, including memory loss, stiffness, and difficulty with movement.

In addition to the development of new treatments for neurodegenerative diseases, the cam-PDE1C interaction is also being investigated as a potential biomarker for disease diagnosis and monitoring. For example, changes in the

Protein Name: Phosphodiesterase 1C

Functions: Calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:8557689, PubMed:29860631). Has a high affinity for both cAMP and cGMP (PubMed:8557689). Modulates the amplitude and duration of the cAMP signal in sensory cilia in response to odorant stimulation, hence contributing to the generation of action potentials. Regulates smooth muscle cell proliferation. Regulates the stability of growth factor receptors, including PDGFRB (Probable)

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