EMB - embigin | Elisa - Clia - Antibody - Protein

Background

Embigin (EMB) is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily, which is widely known for its role in cell-cell adhesion, signal transduction, and immune response. Embigin was first identified in mouse embryo tissues and later found to be conserved across various species, including humans. The expression of Embigin is noted in a variety of tissues, particularly in the thymus, heart, and certain epithelial tissues, indicating its involvement in diverse physiological processes. Research suggests that Embigin plays a crucial role in cell adhesion, migration, and possibly in the modulation of the extracellular matrix, contributing to tissue architecture and integrity.

Protein Structure

Embigin is characterized by its complex structure, which includes:

1. Extracellular Domain: The extracellular region of Embigin consists of multiple immunoglobulin-like (Ig-like) domains, which are critical for mediating cell-cell and cell-matrix interactions. These domains facilitate the binding to other proteins and receptors, thus playing a role in signal transduction and cellular communication.
2. Transmembrane Domain: This domain spans the cell membrane, anchoring the protein to the cell surface. The transmembrane region ensures that Embigin maintains its position within the cellular membrane, allowing it to participate in interactions both inside and outside the cell.
3. Intracellular Domain: The intracellular region contains motifs and phosphorylation sites essential for interacting with intracellular signaling pathways. These interactions can influence various cellular processes such as proliferation, differentiation, and migration.

The structure of Embigin, particularly its Ig-like domains, underscores its function in mediating adhesive interactions that are critical for cellular communication and the maintenance of tissue architecture.

Classification and Subtypes

Embigin belongs to the immunoglobulin superfamily, a large group of proteins involved in various aspects of immune response and cell adhesion. Within this superfamily, Embigin is classified as a cell adhesion molecule (CAM), which is a category of proteins that facilitate the binding of cells to each other and to the extracellular matrix.

While there are no specific subtypes of Embigin, it is closely related to other members of the immunoglobulin superfamily, such as Basigin (CD147) and Neuroplastin. These proteins share structural similarities and overlapping functions, particularly in cell adhesion and signaling.

Function and Biological Significance

Embigin is implicated in a range of cellular functions, primarily through its role in cell adhesion and migration:

1. Cell Adhesion: Embigin mediates adhesive interactions between cells and the extracellular matrix. This function is vital for maintaining the structural integrity of tissues and facilitating cellular communication.
2. Cell Migration: Embigin influences cell migration, a process crucial for development, wound healing, and immune responses. By modulating interactions with the extracellular matrix, Embigin can direct the movement of cells within tissues.
3. Extracellular Matrix Modulation: Embigin is thought to participate in the modulation of the extracellular matrix, affecting its composition and structure. This modulation can influence various cellular behaviors, including adhesion, migration, and proliferation.
4. Signal Transduction: Through its interactions with other cell surface receptors and intracellular signaling molecules, Embigin can transmit signals that affect cell behavior. This signaling is essential for coordinating cellular responses to environmental cues.

Clinical Issues

Alterations in Embigin expression and function have been associated with several clinical conditions:

1. Cancer: Abnormal expression of Embigin has been observed in various cancers, including breast cancer and melanoma. In these contexts, Embigin may influence tumor progression by affecting cell adhesion, migration, and invasion. Understanding the role of Embigin in cancer could lead to new therapeutic targets.
2. Developmental Disorders: Given its role in cell adhesion and migration, dysregulation of Embigin can potentially contribute to developmental abnormalities. Research is ongoing to elucidate the specific mechanisms and impacts of Embigin in developmental processes.
3. Cardiovascular Diseases: The expression of Embigin in cardiac tissues suggests a role in heart development and function. Changes in Embigin expression may be linked to cardiovascular diseases, although further studies are needed to confirm these associations.
4. Immune System Function: Embigin is expressed in the thymus and other immune-related tissues, indicating a possible role in immune system development and function. Dysregulation of Embigin could potentially impact immune responses and contribute to immune-related disorders.

Summary

Embigin is a critical cell adhesion molecule within the immunoglobulin superfamily, playing essential roles in cell adhesion, migration, and extracellular matrix modulation. Its structure, featuring multiple Ig-like domains, facilitates interactions that are crucial for maintaining tissue architecture and cellular communication. While primarily studied in the context of development and cancer, Embigin's functions extend to immune system regulation and potentially cardiovascular health. Ongoing research aims to further elucidate its roles and therapeutic potential in various clinical contexts. Understanding the multifaceted functions of Embigin can contribute to advancements in treating diseases associated with its dysregulation.