The requirement of light chain for the surface deposition of the heavy chain of immunoglobulin M.
نویسندگان
چکیده
The murine tumor line 70Z/3 resembles a pre-B lymphocyte in containing the heavy chain of IgM (mu) as a cytoplasmic protein in the apparent absence of light chain (L). However, these cells can be induced by lipopolysaccharide to differentiate into a B lymphocyte-like state, containing mu2L2 tetramers as membrane-bound molecules. This is a accompanied by an increase in mu synthesis, the acquisition of complex carbohydrate by mu, and the induction of L chain. We wished to determine which of these events is critical for membrane deposition of mu. We found that uninduced 70Z/3 cells, as well as lipopolysaccharide-uninducible variants, contained a low, constitutive level of membrane bound mu, all of which was found as mu2L2. Dextran sulfate, another inducing agent, apparently caused a redistribution of this pre-existing surface mu without altering the pattern of mu synthesis or processing. One lipopolysaccharide-uninducible variant showed a small subset of surface mu-positive cells, and the proportion of these cells increased with a prolonged induction period. The increase in mu synthesis was nearly normal, but mu did not acquire complex carbohydrate. However, the delayed appearance of surface mu-positive cells was paralleled by a delayed increase in L chain, which occurred only in those cells with mu on their membrane. We concluded that L chain signals the transport of mu to the cell surface.
منابع مشابه
تعیین اپی توپ های ناپیوسته زنجیره سبک ایمونوگلوبولین انسان توسط ایمونولوژی محاسبه ای
Background: Immunoglobulins are a group of proteins that have important role in defense against microorganisms. Immunoglobulins consist of heavy and light chains. In human, immunoglobulin light chain comprises of two isotypes: Kappa (K) and lambda (λ) based on amino acid differences in carboxylic end of their constant region. Marked changes in the K to λ ratio can happen in monocl...
متن کاملCloning and expression of the constant region of rainbow trout (Onchorhynchus mykiss) µ immunoglobulin chain in Escherichia coli
The importance of rainbow trout (Onchorhynchus mykiss) in Iran aquaculture industry on one hand, and increasing the mortality of this fish due to outbreaks of infectious diseases, on the other hand, indicate the requirement for more profound understanding the rainbow trout immune system and access to laboratory tools for definitive diagnosis of its diseases. One of the most important defense me...
متن کاملCloning and expression of the constant region of rainbow trout (Onchorhynchus mykiss) µ immunoglobulin chain in Escherichia coli
The importance of rainbow trout (Onchorhynchus mykiss) in Iran aquaculture industry on one hand, and increasing the mortality of this fish due to outbreaks of infectious diseases, on the other hand, indicate the requirement for more profound understanding the rainbow trout immune system and access to laboratory tools for definitive diagnosis of its diseases. One of the most important defense me...
متن کاملتولید آنتیبادی پلیکلونال شتری علیه گیرنده 2 فاکتور رشد سلولهای آندوتلیال عروق و بررسی عملکرد آن
Abstract Background: In molecular approach, serum of camel contains a unique type of antibodies devoid of light chains since the light chain is missing, the heavy-chain antibodies should bind their antigen by one single domain, the variable domain of the heavy immunoglobulin chain. Vascular endothelial growth factor receptor-2 (VEGFR-2) is one of the important proteins in angiogenesis which...
متن کاملSerum Free Light-chain Assay for the Diagnosis, Management, and Prognosis of Multiple Myeloma
In recent decades, new serum biomarkers have been developed for routine laboratory practice, such as assaying serum free light chains and more recently, assaying immunoglobulin heavy and light chain isotypes (Hevylite). In this work, we highlight the interest of new biomarkers (Hevylite Test) in the management of monoclonal gammopathies because of the technical advantages it confers and the se...
متن کاملCompatibility of B-Sheets with Epitopes Predicted by Immunoinformatic in Human IgG
Background & Aims: Antibodies, well-known as immunoglobulins (Igs), are produced by B lymphocytes and specifically defend against pathogens. Igs are glycoproteins and have high diagnostic value in several diseases including infections (1). Igs are composed of light and heavy chains (2, 3). Each chain is comprised of about 110-120 amino acid residues which create immunoglobulin folds named domai...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 258 8 شماره
صفحات -
تاریخ انتشار 1983