ISLR - immunoglobulin superfamily containing leucine rich repeat | Elisa - Clia - Antibody - Protein

Background

ISLR (Immunoglobulin Superfamily Containing Leucine Rich Repeat) is a protein encoded by the ISLR gene in humans. It belongs to the immunoglobulin superfamily (IgSF), which is known for its involvement in cell adhesion, immune response, and various signaling processes. The ISLR protein is distinguished by its unique structure that includes both immunoglobulin-like (Ig-like) domains and leucine-rich repeats (LRRs). These structural motifs contribute to its role in cellular interactions and signaling pathways.

ISLR is expressed in various tissues, including the nervous system, skeletal muscles, and connective tissues, indicating its multifunctional nature. Research has revealed that ISLR plays a significant role in cellular communication, particularly in processes such as cell adhesion, migration, and differentiation. Its involvement in these fundamental processes underscores its importance in development and disease.

Protein Structure

The ISLR protein is characterized by a combination of structural motifs that are crucial for its function:

1. Immunoglobulin-Like (Ig-like) Domains: These domains are composed of around 70-110 amino acids and form a β-sandwich structure consisting of two sheets of β-strands. Ig-like domains are typically involved in protein-protein interactions, mediating cell adhesion and signaling.
2. Leucine-Rich Repeats (LRRs): LRRs are structural motifs of 20-30 amino acids that are rich in the hydrophobic amino acid leucine. They form a curved solenoid structure, which provides a versatile framework for protein-protein interactions. The LRR domain in ISLR facilitates interactions with other proteins and contributes to its role in cellular signaling and adhesion.
3. Signal Peptide: The N-terminal signal peptide directs the nascent protein to the secretory pathway, indicating that ISLR is likely secreted or associated with the cell membrane.
4. Glycosylation Sites: ISLR contains potential N-linked glycosylation sites, which are critical for its stability, localization, and function.

The unique combination of these structural features enables ISLR to participate in diverse cellular functions, particularly those involving extracellular matrix interactions and signaling.

Classification and Subtypes

The ISLR protein is a member of the immunoglobulin superfamily, which includes a wide variety of proteins involved in immune response, cell adhesion, and signaling. Within this superfamily, ISLR can be classified based on its structural domains and functional roles. While ISLR itself does not have widely recognized subtypes, it is part of a broader group of proteins containing both Ig-like domains and LRRs, which share similar structural and functional characteristics.

Function and Biological Significance

ISLR has several key functions in cellular processes:

1. Cell Adhesion and Migration: ISLR plays a pivotal role in mediating cell-cell and cell-matrix interactions. Its Ig-like domains facilitate adhesion to other cells, while its LRR domains interact with extracellular matrix components, aiding in cell migration.
2. Signal Transduction: By interacting with other cell surface receptors and extracellular matrix proteins, ISLR participates in signaling pathways that regulate cell proliferation, differentiation, and survival.
3. Tissue Development and Repair: ISLR is involved in the development of various tissues, including nervous and connective tissues. It contributes to the regulation of stem cell niches and is implicated in tissue repair processes following injury.
4. Immune Response: As a member of the IgSF, ISLR may have roles in the immune system, particularly in the modulation of immune cell interactions and responses.

Clinical Issues

Aberrations in ISLR expression and function are associated with several pathological conditions:

1. Cancer: Dysregulation of ISLR has been linked to tumor progression and metastasis. Its role in cell adhesion and migration suggests that altered ISLR expression could facilitate cancer cell dissemination and invasion.
2. Fibrosis: Increased ISLR expression is observed in fibrotic tissues, indicating its involvement in the pathological remodeling of the extracellular matrix. Targeting ISLR could be a potential therapeutic strategy for fibrotic diseases.
3. Neurological Disorders: Given its expression in the nervous system, ISLR may play a role in neurodevelopmental disorders. Mutations or dysregulation of ISLR could contribute to abnormal neural development and function.
4. Connective Tissue Diseases: ISLR's involvement in connective tissue development and repair suggests that it may be implicated in disorders affecting these tissues, such as osteoarthritis or tendonopathies.

Summary

ISLR is a multifunctional protein that plays crucial roles in cell adhesion, migration, and signaling. Its unique structure, comprising Ig-like domains and LRRs, enables it to participate in diverse cellular processes essential for tissue development, repair, and immune responses. Dysregulation of ISLR is associated with various diseases, including cancer, fibrosis, and neurological disorders. Understanding the molecular mechanisms underlying ISLR function and its involvement in these conditions could provide new insights into therapeutic strategies targeting this protein. The study of ISLR continues to be an important area of research, offering potential advancements in both basic biology and clinical applications.