scholarly journals THE IMMUNOGLOBULINS OF MICE

1965 ◽  
Vol 122 (1) ◽  
pp. 41-58 ◽  
Author(s):  
John L. Fahey ◽  
Stewart Sell
Keyword(s):  
Serum Level ◽  
Control Mechanism ◽  
High Serum ◽  
The Other ◽  
Fractional Rate ◽  
Myeloma Proteins ◽  
Mouse Immunoglobulin ◽  
Γ Globulins ◽  
Metabolic Properties ◽  
Low Serum

The metabolic properties of immunoglobulin were investigated by comparing five classes of mouse immunoglobulin. Three forms of 7S immunoglobulin had different rates of catabolism. The fractional rates of catabolism were found to be about 13 per cent per day for 7S γ2a-globulin; 25 per cent for 7S γ2b-globulin; and 17 per cent for 7S γ1-globulin. Catabolism of the three classes of 7S γ-globulin (γ2a, γ2b, and γ1) were prolonged at low serum 7S γ-globulin levels and accelerated at high serum 7S γ-globulin levels. Each of the 7S γ-globulin components was influenced by the serum level of the other mouse 7S γ-globulin components and by exogenously administered human 7S γ-globulin. They were not appreciably altered, however, by the serum level of IgA (γ1A-, ß2A-globulin). The progressively changing (longer) half-times observed in turnover studies of normal IgG (7S γ-globulin) may be caused by catabolic heterogeneity of normal 7S immunoglobulins which are immunochemically and catabolically related to γ2a-, γ2b-, and 7S γ1-myeloma proteins. These studies indicate that the 7S γ2a-, 7S γ2b-, and 7S γ1-globulins share a common catabolic control mechanism. This mechanism is influenced by the serum level of each of these components, but is independent of the serum level of IgA (γ1A-globulin) and probably is independent of IgM (γ1M-globulin). Catabolism of IgA (γ1A-, ß2A-globulin) and IgM (γ1M-globulin) was much more rapid than the catabolism of the 7S γ-globulins. The halftimes of the IgA and IgM were approximately 1.2 and 0.5 days respectively. The fractional rate of catabolism of IgA and IgM seemed to be independent of their serum concentration. The rate of catabolism, as well as the rate of synthesis, was shown to play a major role in determining the serum level of each class of immunoglobulin.

scholarly journals ANTIGENIC RELATIONSHIPS BETWEEN IMMUNE GLOBULINS AND CERTAIN RELATED PARAPROTEINS IN MAN

1961 ◽  
Vol 114 (4) ◽  
pp. 521-533 ◽  
Author(s):  
Edward C. Franklin ◽  
Denis R. Stanworth
Keyword(s):  
Biological Properties ◽  
The Other ◽  
Antigenic Specificity ◽  
Myeloma Proteins ◽  
Antigenic Properties ◽  
Immune Globulins ◽  
Γ Globulins ◽  
Antigenic Relationships ◽  
Gel Diffusion ◽  
Bence Jones Proteins

The antigenic properties of normal 19S γ-globulin, pathologic macroglobulins, ß2A-myeloma proteins, and Bence Jones proteins have been compared with 7S γ-globulin and the small 3.5S units derived from it by gel diffusion precipitin techniques. These studies demonstrate that the determinant groups on the 7S γ-globulin molecule responsible for the cross-reaction with each of the other proteins are associated with the two fragments of 7S γ-globulin which have the antibody-combining sites. The antigenic specificity of the 7S γ-globulin which distinguishes it from each of these proteins is associated primarily with the fragment that is richest in hexose and can not combine with antigen. However when compared with certain of the paraproteins additional antigenic specificity was also found to reside in the fragments with antibody-combining activity. The finding of similar antigenic relationships in rabbit γ-globulins suggests that some of the biological properties associated only with the 7S γ-globulins and not with the other immune globulins may reside in the fragment which also carries the antigenic specificity of the protein.

scholarly journals Comparison of the dimensions of the combining sites of the dinitrophenyl-binding immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 by spin-label mapping

1977 ◽  
Vol 165 (2) ◽  
pp. 199-206 ◽  
Author(s):  
Keith J. Willan ◽  
Derek Marsh ◽  
Christopher A. Sunderland ◽  
Brian J. Sutton ◽  
Simon Wain-Hobson ◽  
...  
Keyword(s):  
Binding Sites ◽  
Immunoglobulin A ◽  
Binding Activity ◽  
The Other ◽  
Spin Labels ◽  
Metal Site ◽  
Myeloma Proteins ◽  
Spin Resonance ◽  
Mouse Immunoglobulin ◽  
Positively Charged

The mouse immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 all possess dinitrophenyl (Dnp)-binding activity. Differences in specificities were shown by measuring the affinities of a variety of haptens. By using a series of Dnp-spin-labelled haptens, the dimensions of the binding sites of the three myeloma proteins were compared by the method described for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem. J.165, 177–197]. The dinitrophenyl ring is rigidly held in all three sites. The depths of the sites are all 1.1–1.2nm, but there are differences in the lateral dimensions at the entrance to the sites. For protein XRPC 25 these dimensions are 0.75nm×0.8nm, which may be compared with 0.85nm×1.1nm for protein MOPC 315 and ≥1.0nm×1.1nm for protein MOPC 460. The site in protein MOPC 460 is more symmetrical with respect to the plane of the dinitrophenyl ring than in either of the other two myeloma proteins and also allows greater penetration of solvent. In protein XRPC 25 a positively charged residue was located at the entrance to the site, similarly positioned to that reported for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem. J.165, 177–197]. All three proteins possess lanthanide-binding sites, but only in protein MOPC 315 is there antagonism between lanthanide and hapten binding. However, the effects of the diamagnetic La(III) on the electron-spin-resonance spectra of bound Dnp spin labels in both proteins MOPC 460 and XRPC 25 suggest an interaction between the two sites. Comparison of this effect with that caused by the addition of the paramagnetic Gd(III) enables the distance between the lanthanide- and hapten-binding sites to be calculated. In both proteins MOPC 460 and MOPC 315 the metal site is approx. 1.0nm from the nitroxide moiety of the spin-labelled hapten, but in protein XRPC 25 this distance is at least 2.0nm.

Fibronexus-Like Adhesion Sites are Present at the Invasive Zones of Human Epidermoid Carcinomas

1982 ◽  
Vol 40 ◽  
pp. 106-109
Author(s):  
Irwin I. Singer
Keyword(s):  
Cell Cycle ◽  
Serum Concentration ◽  
Substrate Binding ◽  
High Serum ◽  
Adhesion Sites ◽  
Substrate Adhesion ◽  
Focal Contacts ◽  
Adhesion Complex ◽  
Low Serum

Our previous results indicate that two types of fibronectin-cytoskeletal associations may be formed at the fibroblast surface: dorsal matrixbinding fibronexuses generated in high serum (5% FBS) cultures, and ventral substrate-adhering units formed in low serum (0.3% FBS) cultures. The substrate-adhering fibronexus consists of at least vinculin (VN) and actin in its cytoplasmic leg, and fibronectin (FN) as one of its major extracellular components. This substrate-adhesion complex is localized in focal contacts, the sites of closest substratum approach visualized with interference reflection microscopy, which appear to be the major points of cell-tosubstrate adhesion. In fibroblasts, the latter substrate-binding complex is characteristic of cultures that are arrested at the G1 phase of the cell cycle due to the low serum concentration in their medium. These arrested fibroblasts are very well spread, flattened, and immobile.

131J-speichernde pulmonale und ossäre Metastasen differenzierter Schilddrüsenkarzinome bei niedrigem Serum-Thyreoglobulinspiegel – Ausnahme in der Tumornachsorge?

1987 ◽  
Vol 26 (03) ◽  
pp. 139-142 ◽  
Author(s):  
G. Arning ◽  
O. Schober ◽  
H. Hundeshagen ◽  
Ch. Ehrenheim
Keyword(s):  
Serum Level ◽  
Thyroid Carcinoma ◽  
Bone Metastases ◽  
Differentiated Thyroid Carcinoma ◽  
Serum Thyroglobulin ◽  
Thyroglobulin Level ◽  
Low Serum

In the follow-up of differentiated thyroid carcinoma it is discussed whether the tumormarker thyroglobulin can replace the1311 scan, especially when the thyroglobulin serum level is normal. A positive1311 scan of metastases in the follow-up of patients with differentiated thyroid carcinoma combined with a low serum thyroglobulin level is extremely rare. The literature shows a frequency of about 4%. Recently we found 3 cases with a positive1311 scan demonstrating pulmonary and bone metastases whereas the serum thyroglobulin level was low.

scholarly journals Evaluation of the nature and etiologies of risk factors for diaphyseal atypical femoral fractures

2021 ◽  
Author(s):  
Hiroyuki Tsuchie ◽  
Naohisa Miyakoshi ◽  
Yuji Kasukawa ◽  
Koji Nozaka ◽  
Kimio Saito ◽  
...  
Keyword(s):  
Risk Factors ◽  
Multivariate Analyses ◽  
Femoral Fractures ◽  
Japanese Patients ◽  
High Serum ◽  
Control Group ◽  
Atypical Femoral Fractures ◽  
Factors Affecting ◽  
Lateral Curvature ◽  
Low Serum

Objectives: Differences in the mechanisms of subtrochanteric and diaphyseal atypical femoral fractures (AFFs) have been speculated in studies that have analyzed differences in the patients’ backgrounds. However, the etiologies of each type of AFF have not been investigated in detail. Therefore, this study aimed to investigate the nature and etiologies of the risk factors for diaphyseal AFFs. Materials and Methods: Eighty consecutive Japanese patients with 91 diaphyseal AFFs (the AFF group) and 110 age-matched female patients with osteoporosis (the non-AFF control group) were included. Their clinical data were compared and the factors affecting AFFs were investigated. Furthermore, the etiologies of the risk factors for diaphyseal AFFs were examined. Results: Multivariate analysis revealed that femoral serrated changes, bisphosphonate or denosumab usage, and lateral and anterior femoral curvatures were the risk factors for diaphyseal AFFs (p<0.0011, p=0.0137, and p<0.0001, respectively). Multivariate analyses also revealed that serrated changes and low serum 25(OH)D levels affected the lateral curvature (p=0.0088 and 0.0205, respectively), while serrated changes affected the anterior curvature (p=0.0006); each significantly affected the femoral curvature. In addition, a high serum calcium (Ca) level, lateral femoral curvature, and anterior femoral curvature were the predictors of serrated changes (p=0.0146, 0.0002, and 0.0098, respectively). Conclusion: The risk factors for diaphyseal AFFs were bone resorption inhibitor usage, a strong femoral curvature, and serrated changes. A low serum 25(OH)D level and serrated changes are the risk factors for lateral curvature, while a high serum Ca level is a risk factor for serrated changes.

Variations in serum T3, rT3, 3,3'-diiodothyronine and 3',5'-diiodothyronine induced by acute myocardial infarction and propranolol

1980 ◽  
Vol 94 (3) ◽  
pp. 341-345 ◽  
Author(s):  
Jens Faber ◽  
Carsten Kirkegaard ◽  
Ib Bo Lumholtz ◽  
Kaj Siersbæk-Nielsen ◽  
Thorkild Friis
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Enzyme System ◽  
Serum Levels ◽  
High Serum ◽  
Early Course ◽  
Deiodinase Activity ◽  
Serum T3 ◽  
Low Serum ◽  
Close Parallelism

Abstract. Serum levels of thyroxine, 3,5,3'-triiodothyronine (T3), 3,3',5'-triiodothyronine (rT3), 3,3'-diiodothyronine (3,3'-T2), 3',5'-diiodothyronine (3',5'-T2) and TSH were measured in two clinical situations which are both known to induce a low serum T3 high serum rT3 syndrome: 1) during the early course of acute myocardial infarction (AMI) and after recovery, and 2) before and during one week's propranolol medication (20 mg 4 times a day). In 10 patients with AMI serum levels of the iodothyronines were unchanged on admission to hospital (in average 6.6 h after onset of symptoms). However, already 24 h after onset of symptoms serum T3 and 3,3'T2 were reduced whereas serum rT3 and 3',5'-T2 were increased. Serum T3 and 3,3'-T2 reached a nadir on day 4 and 3, respectively, whereas serum rT3 and 3',5'-T2 reached peak values 24 h after onset of symptoms. In eight healthy, euthyroid volunteers propranolol medication induced similar changes in iodothyronine concentration as AMI did. However, the alterations were more delayed. Serum T3 decreased slowly reaching statistically significantly reduced values on day 7. Serum rT3 and 3',5'-T2 were significantly enhanced from day 3 and 4, respectively. A close parallelism in alterations of serum T3 and 3,3'-T2 levels was observed. Our data suggest that T3 in the two situations studied is a major precursor for 3,3'-T2 probably as a consequence of reduced 5'-deiodinase activity. It seems possible that the mechanisms affecting the metabolism of the iodothyronines in AMI and during propranolol medication involved the same enzyme system. However, the late appearance of the alterations in serum iodothyronines levels during propranolol medication might indicate different modes of action.

Occurrence of Myeloma-Like γ-Globulin in C.S.F of A Four-Month Old Infant with Hydrocephalus

PEDIATRICS ◽  
1964 ◽  
Vol 33 (3) ◽  
pp. 435-440
Author(s):  
G. M. HOCHWALD ◽  
G. J. THORBECKE
Keyword(s):  
Paper Electrophoresis ◽  
Reticulum Cell ◽  
Reticulum Cell Sarcoma ◽  
Myeloma Protein ◽  
Characteristic Appearance ◽  
Myeloma Proteins ◽  
Group I ◽  
Immune Globulins ◽  
Γ Globulins ◽  
Narrow Bands

Myeloma-like immune globulins present themselves as narrow bands upon paper electrophoresis, and usually show a characteristic appearance in immunoelectrophoresis. Two antigenically different groups of myeloma proteins have been described: groups I and II. Recently, 60% of normal γ-globulin, throughout the mobility range of γ-globulin, has been shown to possess the antigen characteristic for group I, and 30% that for group II myeloma. Occurrence of myeloma-like proteins in the serum is not restricted to multiple myeloma. They may also be seen with other tumors, such as reticulum cell sarcoma, and various carcinomas. In addition, Sonnet and Milhaux have reported on the frequent occurrence of myeloma-like ("monoclonal") γ-globulins in the serum of adult Bantus with different diseases. When large amounts of a myeloma protein are present in the serum, it may be found in a much lower concentration in the spinal fluid.

scholarly journals IMMUNOLOGICAL STUDIES OF HUMAN γ-GLOBULIN

1960 ◽  
Vol 112 (1) ◽  
pp. 203-223 ◽  
Author(s):  
G. M. Edelman ◽  
J. F. Heremans ◽  
M.-Th. Heremans ◽  
H. G. Kunkel
Keyword(s):  
Deae Cellulose ◽  
Antigenic Determinants ◽  
Agar Diffusion ◽  
Myeloma Proteins ◽  
Zone Electrophoresis ◽  
Γ Globulins

Two major antigenic fragments were obtained from various purified γ-globulin preparations after papain treatment. One, the F component, had a mobility faster than the original γ-globulin and the second, the S component, had a slower mobility. Similar F and S components were also obtained with certain homogeneous myeloma proteins which were closely related to γ-globulin immunologically. Additional minor antigenic components were detected with certain antisera. The technique of immunoelectrophoresis was particularly useful for bringing out the different antigenic constituents obtained after papain treatment. The F and S components as well as a midfraction were isolated by chromatography on DEAE-cellulose. These were immunologically homogeneous and could be utilized to absorb F and S antibodies from various antisera. The relative amount of F and S antibodies varied in different antisera from individual rabbits immunized with whole γ-globulin. Whole γ-globulin was separated by zone electrophoresis into a fast migrating and a more slowly migrating fraction. Each of these gave rise to F and S components after splitting with papain. The F components of the two γ-globulins were similar in mobility, while the S components showed marked mobility differences although antigenically they were very similar. The mobility differences of the parent γ-globulin appeared to be primarily related to the differences in the S component. Certain antisera against pathological γ-globulins were found to give double lines with a wide variety of γ-globulin preparations in agar diffusion. These were shown to be related to the F and S antigenic determinants of γ-glubulin. This relationship was evident by a number of procedures utilizing both Ouchterlony plate techniques and immunoelectrophoresis. The question of whether these findings indicate heterogeneity of γ-globulin in relation to the F and S antigenic components, or whether different antigenic groups on one molecule can give rise to separate lines in certain instances, is discussed.

scholarly journals Association Between Serum Osmolality and Acute Kidney Injury in Critically Ill Patients: A Retrospective Cohort Study

2021 ◽  
Vol 8 ◽  
Author(s):  
Jie Yang ◽  
Yisong Cheng ◽  
Ruoran Wang ◽  
Bo Wang
Keyword(s):  
Acute Kidney Injury ◽  
Logistic Regression ◽  
Critically Ill ◽  
Critically Ill Patients ◽  
Retrospective Cohort ◽  
Kidney Injury ◽  
High Serum ◽  
Serum Osmolality ◽  
Multivariate Logistic Regression ◽  
Low Serum

Purposes: Acute kidney injury (AKI) is a common complication in critically ill patients and is usually associated with poor outcomes. Serum osmolality has been validated in predicting critically ill patient mortality. However, data about the association between serum osmolality and AKI is still lacking in ICU. Therefore, the purpose of the present study was to investigate the association between early serum osmolality and the development of AKI in critically ill patients.Methods: The present study was a retrospective cohort analysis based on the medical information mart for intensive care III (MIMIC-III) database. 20,160 patients were involved in this study and divided into six subgroups according to causes for ICU admission. The primary outcome was the incidence of AKI after ICU admission. The association between early serum osmolality and AKI was explored using univariate and multivariate logistic regression analyses.Results: The normal range of serum osmolality was 285–300 mmol/L. High serum osmolality was defined as serum osmolality &gt;300 mmol/L and low serum osmolality was defined as serum osmolality &lt;285 mmol/L. Multivariate logistic regression indicated that high serum osmolality was independently associated with increased development of AKI with OR = 1.198 (95% CL = 1.199–1.479, P &lt; 0.001) and low serum osmolality was also independently associated with increased development of AKI with OR = 1.332 (95% CL = 1.199–1.479, P &lt; 0.001), compared with normal serum osmolality, respectively.Conclusions: In critically ill patients, early high serum osmolality and low serum osmolality were both independently associated with an increased risk of development of AKI.

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