CD63 Specific Neutra™ Antibody Products

CD63, also known as lysosome-associated membrane protein 3 (LAMP-3), is a protein that belongs to the tetraspanin family. It is widely recognized for its presence on the surfaces of cells and within cellular vesicles. CD63 is involved in various cellular processes, including the trafficking and fusion of vesicles such as lysosomes and exosomes. It plays a significant role in immune response regulation by participating in the activation and migration of immune cells. CD63 is also notable in the field of cancer research, where it is used as a marker for exosomes in cancer diagnostics. Additionally, CD63 interacts with other molecules to mediate signal transduction and cellular adhesion, making it a crucial component in both physiological and pathological processes.

Its Gene ID: 967, UniProtKB ID: P08962, OMIM ID: 155740

The Structure of CD63

CD63 is a protein encoded by the CD63 gene located on chromosome 12q13 in humans. It belongs to the tetraspanins family, which is part of the larger 4-transmembrane superfamily (TM4SF), comprising 28 members characterized by their structure and function in cellular processes. The protein has a molecular mass that typically ranges from 30 to 60 kDa and consists of 237 amino acids.

The structure of CD63, like other tetraspanins, features four hydrophobic transmembrane domains that anchor it within the plasma membrane. These transmembrane domains create two distinct extracellular loops and short cytoplasmic tails at both the N- and C-terminals. The smaller extracellular loop (SEL) is positioned between the first and second transmembrane domains, while the larger extracellular loop (LEL) lies between the third and fourth transmembrane domains. An additional intracellular loop connects the second and third transmembrane domains, further characterizing its structural complexity.

This complex structure enables CD63 to interact with various other proteins, including integrins and other tetraspanins, forming tetraspanin-enriched microdomains that facilitate a range of cell signaling processes. These interactions are essential for the diverse functions attributed to CD63, from immune response modulation to involvement in pathological conditions such as cancer and viral infections.

Fig.1 The probable structure of CD63.¹

The Function of CD63

CD63 forms complexes with other proteins like TIMP1 and β1-integrin, influencing cellular behavior in tumor progression. The interaction between CD63, TIMP1 (Tissue Inhibitor of Metalloproteinases 1), and β1-integrin has been studied for its potential impact on cancer development and progression. TIMP1 is known for its ability to inhibit matrix metalloproteinases (MMPs), which are involved in the degradation of the extracellular matrix and play a crucial role in tumor metastasis.

The complex formed by TIMP1, CD63, and β1-integrin has been shown to affect several cellular functions such as cell adhesion, migration, proliferation, and survival. This interaction may activate specific signaling pathways that contribute to the malignant behavior of cancer cells, suggesting a potential target for therapeutic intervention in cancer treatment.

CD63-related Signaling Pathways

The TIMP-1/CD63/β1-integrin signaling pathway plays a critical role in modulating cellular behaviors that are crucial in cancer biology, including cell adhesion, migration, and survival. TIMP-1 binds to CD63, a tetraspanin protein that facilitates its interaction with β1-integrin, forming a complex that is pivotal in signal transduction at the cell membrane. This complex formation triggers the activation of Focal Adhesion Kinase (FAK) and Extracellular Signal-Regulated Kinase (ERK) signaling pathways. FAK and ERK are well-known mediators of cell survival, proliferation, and motility-processes integral to tumor growth and metastasis. The activation of these pathways promotes cellular processes that enhance the survival capabilities of cancer cells, aid in their proliferation, and facilitate their movement, thereby contributing to the invasive and metastatic potential of tumors. Moreover, the TIMP-1/CD63/β1-integrin pathway impacts other downstream signaling molecules and pathways, influencing cellular interactions with the extracellular matrix and neighboring cells, which further supports cancer cell adaptation and survival in the tumor microenvironment.

Fig.2 Intracellular signaling pathways activated by the TIMP-1/CD63/β1-integrin.¹

CD63 in Cancer Progression

CD63 plays a critical player in cancer biology, affecting tumor growth, angiogenesis, and the ability of cancer cells to invade new tissues. This underscores the potential of targeting CD63 in therapeutic strategies aimed at controlling tumor spread and improving cancer treatment outcomes.

CD63 is particularly significant due to its ability to interact with other critical molecules like TIMP-1 and β1-integrin, forming complexes that significantly influence cancer cell behavior. The complex activates signaling pathways mediated by Focal Adhesion Kinase (FAK) and Extracellular Signal-Regulated Kinase (ERK), which are crucial for the invasive capabilities of cancer cells.

Additionally, CD63 impacts the cellular microenvironment by influencing the behavior of exosomes. These small vesicles are rich in CD63 and are involved in communication between cells, including the transfer of oncogenic proteins and nucleic acids that can alter the tumor microenvironment to favor cancer progression and metastasis.

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REFERENCE

1. Justo, Beatriz Laís, and Miriam Galvonas Jasiulionis. "Characteristics of TIMP1, CD63, and β1-integrin and the functional impact of their interaction in cancer." International journal of molecular sciences 22.17 (2021): 9319. Distributed under Open Access license CC BY 4.0, without modification.