scholarly journals Brief Report: Ultrastructural Localization of Myeloperoxidase in Human Neutrophil and Rabbit Heterophil and Eosinophil Leukocytes

Blood ◽  
1968 ◽  
Vol 32 (6) ◽  
pp. 935-944 ◽  
Author(s):  
W. B. DUNN ◽  
J. H. HARDIN ◽  
S. S. SPICER
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Human Neutrophil ◽  
Polymorphonuclear Leukocytes ◽  
Ultrastructural Localization ◽  
Human Monocytes ◽  
Specific Granules ◽  
Human Polymorphonuclear Leukocytes

Abstract Ultrastructural cytochemical observations revealed peroxidase reactivity in primary (azurophil) granules, but not in secondary (specific) granules, of rabbit and human polymorphonuclear leukocytes. Peroxidase reactivity was also observed in the rough endoplasmic reticulum and granules of rabbit eosinophils and in granules of human monocytes.

scholarly journals Localization of D-amino acid oxidase on the cell surface of human polymorphonuclear leukocytes

1978 ◽  
Vol 77 (1) ◽  
pp. 59-71 ◽  
Author(s):  
JM Robinson ◽  
RT Briggs ◽  
MJ Karnovsky
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cell Surface ◽  
Polymorphonuclear Leukocytes ◽  
Ultrastructural Localization ◽  
H2o2 Production ◽  
Acid Oxidase ◽  
Resting Cells ◽  
Amino Acid Oxidase ◽  
Human Polymorphonuclear Leukocytes

The ultrastructural localization of D-amino acid oxidase (DAO) was studied cytochemically by detecting sites of hydrogen peroxide production in human polymorphonuclear leukocytes (PMNs). Reaction product, which forms when cerous ions react with H2O2 to form an electron-dense precipitate, was demonstrated on the cell surface and within the phagosomes of phagocytically stimulated cells when D-amino acids were provided as substrate. Resting cells showed only slight activity. The competitive inhibitor D,L-2-hydroxybutyrate greatly reduced the D-amino acid-stimulated reaction while KCN did not. The cell surface reaction was abolished by nonpenetrating inhibitors of enzyme activity while that within the phagosome was not eliminated. Dense accumulations of reaction product were formed in cells which phagocytosed Staphylococcus aureus in the absence of exogenous substrate. No reaction product formed with Proteus vulgaris while an intermediate amount formed when Escherichia coli were phagocytosed. Variation in the amount of reaction product with the different bacteria correlated with the levels of D-amino acids in the bacterial cell walls which are available for the DAO of PMNs. An alternative approach utilizing ferricyanide as an electron acceptor was also used. This technique verified the results obtained with the cerium reaction, i.e., the DAO is located in the cell surface and is internalized during phagocytosis and is capable of H2O2 production within the phagosome. The present finding that DAO is localized on the cell surface further supports the concept that the plasma membrane is involved in peroxide formation in PMNs.

scholarly journals Modulation of Human Neutrophil Functions In Vitro by Treponema denticola Major Outer Sheath Protein

2006 ◽  
Vol 74 (3) ◽  
pp. 1954-1957 ◽  
Author(s):  
Bina Puthengady Thomas ◽  
Chun Xiang Sun ◽  
Elena Bajenova ◽  
Richard P. Ellen ◽  
Michael Glogauer
Keyword(s):  
Human Neutrophil ◽  
Polymorphonuclear Leukocytes ◽  
Calcium Transients ◽  
Treponema Denticola ◽  
Actin Assembly ◽  
Outer Sheath ◽  
Induced Apoptosis ◽  
Human Polymorphonuclear Leukocytes ◽  
Oxidative Responses

ABSTRACT In this study of human polymorphonuclear leukocytes (PMNs), pretreatment with Treponema denticola major outer sheath protein (Msp) inhibited formyl-methionyl-leucyl-phenylalanine (fMLP)-induced chemotaxis, phagocytosis of immunoglobulin G-coated microspheres, fMLP-stimulated calcium transients, and actin assembly. Msp neither altered oxidative responses to phorbol myristate or fMLP nor induced apoptosis. Msp selectively impairs chemotaxis and phagocytosis by impacting the PMN cytoskeleton.

scholarly journals Elastase Is the Only Human Neutrophil Granule Protein That Alone Is Responsible for In Vitro Killing of Borrelia burgdorferi

1998 ◽  
Vol 66 (4) ◽  
pp. 1408-1412 ◽  
Author(s):  
Rodolfo Garcia ◽  
Laura Gusmani ◽  
Rossella Murgia ◽  
Corrado Guarnaccia ◽  
Marina Cinco ◽  
...  
Keyword(s):  
Borrelia Burgdorferi ◽  
Human Neutrophil ◽  
Polymorphonuclear Leukocytes ◽  
In Vitro Assay ◽  
Chloride System ◽  
Vitro Assay ◽  
Human Polymorphonuclear Leukocytes ◽  
Primary Granule ◽  
Secondary Granule

ABSTRACT Phagocytosis of Borrelia burgdorferi by human polymorphonuclear leukocytes triggers oxygen-dependent and -independent mechanisms of potentially cidal outcome. Nevertheless, no factor or process has yet been singled out as being borreliacidal. We have studied the B. burgdorferi-killing ability of the myeloperoxidase-H2O2-chloride system and that of primary and secondary granule components in an in vitro assay. We found that neither secondary granule acid extracts nor the chlorinating system could kill these microorganisms, while primary granule extracts were effective. The Borrelia-killing factor was purified to homogeneity and demonstrated to be elastase. Its cidal activity was found to be independent of its proteolytic activity.

scholarly journals Concanavalin A induces microtubule assembly and specific granule discharge in human polymorphonuclear leukocytes.

1976 ◽  
Vol 68 (3) ◽  
pp. 781-787 ◽  
Author(s):  
S Hoffstein ◽  
R Soberman ◽  
I Goldstein ◽  
G Weissmann
Keyword(s):  
Concanavalin A ◽  
Binding Sites ◽  
Polymorphonuclear Leukocytes ◽  
Cytochalasin B ◽  
Microtubule Assembly ◽  
Human Neutrophils ◽  
Con A ◽  
Specific Granules ◽  
Specific Granule ◽  
Human Polymorphonuclear Leukocytes

Human neutrophils stimulated by concanavalin A (Con A, 100 microng/ml) contained markedly enhanced numbers of microtubules and discharged peroxidase-negative (specific) but not peroxidase-position (azurophile) granules. Release of lysozyme from specific granules was dose and time dependent, could be inhibitied by alpha-methyl-D-mannoside, and enhanced by cytochalasin B. Many microtubules were associated with internalized plasma membrane bearing Con A binding sites.

scholarly journals ULTRASTRUCTURAL LOCALIZATION OF CHOLINESTERASE ACTIVITY IN THE DEVELOPING RAT RETINA

1974 ◽  
Vol 22 (9) ◽  
pp. 868-880 ◽  
Author(s):  
ARTHUR W. SPIRA
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Cholinesterase Activity ◽  
Ganglion Cells ◽  
Plexiform Layer ◽  
Ultrastructural Localization ◽  
Acetylcholinesterase Activity ◽  
Inner Plexiform Layer ◽  
Cholinesterase Activities ◽  
Developing Rat

Retinae of rats from the 16th day of gestation to 10 weeks postnatal age were treated for the ultrastructural localization of cholinesterases according to the method of Lewis and Shute. The use of selective inhibitors served to differentiate between acetylcholinesterase and nonspecific cholinesterase activities. Nonspecific cholinesterase activity was marked in the rough endoplasmic reticulum of pigmented epithelium but only during the 1st 2 postnatal weeks. Acetylcholinesterase activity was prominent (a) in the rough endoplasmic reticulum, nuclear envelope and Golgi apparatus of ganglion cells in fetal and mature retinae; (b) transiently, between processes in the outer plexiform layer and in the perikarya of some horizontal cells; and (c) between processes in the inner plexiform layer coincident with the appearance of synapses, as well as in the mature retina. These localizations are suggestive of an association between cholinesterases and early stages of photoreceptor segment formation and consistent with a function in plexiform layer maturation and synaptic transmission in the inner plexiform layer.

Regulation of enzyme release from human polymorphonuclear leukocytes: further evidence for the independent regulation of granule subpopulations

1987 ◽  
Vol 65 (12) ◽  
pp. 1007-1015 ◽  
Author(s):  
Patricia Murphy ◽  
David A. Hart
Keyword(s):  
Polymorphonuclear Leukocytes ◽  
Second Messenger ◽  
Cytochalasin D ◽  
Enzyme Release ◽  
Specific Granules ◽  
Second Messenger Systems ◽  
Specific Granule ◽  
Human Polymorphonuclear Leukocytes

Addition of 5–20 mM LiCl to purified human polymorphonuclear leukocytes led to the release of lysozyme, the specific granule constituent, but not the release of elastase which is in azurophilic granules. In contrast, 2.5–10 μg cytochalasin D/mL induced the release of both lysozyme and elastase. Addition of lipopolysaccharide to leukocytes did not induce enzyme release but primed cells for enhanced release induced by cytochalasin D. Lipopolysaccharide also primed cells for enhanced release of lysozyme by either N-formylmethionylleucylphenylalanine (fMLP) or Li+ but did not prime cells for elastase release by these stimuli. In contrast, fMLP + cytochalasin D interacted synergistically, leading to enhanced elastase release but not lysozyme release from the cells. Additional experiments with combinations of secretogogues and lipopolysaccharide yielded results consistent with the hypothesis that specific granules and subpopulations of azurophilic granules are under separate regulation and, thus, may be influenced by separate elements of intracellular second messenger systems.

scholarly journals The ultrastructural localization of immunoglobulin in chronic lymphocytic lymphoma cells: changes in light and heavy chain distribution induced by mitogen stimulation

Blood ◽  
1983 ◽  
Vol 61 (3) ◽  
pp. 511-519 ◽  
Author(s):  
DG Newell ◽  
AH Harris ◽  
JL Smith
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Heavy Chain ◽  
Ultrastructural Localization ◽  
Lymphocytic Leukemia ◽  
Pokeweed Mitogen ◽  
Light Chains ◽  
Immunoperoxidase Technique ◽  
Mitogen Stimulation ◽  
Heavy Chains

Abstract The distribution of light and heavy immunoglobulin chains in chronic lymphocytic leukemia (CLL) cells has been investigated at the ultrastructural level using an immunoperoxidase technique. Light chains were localized in the lumens of the perinuclear space and rough endoplasmic reticulum, while staining for heavy chains was weak or negative and generally confined to the membranes of the rough endoplasmic reticulum. This pattern is consistent with immunoglobulin biosynthetic studies on CLL cells in which light chains are synthesized in excess over heavy chains and secreted as the exclusive immunoglobulin product. The pokeweed mitogen stimulation of two populations of CLL cells for 6 days resulted in a balanced synthesis and secretion of light and heavy chains that was reflected in concomitant change in light and heavy chain distribution and intensity of staining using the immunoperoxidase technique.

scholarly journals Ultrastructural localization of complex carbohydrates in odontoblasts, predentin, and dentin.

1981 ◽  
Vol 29 (6) ◽  
pp. 747-758 ◽  
Author(s):  
M Takagi ◽  
R T Parmley ◽  
F R Denys
Keyword(s):  
Extracellular Matrix ◽  
Endoplasmic Reticulum ◽  
Secretory Granule ◽  
Rough Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Ultrastructural Localization ◽  
Collagen Fibrils ◽  
Multivesicular Bodies ◽  
Essential Components ◽  
Dentin Matrix

Glycosaminoglycans (GAGs) and glycoproteins (GPs) are essential components for dentinogenesis. We have examined rat odontoblasts, predentin, and dentin decalcified with EDTA and stained with: 1) Spicer's hig-iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) method for sulfated glycoconjugates, and 2) Thiéry's periodate-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method for vicinal glycol-containing glycoconjugates. HIS-TCH-SP stained distended portions of Golgi saccules and secretory granules. The predentin contained three times the number of HID-TCH-SP stain precipitates when compared to the mineralization front of the dentin matrix. PA-TCH-SP weakly stained membranes of Golgi saccules and cisternae of rough endoplasmic reticulum (RER), whereas stronger staining was observed in secretory granules, lysosomes, and multivesicular bodies (MVBs). Collagen fibrils in predentin demonstrated moderate PA-TCH-SP staining. In contrast, strong PA-TCH-SP staining was observed on and between collagen fibrils in the mineralization front of the dentin matrix. TCH-SP controls of unosmicated specimens lacked significant staining, however, osmicated control specimens did contain some TCH-SP stain deposits in the mineralization front. These results indicate that sulfated and vicinal glycol-containing glycoconjugates are packaged in the same type of secretory granule and released into the extracellular matrix; subsequently vicinal glycol-containing glycoconjugates concentrate in the calcification front, whereas sulfated glycoconjugates accumulate in the predentin and are either removed or masked to staining in the dentin.

scholarly journals The ultrastructural localization of immunoglobulin in chronic lymphocytic lymphoma cells: changes in light and heavy chain distribution induced by mitogen stimulation

Blood ◽  
1983 ◽  
Vol 61 (3) ◽  
pp. 511-519 ◽  
Author(s):  
DG Newell ◽  
AH Harris ◽  
JL Smith
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Heavy Chain ◽  
Ultrastructural Localization ◽  
Lymphocytic Leukemia ◽  
Pokeweed Mitogen ◽  
Light Chains ◽  
Immunoperoxidase Technique ◽  
Mitogen Stimulation ◽  
Heavy Chains

The distribution of light and heavy immunoglobulin chains in chronic lymphocytic leukemia (CLL) cells has been investigated at the ultrastructural level using an immunoperoxidase technique. Light chains were localized in the lumens of the perinuclear space and rough endoplasmic reticulum, while staining for heavy chains was weak or negative and generally confined to the membranes of the rough endoplasmic reticulum. This pattern is consistent with immunoglobulin biosynthetic studies on CLL cells in which light chains are synthesized in excess over heavy chains and secreted as the exclusive immunoglobulin product. The pokeweed mitogen stimulation of two populations of CLL cells for 6 days resulted in a balanced synthesis and secretion of light and heavy chains that was reflected in concomitant change in light and heavy chain distribution and intensity of staining using the immunoperoxidase technique.

Sign in / Sign up

Export Citation Format

Share Document