scholarly journals Ultrastructural localization of gamma-chain and immunoglobulin G in human lymphocytes using enzyme-labeled Fab fragment.

1975 ◽  
Vol 23 (8) ◽  
pp. 624-631 ◽  
Author(s):  
C T Lin ◽  
J P Chang ◽  
J P Chen
Keyword(s):  
Endoplasmic Reticulum ◽  
Immunoglobulin G ◽  
Human Lymphocytes ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Gamma Chain ◽  
Fab Fragment ◽  
Peripheral Lymphocytes ◽  
Human Peripheral Lymphocytes ◽  
Normal Human

By the use of rabbit antibodies against the heavy chain of human immunoglobulin G (IgG), the gamma-chain and IgG molecules were successfully localized at the ultrastructural level in human peripheral lymphocytes. The rabbit Fab fragment was coupled to horseradish peroxidase by means of glutaraldehyde and the resulting conjugate could penetrate the intact plasma membrane. Discernible reaction product was observed in cisternae of the nuclear envelope, rough endoplasmic reticulum and Golgi apparatus as well as on the surface of the lymphocytes. In normal human individuals under no specific antigenic stimulation, only a few peripheral lymphocytes showed a rare positive intractoplasmic reaction. Reaction product may represent either the whole IgG molecule, the half molecule consisting of one heavy and one light chain or nascent gamma-chain.

Surface morphology and agglutination of lectin-treated human lymphocytes and lymphoblasts

1976 ◽  
Vol 21 (3) ◽  
pp. 563-578
Author(s):  
J.H. Temmink ◽  
J.G. Collard ◽  
J. Roosien ◽  
J.F. Van den Bosch
Keyword(s):  
Cell Surface ◽  
Surface Morphology ◽  
Human Lymphocytes ◽  
Cell Type ◽  
A Cell ◽  
Human Peripheral Lymphocytes ◽  
Normal Human ◽  
Altered Cell ◽  
Induced Changes ◽  
Cell Surface Morphology

Two human lymphoblasts (Raji and EB3) and normal human peripheral lymphocytes were exposed to different concentrations of Concanavalin A and wheat germ agglutinin. The lectin-induced agglutination was determined and correlated with lectin-induced changes in the surface morphology of these cells as studied in a scanning electron microscope. Whenever the lectin induced high agglutinability in a cell type, it also invariably had a smoothing effect on the cell surface. In contrast, when cells did not agglutinate well with a certain lectin, their cell surface remained essentially rough (villous) after addition of the lectin. The correlation found between increased agglutinability and altered cell surface morphology upon treatment with certain lectins suggests that both phenomena result from one and the same process. Additional evidence for this postulate is presented.

scholarly journals Heterogeneity of uroplakin localization in human normal urothelium, papilloma and papillary carcinoma

2013 ◽  
Vol 47 (4) ◽  
pp. 338-345 ◽  
Author(s):  
Dasa Zupancic ◽  
Rok Romih
Keyword(s):  
Papillary Carcinoma ◽  
Recurrence Rate ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Apical Plasma Membrane ◽  
High Recurrence Rate ◽  
Tumour Resection ◽  
Urothelial Cells ◽  
Normal Human ◽  
Normal Urothelium

Abstract Background. Uroplakins are differentiation-related membrane proteins of urothelium. We compared uroplakin expression and ultrastructural localization in human normal urothelium, papilloma and papillary carcinoma. Because of high recurrence rate of these tumours, treated by transurethral resection, we investigated urothelial tumour, resection border and uninvolved urothelium. Patients and methods. Urinary bladder samples were obtained from tumour free control subjects and patients with papilloma and papillary carcinoma. Immunohistochemical and immunoelectron labelling of uroplakins were performed. Results. In normal human urothelium with continuous uroplakin-positive superficial cell layer uroplakins were localized to flattened mature fusiform vesicles and apical plasma membrane of umbrella cells. Diverse uroplakin expression was found in papilloma and papillary carcinoma. Three aberrant differentiation stages of urothelial cells, not found in normal urothelium, were recognized in tumours. Diverse uroplakin expression and aberrant differentiation were occasionally found in resection border and in uninvolved urothelium. Conclusions. We demonstrated here that uroplakin expression and localization in urothelial tumours is altered when compared to normal urothelium. In patients with papilloma and papillary carcinoma immunolabelling of uroplakins at ultrastructural level shows aberrant urothelial differentiation. It is possible that aberrant differentiation stages of urothelial cells in resection border and in uninvolved urothelium contribute to high recurrence rate.

THE IN VITRO RESPONSE OF HUMAN LYMPHOCYTES CHALLENGED BY RAGWEED ANTIGEN

PEDIATRICS ◽  
1968 ◽  
Vol 42 (6) ◽  
pp. 976-979
Author(s):  
Stuart H. Young ◽  
Raymond E. P. Zimmerman ◽  
Elizabeth M. Smithwick
Keyword(s):  
Human Lymphocytes ◽  
Peripheral Lymphocytes ◽  
Human Peripheral Lymphocytes ◽  
In Vitro Response ◽  
Antigen Antibody ◽  
Sensitive Individual ◽  
Circulating Antibody

More than 50% of human peripheral lymphocytes in culture will transform to a blastlike cell when incubated with phytohemagglutinin. To a lesser degree, the lymphocytes of a sensitive individual incubated with the appropriate antigen will also undergo blastogenesis. This phenomenon occurs not only in antigen-antibody systems associated with circulating antibody (e.g., tetanus) but also in those systems associated with delayed sensitivity (e.g., tuberculin). This study demonstrates that lymphocytes from a sensitive individual will also undergo blastogenesis when incubated with the appropriate antigen from the reagin group, in this case, ragweed antigen.

The expression of insulin-like growth factors and their binding proteins in normal human lymphocytes

1993 ◽  
Vol 128 (2) ◽  
pp. 168-172 ◽  
Author(s):  
Tuulikki Nyman ◽  
Fredrika Pekonen
Keyword(s):  
Growth Factors ◽  
Binding Proteins ◽  
Human Lymphocytes ◽  
Polymerase Chain Reaction Method ◽  
Igf I ◽  
Pcr Products ◽  
Human Peripheral Lymphocytes ◽  
Normal Human ◽  
Polymerase Chain ◽  
Insulin Like Growth Factors

The expression of insulin-like growth factors and their binding proteins in normal human peripheral lymphocytes was studied using the reverse transcriptase polymerase chain reaction method and Western ligand blotting. A quantitation of RT-PCR products was used to study the differences between normal and PHA stimulated lymphocytes. Normal freshly collected lymphocytes expressed mRNAs for both IGF-I receptor and IGF-II receptor but no expression of the corresponding growth factors was detectable. After stimulation with phytohemagglutinin the lymphocytes, however, expressed both IGF-I and IGF-II. Of the five IGFBPs examined, unstimulated lymphocytes expressed only IGFBP-2 and -3. Stimulated lymphocytes expressed IGFBP-4 and -5, in addition to IGFBP-2 and -3, whereas IGFBP-1 mRNA remained undetectable. The ligand blotting of lymphocyte conditioned media revealed production of 34K. 43K and 49K IGFBPs. The addition of estrogen, progesterone, IGF-I or growth hormone did not affect secretion of IGFBPs by lymphocytes.

Ultrastructural localization of cellulase in Trichoderma reesei using immunocytochemistry and enzyme cytochemistry.

1983 ◽  
Vol 31 (12) ◽  
pp. 1363-1366 ◽  
Author(s):  
C M Chapman ◽  
J R Loewenberg ◽  
M J Schaller ◽  
J E Piechura
Keyword(s):  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Trichoderma Reesei ◽  
Growth Medium ◽  
Culture Medium ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Enzyme Cytochemistry ◽  
Specific Staining ◽  
Cellulase Complex

Two components of the cellulase complex (E.C. 3.2.1.4) of the fungus Trichoderma reesei were localized at the ultrastructural level. Immunocytochemistry and enzyme cytochemistry demonstrated that cellobiohydrolase and beta-1,4 glucanase were localized within cisternae of endoplasmic reticulum and within membrane complexes of cellulose-grown hyphae. Both enzymes were also present in the culture medium. Glucose-grown control hyphae lacked enzyme-specific staining, and no enzyme activity was detected in the growth medium.

scholarly journals Intracellular localization of fibronectin by immunoelectron microscopy.

1980 ◽  
Vol 28 (9) ◽  
pp. 953-960 ◽  
Author(s):  
S S Yamada ◽  
K M Yamada ◽  
M C Willingham
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Intracellular Localization ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Protein Synthesis Inhibitors ◽  
Cultured Fibroblasts ◽  
Extracellular Glycoprotein

We have localized fibronectin, a major extracellular glycoprotein of cultured fibroblasts, in chick embryo fibroblasts at the ultrastructural level using affinity-purified antibodies to fibronectin. The use of a ferritin bridge procedure permitted quantitation of localization in various organelles. These results provide the first intracellular ultrastructural localization of fibronectin. Extracellular labeling was confined to aggregates and fibrils, with little or no labeling of the plasma membrane. The principal sites of intracellular localization were the rough endoplasmic reticulum and the Golgi apparatus. Treatment of cells with the protein synthesis inhibitors cycloheximide and pactamycin reduced fibronectin localization in the endoplasmic reticulum to 50% of normal levels. Removal of cycloheximide permitted recovery of labeling to 85% of control levels in the endoplasmic reticulum. Similar, but much reduced, changes also occurred in the Golgi apparatus.

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