PGLYRP1: A Potential Drug Target and Biomarker for Peptidoglycan Recognition

Target Name: PGLYRP1

NCBI ID: G8993

PGLYRP1

PGLYRP1: A Potential Drug Target and Biomarker for Peptidoglycan Recognition

Introduction

Peptidoglycan (PG) is a complex carbohydrate found in various cell types, including platelets, endothelial cells, and cancer cells. It is composed of a core 伪-glucan and a linear trisaccharide chain (尾-glucan). PGs play a crucial role in cell-cell adhesion, tissue repair, and inflammation. The recognition of PGs by various proteins, including PGLYRP1 (peptidoglycan recognition protein 1), is crucial for cellular processes. PGLYRP1 is a transmembrane protein that is expressed in various tissues and cell types. Its function in cell-cell adhesion, tissue repair, and inflammation makes it an attractive drug target and a potential biomarker.

PGLYRP1: Structure and Function

PGLYRP1 is a 21-kDa protein that is expressed in various tissues, including platelets, endothelial cells, liver cells, and cancer cells. It is localized to the endoplasmic reticulum (ER) and is predominantly expressed in the cytoplasm. PGLYRP1 is a cytoplasmic protein that is involved in the recognition of PGs. It consists of a 154 amino acid long N-terminus, a 21-kDa transmembrane domain, and a C-terminus that contains a unique N-glycosylation site.

PGLYRP1 is involved in several cellular processes, including cell-cell adhesion, migration, and invasion. It plays a critical role in the regulation of cell-cell adhesion by recognizing and interacting with PGs. PGLYRP1 recognizes PGs through its N-terminus and interacts with them through its transmembrane domain. This interaction between PGLYRP1 and PGs allows PGLYRP1 to regulate cellular processes, including cell-cell adhesion, migration, and invasion.

PGLYRP1 has also been shown to be involved in tissue repair and regeneration. It has been shown to be a critical regulator of cell-cell adhesion in wound healing and tissue regeneration. PGLYRP1 has also been shown to be involved in the regulation of cancer cell migration. and invasion. Its involvement in these processes makes PGLYRP1 an attractive drug target and a potential biomarker for cancer.

PGLYRP1 as a Drug Target

PGLYRP1 is a potential drug target due to its involvement in several cellular processes that are crucial for human health. PGLYRP1 can be targeted by small molecules, including inhibitors of its N-glycosylation site, which would disrupt its ability to recognize PGs. Additionally, PGLYRP1 can be targeted by antibodies that recognize its unique N-terminus and transmembrane domain.

PGLYRP1 has also been shown to be involved in several diseases, including cancer. Its involvement in cancer cell migration and invasion makes it an attractive drug target for cancer treatment. PGLYRP1 has also been shown to be overexpressed in various types of cancer, including breast, lung , and colorectal cancer. This overexpression of PGLYRP1 has been shown to contribute to the development and progression of these diseases.

PGLYRP1 has also been shown to be involved in several other cellular processes that are important for human health. Its involvement in cell-cell adhesion, tissue repair, and inflammation makes it an important regulator of these processes. Additionally, PGLYRP1 has been shown to play a critical role in the regulation of the immune response. Its involvement in these processes makes PGLYRP1 an attractive drug target for the development of new treatments for a variety of diseases.

PGLYRP1 as a Biomarker

PGLYRP1 has also been shown to be a potential biomarker for several diseases, including cancer. Its involvement in cancer cell migration and invasion makes it an

Protein Name: Peptidoglycan Recognition Protein 1

Functions: Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria and thus provides bactericidal activity (PubMed:9707603). Forms an equimolar complex with heat shock protein HSPA1A and induces programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane (PubMed:21247889, PubMed:26183779). In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement (PubMed:26654597). Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system (PubMed:30713770). Promotes also the activation of lymphocytes that become able to kill virus-infected cells as well as tumor cells by modulating the spectrum of their target-cell specificity (PubMed:29083508, PubMed:28977785). Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor (PubMed:28977785, PubMed:25595774)

The "PGLYRP1 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 PGLYRP1 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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