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Comparative Immunology
Published in Julius P. Kreier, Infection, Resistance, and Immunity, 2022
The camel (Camelus dromedarius) has three IgG subclasses IgG1, IgG2, and lgG3. One of these, IgG1 has a conventional structure. The other two subclasses, IgG2 and IgG3 are heavy chain dimers that have no light chains. Despite the absence of light chains these molecules can bind a variety of antigens suggesting that light chains contribute minimally to antigen binding. Camels from both the old world (Camelas bactrianus) and the new world (Lama pacos, L glama, and L viguna) also possess a high proportion of these heavy-chain immunoglobulins.
Infectious Diseases
Published in Lyle D. Broemeling, Bayesian Analysis of Infectious Diseases, 2021
Antibodies are proteins called immunoglobulins, where each is made up of a chain of chemical subunits, or amino acids, and a light chain of them. The light chains have special sites, where the amino acids can link with complements on an antigen molecule. When an antibody attaches to an antigen, it deactivates by covering a key portion of the harmful substance. In some cases, through a process called opsonization, antibodies “butter” the surface of the antigens in order to make them more susceptible to phagocytes, which then devour the antigens. Often an antibody attaches to a bacterial antigen but requires an intermediate or complement to actually devour the bacterium. As the antibody-antigen union circulates in the blood, the complex “fixes” the complement to it which then the complex produces enzymes to eat through the bacterial wall to make the organism burst.
Diseases of the Peripheral Nerve and Mononeuropathies
Published in Philip B. Gorelick, Fernando D. Testai, Graeme J. Hankey, Joanna M. Wardlaw, Hankey's Clinical Neurology, 2020
Diana Mnatsakanova, Charles K. Abrams
20–40% of multiple myeloma patients, most commonly with light chains (2:1 λ–κ). Painful sensory or motor sensory neuropathy with a prominent small fiber component causing pain and autonomic dysfunction.
Combined serum free light chain predicts prognosis in acute kidney injury following cardiovascular surgery
Published in Renal Failure, 2022
Wenji Wang, Lulu Zhang, Tianye Yang, Shaojun Ma, Qi Zhang, Peng Shi, Feng Ding
The immunoglobulin light chains, as part of the immunoglobulins, are produced by plasma cells. There are two isotypes of light chains, kappa (κ) and lambda (λ) [7]. Monoclonal production of free light chains (FLCs) is important in almost all plasma cell disorders, such as multiple myeloma, amyloidosis, and monoclonal gammopathy of undetermined significance [8]. Recently, elevated concentrations of serum polyclonal combined FLCs (cFLC), as a potential biomarker of activation of the B-lymphocyte, have been investigated in a number of non-hematological malignant and inflammatory disorders including diabetes, CKD, and systemic lupus erythematosus (SLE) [9–11]. Nonspecific increases in cFLC occurred in a similar to the nonspecific increases in C reactive protein seen with inflammation[12]. The elevation of cFLC is also the result of reduced removal by impaired renal function [7,13]. Furthermore, elevated cFLC was demonstrated as a predictor of poorer overall survival in the general population, in patients with heart failure and in patients with CKD, as well [14–16].
Early stage IgD multiple myeloma in a 50-year-old man
Published in Baylor University Medical Center Proceedings, 2020
C. Lake Littlejohn, Andrew Whiteley, Marvin J. Stone
Immunoglobulin D multiple myeloma is rare, with an incidence of about 2% of all patients diagnosed with myeloma. Before Bladé et al2 described 53 patients with IgD myeloma in 1994, only seven series reported five or more patients with this particular class. Classically it was thought to be associated with a poorer prognosis compared to other myelomas; however, with the use of modern therapies, outcomes have been shown to be similar to other myeloma classes.1–3 IgD myeloma tends to present at a younger age, favor male gender, be of more advanced stage, and have more features of high-risk disease vs others.3,4 Unlike other myelomas, lambda light chain predominance is a characteristic feature of IgD myeloma and is seen in 70% to 90% of cases.4,5 Furthermore, IgD myeloma has been shown to present with higher rates of renal failure and Bence Jones proteinuria compared to other myelomas.3 Because the serum concentration of physiologic IgD is present at a much lower concentration (0–10 mg/dL) compared to IgG (1020–1460 mg/dL) and IgA (210–350 mg/dL), the M-spike on electrophoresis is often very small or even unrecognizable in IgD myeloma.4,5
Inter-assay variability in automated serum free light chain assays and their use in the clinical laboratory
Published in Critical Reviews in Clinical Laboratory Sciences, 2020
Laura Caponi, Nadia Romiti, Elona Koni, Annarita Di Fiore, Aldo Paolicchi, Maria Franzini
The five types of heavy chains (α, δ, ε, γ, μ) correspond to the five immunoglobulin (Ig) classes (IgA, IgD, IgE, IgG, IgM). The two light chains are kappa (κ) and lambda (λ), the latter consisting of peptides of about 220 amino acids, with a molecular weight of 22–25 kDa. In humans, about 60% of antibodies contain the κ chain and 40%, the λ chain, irrespective of the Ig class [2]. Both the light and heavy chains display structural regions called immunoglobulin domains, which are named constant (when shared by all immunoglobulins of the same class), or variable (when specific for each antibody). The paired variable domains of the heavy and light chains form the antigen-binding site. Although most of the heterogeneity between different Igs exists in the variable domains, a certain degree of heterogeneity also exists in the constant domains of the light chains; at least four functional isotypes of the λ chain [3,4] and three allotypes of the κ chain have been reported [4]. Plasma cells produce more light chains (10–40%) than heavy chains [5–7], and excess light chains secreted in the blood are known as free light chains (FLC). It is estimated that healthy subjects release 500 mg/day of FLC into the bloodstream [6,8].