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Journal articles on the topic 'Immunoglobulins'

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Published: 4 June 2021

Last updated: 25 May 2024

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1

Markina, Yuliya V., Elena V. Gerasimova, Alexander M. Markin, Victor Y. Glanz, Wei-Kai Wu, Igor A. Sobenin, and Alexander N. Orekhov. "Sialylated Immunoglobulins for the Treatment of Immuno-Inflammatory Diseases." International Journal of Molecular Sciences 21, no. 15 (July 31, 2020): 5472. http://dx.doi.org/10.3390/ijms21155472.

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Immunoglobulins are the potent effector proteins of the humoral immune response. In the course of evolution, immunoglobulins have formed extremely diverse types of molecular structures with antigen-recognizing, antigen-binding, and effector functions embedded in a single molecule. Polysaccharide moiety of immunoglobulins plays the essential role in immunoglobulin functioning. There is growing evidence that the carbohydrate composition of immunoglobulin-linked glycans, and especially their terminal sialic acid residues, provide a key effect on the effector functions of immunoglobulins. Possibly, sialylation of Fc glycan is a common mechanism of IgG anti-inflammatory action in vivo. Thus, the post-translational modification (glycosylation) of immunoglobulins opens up significant possibilities in the diagnosis of both immunological and inflammatory disorders and in their therapies. This review is focused on the analysis of glycosylation of immunoglobulins, which can be a promising addition to improve existing strategies for the diagnosis and treatment of various immuno-inflammatory diseases.

2

Okamoto, Yasuyuki, Noboru Hamada, Toshimichi Fujisawa, Jaeduk Noh, Junichi Yamakawa, Mariko Ohno, Kunihiko Ito, and Hirotoshi Morii. "Why no simple relationship between thyroid peroxidase activity-inhibiting immunoglobulins and thyroid function in autoimmune thyroid disease?" Acta Endocrinologica 124, no. 4 (April 1991): 442–48. http://dx.doi.org/10.1530/acta.0.1240442.

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Abstract. We have reported that some anti-thyroid peroxidase antibodies inhibit the activity of thyroid peroxidase in vitro. These thyroid peroxidase activity-inhibiting immunoglobulins seem to inhibit thyroid function in some patients, but the relationship between thyroid peroxidase activity-inhibiting immunoglobulins and thyroid function is not simple. We designed this study to explore this lack of a simple relationship. We stained immunoglobulin G deposits by immunofluorescence staining or the peroxidase-antiperoxidase method, and stained endogenous thyroid peroxidase activity by enzyme histochemistry in thyroid sections. When cryostat thyroid sections were incubated with thyroid peroxidase activity-inhibiting immunoglobulins, immunoglobulin G deposits were seen as lines of stain on the apical border and as intracellular staining, and endogenous thyroid peroxidase activity was inhibited. In paraffin-embedded thyroid sections from 5 Hashimoto's patients and 6 Graves' patients, immunoglobulin G deposits were not found on the apical border of the follicular epithelium. In frozen thyroid sections from 22 Graves' patients, no clear deposits of immunoglobulin G on this apical border were seen. In organ-cultured thyroid slices incubated with thyroid peroxidase activity-inhibiting immunoglobulins, endogenous thyroid peroxidase activity was not inhibited. In conclusion, thyroid peroxidase activity-inhibiting immunoglobulins may reach its antigen only with difficulty. This is one of the reasons why no simple relationship is observed between thyroid peroxidase activity-inhibiting immunoglobulins and thyroid function.

3

Almaghlouth, Ibrahim, Sindhu R. Johnson, Eleanor Pullenayegum, Dafna Gladman, and Murray Urowitz. "Immunoglobulin levels in systemic lupus erythematosus: A narrative review." Lupus 30, no. 6 (March 28, 2021): 867–75. http://dx.doi.org/10.1177/09612033211004714.

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Immunoglobulins play a fundamental role in the protection of the human body against internal and external threats. They also contribute to the immune system homeostasis and maintenance of self-tolerance. Hypogammaglobulinemia is occasionally encountered in routine clinical practice by rheumatologists. Low levels of immunoglobulins can occur as primary or secondary issues and may predispose patients to various forms of infection. However, the impact of the low immunoglobulin level abnormality varies with the underlying condition. In this narrative review, we shed light on the overall types and functions of immunoglobulins for clinicians. We discuss important principles of immunoglobulin measurements. We then consider the primary and secondary causes of low immunoglobulins with a special focus on hypogammaglobulinemia in patients with systemic lupus erythematosus (SLE).

4

DREW, M. D., and B. D. OWEN. "THE PROVISION OF PASSIVE IMMUNITY TO COLOSTRUM-DEPRIVED PIGLETS BY BOVINE OR PORCINE SERUM IMMUNOGLOBULINS." Canadian Journal of Animal Science 68, no. 4 (December 1, 1988): 1277–84. http://dx.doi.org/10.4141/cjas88-143.

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Bovine and porcine serum immunoglobulins were obtained from abattoir blood by sodium polyphosphate fractionation and mixed with sow milk replacer to provide an IgG level of 20 mg mL−1 for diets fed on day 1 and 4 mg mL−1 for diets fed on days 2–14. Control piglets received only sow milk replacer. The control group had a survival rate of 22% compared to 75% for the piglets receiving bovine immunoglobulins and 92% for those receiving porcine immunoglobulins. Diarrhea was more severe in the control group for the first 21 d than in the other two groups. The bovine and porcine groups did not differ in the incidence of diarrhea at any time during the experiment. The average daily gains measured over the 28-d period were significantly different between the three treatments with the controls gaining 83.9 g d−1, bovine immunoglobulin fed piglets 140.6 g d−1 and porcine immunoglobulin fed piglets 169.8 g d−1. Serum immunoglobulins were not detectable until 7 d of age in the controls and the concentration rose to 14.6 mg d−1 on day 21. Porcine immunoglobulins were absorbed to a much higher degree than bovine immunoglobulins. Piglets receiving porcine immunoglobulins had a serum IgG concentration of 19.7 mg d−1 at 1 d of age compared to 5.0 mg d−1 for the bovine treatment piglets. Procine serum immunoglobulins were judged superior to bovine immunoglobulins in providing passive immunity to colostrum-deprived piglets. Key words: Immunoglobulins, colostrum-deprived, piglet, milk replacer

5

Goode, N. P., A. M. Davison, G. Gowland, and M. Shires. "Spontaneous glomerular immunoglobulin deposition in young Sprague-Dawley rats." Laboratory Animals 22, no. 4 (October 1, 1988): 287–92. http://dx.doi.org/10.1258/002367788780746232.

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The frequency, age-onset and distribution of spontaneously deposited immunoglobulins (lgs) in glomeruli of Sprague-Dawley rats has been investigated. Groups of rats ( n=10) were examined at 4-7 day intervals from birth (presuckling) until 30 days of age. Findings were compared with circulating immunoglobulin concentrations in each age group. Immunoglobulins were undetectable in immature kidneys of newborn rats. However, as early as 5 days, scanty IgA and IgM deposits were observed predominantly in mesangial areas of mature glomeruli, corresponding to low circulating concentrations of these immunoglobulins. By contrast, glomerular IgG deposits were not observed until 21 days, despite relatively high concentrations of circulating maternal IgG from birth. Mesangial deposition of immunoglobulins increased with age. Absence of complement C3c or electron dense deposits associated with this mesangial localization suggests that immunoglobulins were not deposited as immune complexes. Accumulation of non-phlogogenic immunoglobulins in the mesangium of normal rats supports the concept that the mesangium is constantly perfused by circulating macro-molecules and filtration residues. The results indicate problems of interpretation of the significance of endogenous immunoglobulin deposition in models of experimental glomerulonephritis, even in studies involving weanling rats.

6

Srikumaran, S., E. A. Kluever, D. V. Onisk, and K. Hariharan. "Quantitation of bovine immunoglobulins in culture fluids by use of sandwich radioimmunoassay with monoclonal antibodies." American Journal of Veterinary Research 52, no. 2 (February 1, 1991): 243–46. http://dx.doi.org/10.2460/ajvr.1991.52.02.243.

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SUMMARY Bovine immunoglobulin isotype-specific murine monoclonal antibodies were used in sandwich radioimmunoassays to detect and quantitate bovine IgG1, IgG2, IgM, and IgA in culture fluids. The concentrations of bovine immunoglobulins in unknown samples were extrapolated from standard curves generated with bovine monoclonal immunoglobulins. The lowest detection limits for the bovine immunoglobulin isotypes ranged from 65 to 270 ng/ml.

7

Westhrin, Marita, Vlado Kovcic, Zejian Zhang, Siv H. Moen, Tonje Marie Vikene Nedal, Albert Bondt, Stephanie Holst, et al. "Monoclonal immunoglobulins promote bone loss in multiple myeloma." Blood 136, no. 23 (December 3, 2020): 2656–66. http://dx.doi.org/10.1182/blood.2020006045.

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Abstract Most patients with multiple myeloma develop a severe osteolytic bone disease. The myeloma cells secrete immunoglobulins, and the presence of monoclonal immunoglobulins in the patient’s sera is an important diagnostic criterion. Here, we show that immunoglobulins isolated from myeloma patients with bone disease promote osteoclast differentiation when added to human preosteoclasts in vitro, whereas immunoglobulins from patients without bone disease do not. This effect was primarily mediated by immune complexes or aggregates. The function and aggregation behavior of immunoglobulins are partly determined by differential glycosylation of the immunoglobulin-Fc part. Glycosylation analyses revealed that patients with bone disease had significantly less galactose on immunoglobulin G (IgG) compared with patients without bone disease and also less sialic acid on IgG compared with healthy persons. Importantly, we also observed a significant reduction of IgG sialylation in serum of patients upon onset of bone disease. In the 5TGM1 mouse myeloma model, we found decreased numbers of lesions and decreased CTX-1 levels, a marker for osteoclast activity, in mice treated with a sialic acid precursor, N-acetylmannosamine (ManNAc). ManNAc treatment increased IgG-Fc sialylation in the mice. Our data support that deglycosylated immunoglobulins promote bone loss in multiple myeloma and that altering IgG glycosylation may be a therapeutic strategy to reduce bone loss.

8

Gong, Yuxin, Bo Liao, Dejun Peng, and Quan Zou. "Accurate Prediction and Key Feature Recognition of Immunoglobulin." Applied Sciences 11, no. 15 (July 27, 2021): 6894. http://dx.doi.org/10.3390/app11156894.

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Immunoglobulin, which is also called an antibody, is a type of serum protein produced by B cells that can specifically bind to the corresponding antigen. Immunoglobulin is closely related to many diseases and plays a key role in medical and biological circles. Therefore, the use of effective methods to improve the accuracy of immunoglobulin classification is of great significance for disease research. In this paper, the CC–PSSM and monoTriKGap methods were selected to extract the immunoglobulin features, MRMD1.0 and MRMD2.0 were used to reduce the feature dimension, and the effect of discriminating the two–dimensional key features identified by the single dimension reduction method from the mixed two–dimensional key features was used to distinguish the immunoglobulins. The data results indicated that monoTrikGap (k = 1) can accurately predict 99.5614% of immunoglobulins under 5-fold cross–validation. In addition, CC–PSSM is the best method for identifying mixed two–dimensional key features and can distinguish 92.1053% of immunoglobulins. The above proves that the method used in this paper is reliable for predicting immunoglobulin and identifying key features.

9

Lock, R. J., and D. J. Unsworth. "Immunoglobulins and immunoglobulin subclasses in the elderly." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 40, no. 2 (March 1, 2003): 143–48. http://dx.doi.org/10.1258/000456303763046067.

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Background: Published data imply that adult concentrations are achieved for all Ig isotypes and plateau by 15--18 years of age. Recent data, however, suggest that these results are not applicable in the elderly. There are no equivalent data for IgG subclasses. We present reference range data for an elderly UK patient population, for IgG, IgA, IgM and IgG subclasses. Methods: Serum immunoglobulins were reviewed on samples from 1146 patients > 60 years of age and 925 patients aged 18--60 years. Serum IgG subclasses were reviewed on samples from 498 patients >60 years and 484 patients aged 18--60 years. All Igs and subclasses were measured by nephelometry. Reference ranges were derived by probability plotting. Results: Serum median IgG and IgM concentrations are reduced in the elderly (IgG female P < 0·001, IgG male P < 0·03; IgM female P < 0·001, IgM male P < 0·001). Serum IgA concentrations are maintained. Indeed, men showed a slight increase in serum IgA with age ( P = 0·03). Few differences dependent on gender were seen. Median IgM was lower in men in the younger age groups (18--60 years P < 0·001; 61--70 years P = 0·017). IgG2 is reduced in elderly men ( P = 0·002) and IgG, reduced in elderly women ( P = 0·009). Conclusions: We advocate that centres offering these investigations provide local, method-dependent reference ranges, and suggest an approach as to how this might be achieved.

10

Walther, Stefanie, Tamara V. Rusitzka, Ulrike S. Diesterbeck, and Claus-Peter Czerny. "Equine immunoglobulins and organization of immunoglobulin genes." Developmental & Comparative Immunology 53, no. 2 (December 2015): 303–19. http://dx.doi.org/10.1016/j.dci.2015.07.017.

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11

Butler, J. E., and W. R. Brown. "The immunoglobulins and immunoglobulin genes of swine." Veterinary Immunology and Immunopathology 43, no. 1-3 (October 1994): 5–12. http://dx.doi.org/10.1016/0165-2427(94)90114-7.

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12

Wagner, Bettina. "Immunoglobulins and immunoglobulin genes of the horse." Developmental & Comparative Immunology 30, no. 1-2 (January 2006): 155–64. http://dx.doi.org/10.1016/j.dci.2005.06.008.

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13

Hasegawa, Haruki. "Aggregates, Crystals, Gels, and Amyloids: Intracellular and Extracellular Phenotypes at the Crossroads of Immunoglobulin Physicochemical Property and Cell Physiology." International Journal of Cell Biology 2013 (2013): 1–22. http://dx.doi.org/10.1155/2013/604867.

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Recombinant immunoglobulins comprise an important class of human therapeutics. Although specific immunoglobulins can be purposefully raised against desired antigen targets by various methods, identifying an immunoglobulin clone that simultaneously possesses potent therapeutic activities and desirable manufacturing-related attributes often turns out to be challenging. The variable domains of individual immunoglobulins primarily define the unique antigen specificities and binding affinities inherent to each clone. The primary sequence of the variable domains also specifies the unique physicochemical properties that modulate various aspects of individual immunoglobulin life cycle, starting from the biosynthetic steps in the endoplasmic reticulum, secretory pathway trafficking, secretion, and the fate in the extracellular space and in the endosome-lysosome system. Because of the diverse repertoire of immunoglobulin physicochemical properties, some immunoglobulin clones’ intrinsic properties may manifest as intriguing cellular phenotypes, unusual solution behaviors, and serious pathologic outcomes that are of scientific and clinical importance. To gain renewed insights into identifying manufacturable therapeutic antibodies, this paper catalogs important intracellular and extracellular phenotypes induced by various subsets of immunoglobulin clones occupying different niches of diverse physicochemical repertoire space. Both intrinsic and extrinsic factors that make certain immunoglobulin clones desirable or undesirable for large-scale manufacturing and therapeutic use are summarized.

14

Korhonen, Hannu, P. Marnila, and H. S. Gill. "Milk immunoglobulins and complement factors." British Journal of Nutrition 84, S1 (November 2000): 75–80. http://dx.doi.org/10.1017/s0007114500002282.

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The importance of colostrum for the growth and health of newborn offspring is well known. In bovine colostrum, the antibody (immunoglobulin) complement system provides a major antimicrobial effect against a wide range of microbes and confers passive immunity until the calf's own immune system has matured. Bovine serum and lacteal secretions contain three major classes of immunoglobulins: IgG, IgM and IgA. The immunoglobulins are selectively transported from the serum into the mammary gland, as a result of which the first colostrum contains very high concentrations of immunoglobulins (40–200 mg/ml). IgG1 accounts for over 75 % of the immunoglobulins in colostral whey, followed by IgM, IgA and IgG2. All these immunoglobulins decrease within a few days to a total immunoglobulin concentration of 0.7–1.0 mg/ml, with IgG1 representing the major Ig class in milk throughout the lactation period. Together with the antibodies absorbed from colostrum after birth, the complement system plays a crucial role in the passive immunisation of the newborn calf. The occurrence of haemolytic or bactericidal complement activity in bovine colostrum and milk has been demonstrated in several studies. This review deals with the characteristics of bovine Igs and the complement system to be exploited as potential ingredients for health-promoting functional foods.

15

Спицын, А. Н., Д. В. Уткин, М. Н. Киреев, М. В. Овчинникова, О. С. Кузнецов, П. С. Ерохин, and В. И. Кочубей. "Спектрофотометрическая характеристика конъюгатов иммуноглобулинов для диагностики возбудителей особо опасных инфекций." Журнал технической физики 128, no. 3 (2020): 430. http://dx.doi.org/10.21883/os.2020.03.49071.76-19.

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The possibility of using spectrophotometric analysis to characterize fluorescent immunoglobulins as a control method was considered. A comparative analysis of the optical properties of fluorescent immunoglobulin preparations and their constituent components - immunoglobulins, fluorochrome was carried out. The results suggest that the proposed methodological approach of optical detection of labeled immunoglobulin molecules is promising for controlling the preparation of conjugates used in the formulation of immunological reactions to identify specific antigens of pathogens of particularly dangerous infections.

16

Shehzad, Muzzamil, Tayyab Ali, Nusrat Bibi, and Shoaib Shafique. "A comprehensive review on preparation of pure immunoglobulins Authors." International Journal of Natural Medicine and Health Sciences 2, no. 1 (December 31, 2022): 48–55. http://dx.doi.org/10.52461/ijnms.v2i1.1372.

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Immunoglobulins are also known as antibodies. Plasma cells are responsible for the production of immunoglobulins. Beta cells are activated against a pathogenic attack and facilitated the formation of different types of immunoglobulins naturally. These immunoglobulins are also artificially synthesized by non-specific laboratorial techniques include fractionation precipitation, electrophoretic methods, gel filtration chromatography, ion exchange chromatography, hydrophobic chromatography and by the specific immuno- adsorbent methods. Third generation immunoglobulins are effectively used for therapeutic purpose against viral infections intravenously. Second generation immunoglobulins synthesis involved removal of anti-complement contaminants and IgG aggregates, through enzymatic degradation and chemical modification. The harmful effects of intravenous immunoglobulins can be reduced by using ultraviolet light, P-propiolactone, and pepsin at pH 4. Intravenous immunoglobulin drugs lead to anti-inflammatory and immunomodulatory effects in various infections. The mechanism of action of intravenous immunoglobulins is dependent on the binding between the Fc portion of injected IgG and target cell receptors. Radiolabeling is performed by two methods as in vivo, in which radiolabeled antibodies are incorporated into the body to bind with the antibodies and in vitro method, radioactive material is bound with already formed antibodies. This chapter highlighted the artificial methods adopted for production of radiolabeled immunoglobulins holding significant therapeutic and diagnostic applications.

17

Wiese, Rick, Aliya Gessling, and David Hayes. "Multiplex immunoglobulin isotyping assays for human, mouse or rat serum samples (65.25)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 65.25. http://dx.doi.org/10.4049/jimmunol.186.supp.65.25.

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Abstract The determination of serum immunoglobulin isotype concentrations is an important indicator of immunological health. We have constructed several multiplex isotyping assays on the Luminex® assay platform. These assays allow for the analysis of human, mouse and rat serum, tissue culture or body fluid samples. The human isotyping assay enables the quantification of immunoglobulins A, M, G1, G2, G3 and G4 in a single assay well. While the mouse isotyping assay cover immunoglobulins A, M, G1, G2A, G2B, and G3, and the rat isotyping immunoglobulins A, E, M, G1, G2A, G2B, G2C. Since the concentrations of IgE in human and mouse samples are typically much lower than the other immunoglobulin isotypes we have also designed separate assays for mouse and human IgE analysis. This collection of assays allows for the rapid, multiplex analysis of major immunoglobulin isotypes in the human , as well as the two predominant research maodels, rat and mouse.

18

Conti, Francesca, Mattia Moratti, Lucia Leonardi, Arianna Catelli, Elisa Bortolamedi, Emanuele Filice, Anna Fetta, et al. "Anti-Inflammatory and Immunomodulatory Effect of High-Dose Immunoglobulins in Children: From Approved Indications to Off-Label Use." Cells 12, no. 19 (October 7, 2023): 2417. http://dx.doi.org/10.3390/cells12192417.

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Background: The large-scale utilization of immunoglobulins in patients with inborn errors of immunity (IEIs) since 1952 prompted the discovery of their key role at high doses as immunomodulatory and anti-inflammatory therapy, in the treatment of IEI-related immune dysregulation disorders, according to labelled and off-label indications. Recent years have been dominated by a progressive imbalance between the gradual but constant increase in the use of immunoglobulins and their availability, exacerbated by the SARS-CoV-2 pandemic. Objectives: To provide pragmatic indications for a need-based application of high-dose immunoglobulins in the pediatric context. Sources: A literature search was performed using PubMed, from inception until 1st August 2023, including the following keywords: anti-inflammatory; children; high dose gammaglobulin; high dose immunoglobulin; immune dysregulation; immunomodulation; immunomodulatory; inflammation; intravenous gammaglobulin; intravenous immunoglobulin; off-label; pediatric; subcutaneous gammaglobulin; subcutaneous immunoglobulin. All article types were considered. Implications: In the light of the current imbalance between gammaglobulins’ demand and availability, this review advocates the urgency of a more conscious utilization of this medical product, giving indications about benefits, risks, cost-effectiveness, and administration routes of high-dose immunoglobulins in children with hematologic, neurologic, and inflammatory immune dysregulation disorders, prompting further research towards a responsible employment of gammaglobulins and improving the therapeutical decisional process.

19

Sokołowska, J., J. Micuń, K. Zabielska, E. Malicka, and R. Lechowski. "Immunohistochemical study of expression of immunoglobulins in canine B-cell lymphomas." Polish Journal of Veterinary Sciences 13, no. 4 (December 1, 2010): 623–28. http://dx.doi.org/10.2478/v10181-010-0004-5.

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Immunohistochemical study of expression of immunoglobulins in canine B-cell lymphomasNineteen canine lymphomas were included in this study. Tumors were classified according to the updated Kiel classification adapted for canine lymphomas by Fournel-Fleury et al. Immunoglobulin light chains (κ and λ) and IgM and IgG expression were determined by immunohistochemical method. In all examined cases neoplastic cells were positive for one of the immunoglobulin light chains. Expression of λ light chains and κ light chains was observed in 18/19 and 1/19 tumors, respectively. In the majority of neoplastic cells in each examined specimen this reaction had a membranous pattern (sκ/sλ). In all examined cases the presence of immunoglobulin light chains was also observed in the cytoplasm of some neoplastic cells (cκ/cλ). These cells were usally rare and never constituted a dominant population. The expression of immunoglobulin was found in 13/19 cases. Most lymphomas were sIgM positive (11/13 cases). In one case expression of IgG was found, and in another lymphoma two populations of neoplastic cells with different expression of examined immunoglobulins (cells with IgM+and IgG+phenotypes) were observed. The reaction also had a membranous pattern. The cells containing cytoplasmic immunoglobulins were rare, and in most cases were of the same type as the surface immunoglobulins. Our study has confirmed that canine lymphomas are a monoclonal proliferation of B-cells usually expressing immunoglobulin λ light chains and that the vast majority of tumors deriving from B-cells express IgM. Our study also indicates a possibility of occurence of biclonal lymphomas in canine species.

20

Tsavaris, N., D. Tsigalacis, C. Kosmas, CH Koufos, G. Vaiopoulos, M. Tzivras, G. Kouraklis, et al. "Preliminary Evaluation of the Potential Prognostic Value of Serum Levels of Immunoglobulins (IgA, IgM, IgG, IgE) in Patients with Gastric Cancer." International Journal of Biological Markers 13, no. 2 (April 1998): 87–91. http://dx.doi.org/10.1177/172460089801300204.

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Sixty patients with advanced gastric carcinoma who refused to receive cytotoxic chemotherapy were examined for serum immunoglobulin levels (IgG, IgM, IgA, IgE). Three samples were obtained every two months thereafter. The group of patients who had above-normal values of one or more of the examined immunoglobulins had a longer survival than the other (p<0.024). Immunoglobulin values were independent of the Helicobacter pylori antibody titer and of acute phase reactants. It is concluded that survival potentially correlates with serum immunoglobulin levels. Further studies including larger numbers of patients and correlating serum immunoglobulin levels with specific clinical parameters are needed to establish the prognostic role of serum immunoglobulins in patients with gastric carcinoma.

21

Kouvalainen, K., and I. Moilanen. "Intrapair Similarity of Immunoglobulin Levels in Twins." Acta geneticae medicae et gemellologiae: twin research 36, no. 4 (October 1987): 509–15. http://dx.doi.org/10.1017/s0001566000006887.

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AbstractLevels of immunoglobulins IgG, IgA, IgM and IgE were determined in 8 MZ and 14 DZ twin pairs at the ages of 6-11 years, 12-17 years and 15-20 years. Intrapair similarity in immunoglobulin levels was found to be higher in the MZ than in the DZ twins, especially in the case of immunoglobulins IgA and IgM.

22

Zweig, M. H., G. Csako, C. C. Benson, B. D. Weintraub, and B. B. Kahn. "Interference by anti-immunoglobulin G antibodies in immunoradiometric assays of thyrotropin involving mouse monoclonal antibodies." Clinical Chemistry 33, no. 6 (June 1, 1987): 840–44. http://dx.doi.org/10.1093/clinchem/33.6.840.

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Abstract "Sandwich"-type assays are subject to positive interference by the patient's "heterophile" antibodies. If present, these bind to the animal immunoglobulins in the assay reagents, forming artefactual sandwiches indistinguishable from those formed with the analyte itself. Immunoglobulins from non-immunized animals, added to the assay reagents, can diminish this effect by blocking the patient's antibodies. Elsewhere, we studied several patients with anti-mouse immunoglobulin activity, whose serum gave spuriously high results for thyrotropin (TSH) concentrations. Here we have studied this phenomenon by adding, to pooled zero-TSH serum, antibodies to mouse, goat, and horse immunoglobulins and then assaying TSH by several other sandwich-type assays involving mouse monoclonal antibodies. Assays not supplemented with blocking immunoglobulins from mice or other animals were more susceptible to this effect. When large amounts of antibody were added, the antibody excess diminished the interference. However, the presence of blocking immunoglobulins could reverse such antibody excess, actually enhancing, instead of diminishing, the positive interference. Users should be aware that blocking immunoglobulins may diminish but not necessarily eliminate this problem with such assays.

23

Machado Neto, Raul, Irineu Umberto Packer, Gladys Villas Boas do Prado, Rosana Bessi, and Patricia Pauletti. "Colostral immunoglobulins absorption in Canchim and Nelore calves." Revista Brasileira de Zootecnia 33, no. 6 (December 2004): 1544–47. http://dx.doi.org/10.1590/s1516-35982004000600021.

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The efficiency of absorption of colostral immunoglobulins was evaluated in five Canchim and seven Nelore calves. They received colostrum pools with concentration of 70.20 ± 6.14 mg/mL through esofageal feeder at 2, 12, 24 and 36 hours after birth. The immunoglobulins concentrations of the pools were estimated through specific gravity and measured by radial immunodifusion. In the blood collection at birth and during the first 70 days of life, the total protein was assayed by biuret method and the immunoglobulins were assayed by radial immunodifusion. Data were analysed as a randomized split-plot statistical model. The highest concentrations of serum immunoglobulins and total protein were observed at 24 hours of age. No significant differences (P>0.5484) were observed for immunoglobulins concentration at 24 hours, with concentrations of 28.80 ± 7.24 mg/mL for Canchim and 27.32 ± 9.54 mg/mL for Nelore. The efficiency for immunoglobulins absorption was not significantly different (P>0.8715) between breeds, 64.04 ± 7.74% for Canchim and 62.30 ± 6.93% for Nelore. The lack of statistical significance persisted until the fourtieth day of life, period of maternal immunoglobulin predominance in the calves blood circulation. In the following period, from 40 to 70 days of age, phase of establishment of the endogenous production of immunoglobulin, differences in the IgG concentrations between the two groups were detected refflecting a possible breed effect difference. The process of colostral IgG absorption by the newborn calves was not affected by breed. The differences between breeds in the calves serum IgG were related to the phase of endogenous production of antibodies.

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Dimitroglou, Margarita, Rozeta Sokou, Nicoletta Iacovidou, Abraham Pouliakis, Georgios Kafalidis, Theodora Boutsikou, and Zoi Iliodromiti. "Anti-SARS-CoV-2 Immunoglobulins in Human Milk after Coronavirus Disease or Vaccination—Time Frame and Duration of Detection in Human Milk and Factors That Affect Their Titers: A Systematic Review." Nutrients 15, no. 8 (April 14, 2023): 1905. http://dx.doi.org/10.3390/nu15081905.

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Human milk (HM) of mothers infected with or vaccinated against SARS-CoV-2 contains specific immunoglobulins, which may protect their offspring against infection or severe disease. The time frame and duration after infection or vaccination, during which these immunoglobulins are detected in HM, as well as the major factors that influence their levels, have not been fully elucidated. This systematic review aimed to collect the existing literature and describe the immune response, specifically regarding the immunoglobulins in HM after COVID-19 disease or vaccination in non-immune women. We conducted a systematic search of PubMed and Scopus databases to identify studies published up until 19 March 2023. In total, 975 articles were screened, and out of which 75 were identified as being relevant and were finally included in this review. Infection by SARS-CoV-2 virus primarily induces an IgA immune response in HM, while vaccination predominantly elevates IgG levels. These immunoglobulins give HM a neutralizing capacity against SARS-CoV-2, highlighting the importance of breastfeeding during the pandemic. The mode of immune acquisition (infection or vaccination) and immunoglobulin levels in maternal serum are factors that seem to influence immunoglobulin levels in HM. Further studies are required to determine the impact of other factors, such as infection severity, lactation period, parity, maternal age and BMI on immunoglobulin level in HM.

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Pohanka, M. "Evaluation of Immunoglobulin Production during Tularaemia Infection in BALB/c Mouse Model." Acta Veterinaria Brno 76, no. 4 (2007): 579–84. http://dx.doi.org/10.2754/avb200776040579.

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Abstract:

The chromatographic technique was used for assay of time-dependent content of antibodies in mice BALB/c infected by tularaemia. The assay was consequently performed on two types of chromatographic sorbents. The first was commercial CBindTM specific for serum immunoglobulins IgM, IgG and IgA. The second was originally prepared sorbent including protein G covalently bound on EnzacrylRAH particles. This sorbent has specificity for immunoglobulin IgG and its subclasses only. Finally, mass concentration of immunoglobulins in serum was determined. Two curves expressing time behavior of immunoglobulin content (immunoglobulin mass concentration vs. days after immunization) were used for finding the proper mathematical function. The function found was sigmoid; subsequently, appropriate constants needed for function solution were evaluated.

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Campos-Neto, Antonio, Isabelle Suffia, Karen A. Cavassani, Shyian Jen, Kay Greeson, Pamela Ovendale, João S. Silva, Steven G. Reed, and Yasir A. W. Skeiky. "Cloning and Characterization of a Gene Encoding an Immunoglobulin-Binding Receptor on the Cell Surface of Some Members of the Family Trypanosomatidae." Infection and Immunity 71, no. 9 (September 2003): 5065–76. http://dx.doi.org/10.1128/iai.71.9.5065-5076.2003.

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ABSTRACT Several members of the Trypanosomatidae family, when freshly isolated from their mammalian hosts, have immunoglobulins adsorbed to their cell surfaces. However, a significant portion of these antibody molecules is not parasite specific, i.e., the immunoglobulins are bound to the parasite's cell surface molecules via noncognitive interactions. It has been proposed that this noncognitive adsorption of immunoglobulins to the parasite is mediated by an Fc-like receptor present in several members of the Trypanosomatidae family. However, the molecular identification of this receptor has never been defined. Here, we describe the cloning of a gene encoding a protein that might represent this molecule. The gene, named Lmsp1, was cloned by screening a Leishmania major cDNA expression library using a rabbit antiserum. Lmsp1 is present in both Leishmania and Trypanosoma and is expressed in all developmental stages of these parasites. The predicted protein has a molecular mass of 16.6 kDa and contains an RGD sequence starting at residue 104 and three cysteine residues at positions 55, 74, and 116. The purified recombinant protein strongly binds to normal immunoglobulins of various animal species (humans, rabbits, sheep, goats, guinea pigs, donkeys, rats, and mice) and the binding to human immunoglobulins appears to be immunoglobulin G (IgG) and IgM isotype specific. Moreover, Lmsp1 binds to both purified Fc and Fab fragments of IgG from both humans and rabbits. The mapping of the Lmsp1 epitopes that bind human IgG revealed that different sequences of the molecule bind to Fc or Fab. In addition, fluorescence-activated cell sorter analyses with a specific rabbit anti-Lmsp1 antiserum showed that Lmsp1 is associated with the parasite's cell surface. Finally, inhibition experiments point to an active role of this molecule in the immunoglobulin-mediated attachment and penetration of Trypanosoma cruzi in its macrophage host cells, thus suggesting that Lmsp1 is a putative Trypanosomatidae immunoglobulin receptor.

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Kim, Hwan Keun, Fabiana Falugi, Dominique Missiakas, and Olaf Schneewind. "Expression of two immunoglobulin binding proteins is necessary for S. aureus to avoid host mediated innate and adaptive immune systems (P3138)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 186.16. http://dx.doi.org/10.4049/jimmunol.190.supp.186.16.

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Abstract Human or animal infections with S. aureus do not elicit protective immunity against staphylococcal diseases. Staphylococci are notorious to deploy a wide spectrum of strategies to avoid host immune system. Previous work revealed that both innate and adaptive immune systems are hampered by the expression of two immunoglobulin binding proteins; staphylococcal protein A (SpA) and staphylococcal binder of immunoglobulins (Sbi). Staphylococcal protein A, a molecule that associates with both Fc and Fab portions of immunoglobulins, is necessary 1) to neutralize the antibody mediated opsonophagocytosis and 2) to trigger the expansion and apoptotic demise of B cell populations. The second immunoglobulin binding protein, Sbi, can associate with Fc portion of immunoglobulin and complement factor C3 to disable a critical juncture between the innate and adaptive immunity. Although much of biochemical analysis revealed how the two staphylococcal proteins engage with immunoglobulins for many years, their role as immuno modulatory virulence factors in vivo has not been fully understood. We have investigated the significance of immunoglobulin association with staphylococci during acute and chronic infection in animal model and characterized the molecular mechanisms to avert host immune defense system. Strategies are also discussed on how the two secreted products of staphylococci may be exploited for the development of vaccines and therapeutics.

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Westhrin, Marita, Vlado Kovcic, Albert Bondt, Stephanie Holst, Zejian Zhang, Anders Sundan, Tobias S. Slørdahl, Anders Waage, Manfred Wuhrer, and Therese Standal. "Glycosylationof Immunoglobulins Determine Bone Loss in Multiple Myeloma." Blood 134, Supplement_1 (November 13, 2019): 4324. http://dx.doi.org/10.1182/blood-2019-122542.

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About 80% of patients with multiple myeloma develop a severe osteolytic bone disease causing pain and fractures. The myeloma cells secrete immunoglobulins and the presence of monoclonal immunoglobulins in serum is a hallmark of the disease. Immunoglobulins play a role in bone loss, but have not been linked with the bone disease in multiple myeloma. In this work, we isolated immunoglobulins from serum of myeloma patients using protein G coupled magnetic beads and columns. We found that immunoglobulins from patients with bone disease (n=16) promoted osteoclast differentiation when added to human monocyte-derived pre-osteoclasts (p=0.006). We next fractionated the immunoglobulin samples by size-exclusion chromatography and found that the "osteoclast promoting activity" was in the high-molecular weight fractions, suggesting that they are in complexes. Since extent of complex formation may be determined by glycosylation, we examined whether there is a difference in immunoglobulin glycosylation between healthy controls and patients, and whether it changes during disease progression. To this end we analysed IgG glycosylation in serum samples from patients (n=72) and age and sex matched controls (n=51). These analyses showed that patient IgG was less galactosylated (p=0.02) and less sialylated (p=0.04) compared with control IgG. Moreover, patients with bone disease (n=43) had significantly less galactose on IgG compared with patients without bone disease (p=0.02, n=33). Supporting this data, we found that galactosidase treatment of immunoglobulins from patients without bone disease induced osteoclastogenesis (p=0.03), whereas addition of galactose to immunoglobulins of patients with bone disease removed their pro-osteoclastogenic effect (p=0.01). Further, the glycosyltransferases ST6GAL1 and B4GALT11, which add sialic acid and galactose to the sugar chain, respectively, are less expressed in plasma cells obtained from patients with bone disease (n=137) compared with those without (n=36, p<0.002, p<0.001, GSE755). Importantly, we observed a significant reduction of IgG glycosylation (p=0.02, n=8) in serum samples obtained from individual patients before and after the onset of bone disease. Taken together, our data support that immunoglobulins promote bone loss in multiple myeloma. Disclosures No relevant conflicts of interest to declare.

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Mehdiratta, N. K., and H. P. Singh. "Immunogobulins and Thermal Burns Infections." Indian Journal of Plastic Surgery 20, no. 01 (February 1987): 018–22. http://dx.doi.org/10.1055/s-0043-1772536.

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SummaryBurns patients have higher susceptibility to infections, causes of which are many fold. Leakage of immunoglobulins in blister fluid is one of them. The present work was undertaken to find out the relationship between the types of infections and the levels of various immunoglobulins in the sera of burn patients. Radial immunodiffusion technique of Mancini was utilized to measure the levels. It was observed that all types of infections produced rise in immunoglobulin levels. In mixed and Pseudomonas infections the rise of all major immunoglobulins was found statistically insignificant while in fungally invaded patients IgM levels were significantly raised but on excision of the invaded areas, IgM levels dropped to within normal range.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 693 (March 1998): 12. http://dx.doi.org/10.2165/00128415-199806930-00040.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 709 (July 1998): 7. http://dx.doi.org/10.2165/00128415-199807090-00025.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 719 (September 1998): 8. http://dx.doi.org/10.2165/00128415-199807190-00026.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 727 (November 1998): 8. http://dx.doi.org/10.2165/00128415-199807270-00024.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 734 (January 1999): 8. http://dx.doi.org/10.2165/00128415-199907340-00022.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 737 (February 1999): 8. http://dx.doi.org/10.2165/00128415-199907370-00027.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 749 (May 1999): 9. http://dx.doi.org/10.2165/00128415-199907490-00022.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 1170 (September 2007): 21–22. http://dx.doi.org/10.2165/00128415-200711700-00053.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 1170 (September 2007): 22. http://dx.doi.org/10.2165/00128415-200711700-00058.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 1193 (March 2008): 17. http://dx.doi.org/10.2165/00128415-200811930-00053.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 540 (March 1995): 9. http://dx.doi.org/10.2165/00128415-199505400-00029.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 547 (April 1995): 7. http://dx.doi.org/10.2165/00128415-199505470-00019.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 553 (June 1995): 8. http://dx.doi.org/10.2165/00128415-199505530-00029.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 559 (July 1995): 8. http://dx.doi.org/10.2165/00128415-199505590-00021.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 589 (February 1996): 8. http://dx.doi.org/10.2165/00128415-199605890-00024.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 590 (March 1996): 12. http://dx.doi.org/10.2165/00128415-199605900-00036.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 594 (March 1996): 9. http://dx.doi.org/10.2165/00128415-199605940-00034.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 601 (May 1996): 9. http://dx.doi.org/10.2165/00128415-199606010-00027.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 605 (June 1996): 9. http://dx.doi.org/10.2165/00128415-199606050-00029.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 426 (November 1992): 9. http://dx.doi.org/10.2165/00128415-199204260-00040.

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&NA;. "Immunoglobulins." Reactions Weekly &NA;, no. 427 (November 1992): 8. http://dx.doi.org/10.2165/00128415-199204270-00027.

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