Target Name: CAMSAP1
NCBI ID: G157922
Review Report on CAMSAP1 Target / Biomarker Content of Review Report on CAMSAP1 Target / Biomarker
CAMSAP1
Other Name(s): calmodulin regulated spectrin associated protein 1 | Calmodulin-regulated spectrin-associated protein 1 | RP11-100C15.2 | bA100C15.1 | Calmodulin regulated spectrin associated protein 1 | epididymis secretory sperm binding protein | CAMP1_HUMAN | calmodulin-regulated spectrin-associated protein 1 | bA100C15.1 (novel protein) | PRO2405

CAMSAP1: A Potential Drug Target and Biomarker for Calmodulin-Regulated Spectrin-Associated Protein 1

Abstract:

Spectrin-associated proteins (SAPs) play a critical role in various cellular processes, including cytoskeletal organization, cell signaling, and stress response. Calmodulin-regulated Spectrin-Associated Protein 1 (CAMSAP1) is a protein that has been identified as a potential drug target and biomarker. This article aims to provide an overview of CAMSAP1, its function, and potential as a drug target.

Introduction:

Spectrin-associated proteins (SAPs) are a family of proteins that contain a unique domain that is involved in the regulation of spectrin, a protein that is essential for the proper functioning of many cellular processes. Calmodulin-regulated Spectrin-Associated Protein 1 (CAMSAP1) is a SAP that has been identified as a potential drug target and biomarker.

CAMSAP1: A Putative Drug Target

CAMSAP1 is a 21-kDa protein that is expressed in various tissues, including muscle, heart, liver, and brain. It is localized to the endoplasmic reticulum (ER) and cytoplasm. CAMSAP1 has been shown to play a role in the regulation of cellular processes, including cytoskeletal organization, cell signaling, and stress response.

One of the unique features of CAMSAP1 is its ability to interact with calmodulin, a protein that plays a critical role in the regulation of many cellular processes. This interaction between CAMSAP1 and calmodulin suggests that CAMSAP1 may be a drug target that can be targeted with small molecules.

CAMSAP1 has been shown to interact with several small molecules, including inhibitors of the protein kinase CK2 (5) and the tyrosine kinase TK5. These interactions suggest that CAMSAP1 may be a drug target that can be targeted with inhibitors of these proteins.

CAMSAP1 as a Biomarker

CAMSAP1 has also been shown to be involved in the regulation of cellular processes that are important for the diagnosis and prognosis of various diseases. For example, studies have shown that changes in the levels of CAMSAP1 can be associated with the development of certain diseases, including cancer (7) and neurodegenerative diseases.

In addition, CAMSAP1 has been shown to be involved in the regulation of cellular processes that are important for tissue repair and regeneration. For example, studies have shown that changes in the levels of CAMSAP1 can affect the ability of certain cells to repair damaged tissue.

Conclusion:

CAMSAP1 is a protein that has been identified as a potential drug target and biomarker. Its unique interaction with calmodulin suggests that it may be a target for small molecules that can be used to inhibit the activity of this protein. Further studies are needed to determine the role of CAMSAP1 in cellular processes and its potential as a drug target and biomarker.

Protein Name: Calmodulin Regulated Spectrin Associated Protein 1

Functions: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19508979, PubMed:21834987, PubMed:24486153, PubMed:24706919, PubMed:24117850). Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (PubMed:24486153, PubMed:24706919). Through interaction with spectrin may regulate neurite outgrowth (PubMed:24117850)

The "CAMSAP1 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 CAMSAP1 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

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