Journal of Clinical Immunology Research

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Editorial - Journal of Clinical Immunology Research (2023) Volume 6, Issue 2

Allergic sensitization: The role of immunoglobuline (ige) and mast cells.

Oliva Jin*

Department of Clinical Medicine and Public Health, University of Umea, Umea, Sweden

*Corresponding Author:
Oliva Jin
Department of Clinical Medicine and Public Health
University of Umea, Umea, Sweden
E-mail: jin@telia.com

Received: 02-Apr-2023, Manuscript No. AACIR-22-98593; Editor assigned: 05-Apr-2023, Pre QC No. AACIR-23-98593 (PQ); Reviewed: 19-Apr-2023, QC No. AACIR-23-98593; Revised: 22-Apr-2023, Manuscript No. AACIR-23-98593(R); Published: 27-Apr-2023, DOI: 10.35841/aacir-6.2.143

Citation: Jin O. Allergic sensitization: The role of immunoglobuline (ige) and mast cells. J Clin Immunol. 2023;6(2):143

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Abstract

  

Introduction

Immunoglobulins, also known as antibodies, play a crucial role in the immune system's defense against pathogens and foreign substances. They are a class of proteins produced by specialized white blood cells called B lymphocytes or B cells. Immunoglobulins are highly diverse and can recognize and bind to specific antigens, triggering a cascade of immune responses. This article will delve into the role of immunoglobulins in immune function, their structure, types, and their significance in health and disease [1].

Immunoglobulins have a characteristic Y-shaped structure composed of two heavy chains and two light chains. Each chain consists of Variable (V) and Constant (C) Regions. The V regions at the tips of the Y-shaped structure are responsible for antigen recognition, while the C regions provide stability and determine the immunoglobulin's functional properties. The heavy and light chains are linked by disulfide bonds, and together, they form the antigen-binding fragment region. The remaining part of the immunoglobulin, called the crystallizable fragment, is responsible for various effector functions there are five main classes of immunoglobulins: IgG, IgM, IgA, IgD, and

IgE. Each class has distinct properties and functions [2].

IgG: Immunoglobulin G is the most abundant class of antibodies in the bloodstream. It is involved in long-term immunity, neutralizing toxins, opsonization (marking pathogens for destruction), and crossing the placenta to provide passive immunity to the fetus.

IgM: Immunoglobulin M is the first antibody produced during an initial immune response. It is primarily found in the bloodstream and functions as a potent activator of the complement system, which helps eliminate pathogens.

IgA: Immunoglobulin A is predominantly found in mucosal areas, such as the respiratory and gastrointestinal tracts, as well as in saliva and tears. It provides localized immunity by preventing pathogens from attaching to and entering mucosal surfaces.

IgD: Immunoglobulin D is found on the surface of B cells and plays a role in their activation. Its exact functions are not well understood, but it may assist in the immune response against pathogens.

IgE: Immunoglobulin E is involved in allergic responses and defense against parasitic infections. It binds to mast cells and basophils, triggering the release of inflammatory mediators when encountering allergens, leading to allergic reactions [3]. Neurotrophins and other molecules important to neurodevelopmental processes are regulated by cytokines and chemokines, and early-life exposure to certain neuroimmune challenges has an impact on brain development [4].

The Role of immunoglobulins in immune function

Immunoglobulins play a central role in adaptive immunity, which is the body's ability to recognize and mount specific immune responses against particular pathogens. When a pathogen or foreign substance enters the body, B cells produce immunoglobulins that bind to specific antigens present on the surface of the invader. This binding triggers a series of immune responses [5].

Neutralization: Immunoglobulins can neutralize pathogens by binding to their surfaces, preventing them from entering and infecting host cells.

Opsonisation: Immunoglobulins can mark pathogens for destruction by binding to them and facilitating phagocytosis, a process in which immune cells engulf and eliminate the pathogen.

Activation of the complement system: Some immunoglobulins, particularly IgM and IgG, can activate the complement system, a cascade of proteins that enhances the immune response by promoting pathogen destruction and inflammation.

Allergic responses: IgE antibodies are responsible for triggering allergic reactions. When an individual with allergies encounters an allergen, such as pollen or certain foods, IgE antibodies bind to mast cells and basophils, leading to the release of histamine.

Mechanisms of immunoglobulin action

Immunoglobulins exert their protective effect by several mechanisms, including neutralization, opsonisation, complement activation, and Antibody-Dependent Cellular Cytotoxicity (ADCC). Neutralization is the process by which antibodies bind to the surface of pathogens, such as viruses and toxins, and prevent them from entering and damaging host cells. Neutralization can occur by steric hindrance, in which the antibody physically blocks the binding site of the pathogen, or by functional inhibition, in which the antibody interferes with the function of the pathogen, such as preventing the attachment of a virus to its receptor. Opsonisation is the process by which antibodies bind to the surface of pathogens and facilitate their recognition and phagocytosis by immune cells, such as macrophages and neutrophils. opsonisation occurs by the binding of the Fc portion of the antibody to Fc receptors on the surface of immune cells.

References

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