Immunoglobulin Expression in Cancer Cells and Its Critical Roles in Tumorigenesis.

Ming Cui,Quan Liao,Qiaofei Liu,Shenghua Zhang,Jing Huang,Xiaoyan Qiu

doi:10.3389/fimmu.2021.613530

Abstract

Traditionally, immunoglobulin (Ig) was believed to be produced by only B-lineage cells. However, increasing evidence has revealed a high level of Ig expression in cancer cells, and this Ig is named cancer-derived Ig. Further studies have shown that cancer-derived Ig shares identical basic structures with B cell-derived Ig but exhibits several distinct characteristics, including restricted variable region sequences and aberrant glycosylation. In contrast to B cell-derived Ig, which functions as an antibody in the humoral immune response, cancer-derived Ig exerts profound protumorigenic effects via multiple mechanisms, including promoting the malignant behaviors of cancer cells, mediating tumor immune escape, inducing inflammation, and activating the aggregation of platelets. Importantly, cancer-derived Ig shows promising potential for application as a diagnostic and therapeutic target in cancer patients. In this review, we summarize progress in the research area of cancer-derived Ig and discuss the perspectives of applying this novel target for the management of cancer patients.

Highlights

Immunoglobulin (Ig) molecules comprise two immunoglobulin heavy (IgH) chains and two immunoglobulin light (IgL) chains, which are linked by disulfide bridges to form a structure with twofold symmetry
The results suggested that the VHDJH transcripts of cancer-derived Ig share some features with Ig derived from B lymphocytes, such as V(D)J recombination, Nregion insertion, and a high mutation rate
Studies have shown that the antigen recognized by RP215 is an IgG molecule with aberrant glycosylation expressed by cancer cells [67]

Summary

Introduction

Immunoglobulin (Ig) molecules comprise two immunoglobulin heavy (IgH) chains and two immunoglobulin light (IgL) chains, which are linked by disulfide bridges to form a structure with twofold symmetry. Studies have shown that the antigen recognized by RP215 is an IgG molecule with aberrant glycosylation expressed by cancer cells [67]. Studies have shown that cancer-derived Ig acts as a crucial protumorigenic molecule that promotes carcinogenesis via several different mechanisms.

Results

Conclusion