scholarly journals Ultrastructural and Immunofluorescence Studies of the Cells Associated With µ-Chain Disease

Blood ◽  
1971 ◽  
Vol 37 (3) ◽  
pp. 257-271 ◽  
Author(s):  
DOROTHEA ZUCKER-FRANKLIN ◽  
EDWARD C. FRANKLIN
Keyword(s):  
Electron Microscopy ◽  
Secretory Pathway ◽  
Plasma Cells ◽  
Bone Marrow Cells ◽  
Light Chains ◽  
Antigenic Determinants ◽  
Protein Fragments ◽  
Fluorescence And Electron Microscopy ◽  
Golgi Zone ◽  
Heavy Chain Disease

Abstract Fluorescence and electron microscopy studies were carried out on the blood and bone marrow cells of the first patient observed to have µ-chain disease. Since previously reported cases of γ and α heavy-chain disease did not elaborate any light chains, it was of interest to determine whether both the µ-chain fragments and the κ chains found in the serum of this patient originated in the same cell or whether mutations had affected two different clones. The use of rhodamine-conjugated and fluorescein-conjugated antisera to heavy and light chains respectively established that both antigenic determinants were present in the same cell. On electron microscopy, the plasma cells showed large vacuoles which appeared to form in the vicinity of the Golgi zone and frequently extended to the surface of the cell. It is postulated that the structural defect in the µ chain interferes with proper assembly of the gamma-globulin molecule. This in turn may preclude transport via the normal secretory pathway. The accumulated protein fragments may be released by a process of limited cytolysis.

scholarly journals Heavy Chain Disease of the µ (γM) Type: Report of the First Case

Blood ◽  
1970 ◽  
Vol 36 (2) ◽  
pp. 137-144 ◽  
Author(s):  
FRANK A. FORTE ◽  
FRANCES PRELLI ◽  
WILLIAM J. YOUNT ◽  
L. MARTIN JERRY ◽  
SHAUL KOCHWA ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
Heavy Chain ◽  
Lymphocytic Leukemia ◽  
Light Chains ◽  
Antigenic Determinants ◽  
Bence Jones Protein ◽  
First Case ◽  
Heavy Chain Disease ◽  
Serum And Urine

Abstract The serum of a patient with chronic lymphocytic leukemia, and amyloidosis, was found to contain an unusual protein with µ chain antigenic determinants. It was devoid of light chains and was present in the form of multiple disulfide linked polymers. The patient also had a kappa Bence Jones protein in the serum and urine. The possibility is raised that the heavy chain lacks a portion of the chain necessary for coupling with light chains.

Structure of Myosin Subfragment-1 from Electron Microscopy and Crystallography

1988 ◽  
Vol 46 ◽  
pp. 156-157
Author(s):  
Donald A. Winkelmann
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Actin Filaments ◽  
Light Chains ◽  
Myosin Filament ◽  
Primary Role ◽  
Heavy Chains ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Globular Head

The primary role of the interaction of actin and myosin is the generation of force and motion as a direct consequence of the cyclic interaction of myosin crossbridges with actin filaments. Myosin is composed of six polypeptides: two heavy chains of molecular weight 220,000 daltons and two pairs of light chains of molecular weight 17,000-23,000. The C-terminal portions of the myosin heavy chains associate to form an α-helical coiled-coil rod which is responsible for myosin filament formation. The N-terminal portion of each heavy chain associates with two different light chains to form a globular head that binds actin and hydrolyses ATP. Myosin can be fragmented by limited proteolysis into several structural and functional domains. It has recently been demonstrated using an in vitro movement assay that the globular head domain, subfragment-1, is sufficient to cause sliding movement of actin filaments.The discovery of conditions for crystallization of the myosin subfragment-1 (S1) has led to a systematic analysis of S1 structure by x-ray crystallography and electron microscopy. Image analysis of electron micrographs of thin sections of small S1 crystals has been used to determine the structure of S1 in the crystal lattice.

The Ultrastructure of Lymphocytic Hypophysitis

1981 ◽  
Vol 39 ◽  
pp. 466-467
Author(s):  
S.L. Asa ◽  
K. Kovacs ◽  
J. M. Bilbao ◽  
R. G. Josse ◽  
K. Kreines
Keyword(s):  
Electron Microscopy ◽  
Plasma Cells ◽  
Secretory Granules ◽  
Sella Turcica ◽  
Uranyl Acetate ◽  
Lymphocytic Hypophysitis ◽  
Pituitary Cells ◽  
Transmission Electron ◽  
Ultrathin Sections ◽  
Mass Lesions

Seven cases of lymphocytic hypophysitis in women have been reported previously in association with various degrees of hypopituitarism. We report two pregnant patients who presented with mass lesions of the sella turcica, clinically mimicking pituitary adenoma. However, pathologic examination revealed extensive infiltration of the anterior pituitary by lymphocytes and plasma cells with destruction of the gland. To our knowledge, the ultrastructural features of lymphocytic hypophysitis have not been studied so far.For transmission electron microscopy, tissue from surgical specimens was fixed in glutaraldehyde, postfixed in OsO4, dehydrated and embedded in epoxy-resin. Ultrathin sections were stained with uranyl acetate and lead citrate and examined with a Philips 300 electron microscope.Electron microscopy revealed adenohypophysial cells of all types exhibiting varying degrees of injury. In the areas of most dense inflammatory cell infiltration pituitary cells contained large lysosomal bodies fusing with secretory granules (Fig. 1), as well as increased numbers of swollen mitochondria, indicating oncocytic transformation (Fig. 2).

Immunoglobulins and Blood Vessels in the Tonsillar Crypt Epithelium

1973 ◽  
Vol 82 (3) ◽  
pp. 359-369 ◽  
Author(s):  
John F. Schmedtje ◽  
Ann F. Batts
Keyword(s):  
Epithelial Cells ◽  
Blood Vessels ◽  
Plasma Cells ◽  
Border Zone ◽  
Secretory Iga ◽  
Antigenic Determinants ◽  
Crypt Epithelium ◽  
Lower Border

The localization of IgA, IgG, IgM, SP and the relationships of plasma cells and lymphocytes to blood vessels in the tonsillar crypt epithelium were investigated. Immunofluorescent techniques were used that included antisera specific for the two antigenic determinants of external secretory IgA, namely, 4s SP and 7s IgA, and also antisera specific for 7s IgG and 19s IgM. The secretory piece was absent in the crypt epithelium and in most of the crypt lumen. Aggregations of plasmacyte series cells, containing either IgG, IgA, or IgM were present in the crypt epithelium. Mature plasma cells of these aggregations abutted against the walls of blood sinusoids located in the epithelium, which suggested secretion into these sinusoids. All three immunoglobulins were also identified between epithelial cells and small lymphocytes. Postcapillary venules with emigrating small lymphocytes abounded in sub-epithelial sites, and were present at the lower border zone of the epithelium. Lymphocytes in shapes of diapedesis were observed in the endothelium of epithelial blood sinusoids. These observations are in accord with the hypothesis that a “circulation” of many lymphocytes occurs in the epithelium facilitating the activation of any one genetically committed lymphocyte.

scholarly journals Gamma heavy chain disease: clinical aspects and characterization of a deleted, noncovalently linked gamma1 heavy chain dimer (BAZ)

Blood ◽  
1977 ◽  
Vol 49 (4) ◽  
pp. 495-505 ◽  
Author(s):  
GB Faguet ◽  
BP Barton ◽  
LL Smith ◽  
FA Garver
Keyword(s):  
Heavy Chain ◽  
Plasma Cells ◽  
Clinical Feature ◽  
Clinical Aspects ◽  
Submaxillary Glands ◽  
Underlying Malignancy ◽  
V Region ◽  
Allotypic Marker ◽  
Heavy Chain Disease

Abstract This report describes the clinical and immunoglobulin features of a patient with gamma heavy chain disease (HCD), who presented with a clinical picture suggestive of an underlying malignancy rather than the usual picture of lymphoma or granulomatous disease. A unique clinical feature was the nearly total replacement of the submaxillary glands by plasma cells. The patient's serum and urine contained a paraprotein, gammaHCD protein BAZ, which belongs to the gamma1 subclass and forms noncovalently linked dimers with a molecular weight of approximately 60,000 daltons. This mutant protein exhibited a deletion which encompassed most of the variable (V) region, the first constant domain (CH 1), and the hinge region. In addition, preliminary structural analyses demonstrated the replacement of alanine by glycine in position 431 of the carboxyterminal octadecapeptide. This substitution may possibly represent another allotypic marker on IgG1 proteins.

scholarly journals Truncated mu (mu') chains in murine IgM. Evidence that mu' chains lack variable regions.

1985 ◽  
Vol 162 (6) ◽  
pp. 1862-1877 ◽  
Author(s):  
R Marks ◽  
M J Bosma
Keyword(s):  
Bone Marrow ◽  
Lymph Node ◽  
Molecular Mass ◽  
Tumor Cells ◽  
Isoelectric Focusing ◽  
Bone Marrow Cells ◽  
Normal Serum ◽  
Antigenic Determinants ◽  
Variable Regions ◽  
Lymph Node Cells

Secreted IgM was shown to contain truncated mu (mu') chains with an apparent molecular mass of approximately 55 kD. The estimated percentage of IgM heavy (H) chains in the mu' form ranged from less than or equal to 1% in the case of one tumor IgM protein (104E) to greater than or equal to 30% in normal serum IgM. Serum mu' chains lacked antigenic determinants characteristic of immunoglobulin variable regions and showed a restricted isoelectric focusing pattern compared with that of conventional mu chains. Intracellular mu' chains were readily detected in bone marrow cells but not in spleen or lymph node cells; mu' chains were also detected in IgM-producing tumor cells and in a hybridoma cell line that deleted its productive mu allele. These results predict irregularities in IgM structure and recall an old controversy concerning the valence of IgM molecules.

scholarly journals Phenotypic analysis of human myeloma cell lines

Blood ◽  
1989 ◽  
Vol 73 (2) ◽  
pp. 566-572
Author(s):  
C Duperray ◽  
B Klein ◽  
BG Durie ◽  
X Zhang ◽  
M Jourdan ◽  
...  
Keyword(s):  
B Cell ◽  
Cell Lines ◽  
Plasma Cell ◽  
Plasma Cells ◽  
Myeloma Cell ◽  
Light Chains ◽  
Cell Phenotype ◽  
Phenotypic Analysis ◽  
Barr Virus ◽  
Human Myeloma Cell

Multiple myeloma (MM) is a B-cell malignancy characterized by the accumulation, primarily in bone marrow, of a clone of plasma cells. The nature of the stem cells feeding the tumoral compartment is still unknown. To investigate this special point, we have studied the phenotypes of nine well-known human myeloma cell lines (HMCLs) and compared them with those of normal lymphoblastoid cell lines (LCLs). Twenty-four clusters of differentiation involved in B lymphopoiesis were investigated using a panel of 65 monoclonal antibodies (MoAbs). For each cluster, the percentage of positive cells and the antigen density were determined, giving rise to a “quantitative phenotype”. We thus classified the HMCLs into two different groups: those with cytoplasmic mu chains (c mu+) and those without (c mu-). In the first (c mu+) group, comprising seven cell lines, the HMCLs had a phenotype of pre-B/B cells close to that of Burkitt's lymphoma cell lines. They expressed low densities of surface mu chains, without detectable cytoplasmic or surface light chains. Three of them were infected with the Epstein Barr virus (EBV). These c mu+ HMCLs bore most of the B-cell antigens except CD23. They expressed the CALLA antigen (CD10) and lacked the plasma-cell antigen PCA1. In contrast, LCLs expressed surface light chains, high densities of CD23, low densities of PCA1 antigen, and no CD10 antigen. The c mu- HMCLs had a plasma-cell phenotype, lacking most of the B-cell antigens and expressing high densities of PCA1 antigen.(ABSTRACT TRUNCATED AT 250 WORDS)

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