scholarly journals ELECTRON MICROSCOPY OF THE TISSUE MAST CELL

1957 ◽  
Vol 3 (1) ◽  
pp. 9-14 ◽  
Author(s):  
Douglas E. Smith ◽  
Yevette S. Lewis
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Mast Cells ◽  
Internal Structure ◽  
Toluidine Blue ◽  
Structure And Function ◽  
Protamine Sulfate ◽  
Tissue Mast Cell ◽  
And Function ◽  
Double Nature

Electron microscopy was carried out on sections through tissue mast cells from the peritoneal fluid of rats and hamsters, either untreated, x-irradiated, or injected with toluidine blue, protamine sulfate, or stilbamidine. Mast cells from untreated animals have large nuclei and are filled with densely packed, cytoplasmic granules. The latter possess a distinct boundary and an internal structure which is reticular or vacuolar in nature. Between the granules are found elongate mitochondria and endoplasmic reticulum. Mitochondria often appear also in groups in granule-free areas adjacent to the nucleus. Nuclear and cell membranes of an apparent double nature are found. After treatment with toluidine blue, protamine sulfate, and stilbamidine the granules are surrounded by clear areas and are widely separated from one another; the endoplasmic reticulum is more conspicuous. The internal structure of the granule is unchanged. In the mast cells from x-irradiated animals there is an apparent coalescence of granules which is attented by a loss of intragranular structure. The findings are discussed in relation to other work on the structure and function of mast cells.

Use of human autoantibodies and immunoelectron microscopy to study structure and function of the nucleolus and nuclear bodies

1992 ◽  
Vol 50 (1) ◽  
pp. 506-507
Author(s):  
Robert L. Ochs
Keyword(s):  
Electron Microscopy ◽  
Structure And Function ◽  
Nuclear Bodies ◽  
Nuclear Interior ◽  
Coiled Bodies ◽  
Interchromatin Granules ◽  
And Function ◽  
Conventional Electron Microscopy ◽  
Perichromatin Granules ◽  
Perichromatin Fibrils

By conventional electron microscopy, the formed elements of the nuclear interior include the nucleolus, chromatin, interchromatin granules, perichromatin granules, perichromatin fibrils, and various types of nuclear bodies (Figs. 1a-c). Of these structures, all have been reasonably well characterized structurally and functionally except for nuclear bodies. The most common types of nuclear bodies are simple nuclear bodies and coiled bodies (Figs. 1a,c). Since nuclear bodies are small in size (0.2-1.0 μm in diameter) and infrequent in number, they are often overlooked or simply not observed in any random thin section. The rat liver hepatocyte in Fig. 1b is a case in point. Historically, nuclear bodies are more prominent in hyperactive cells, they often occur in proximity to nucleoli (Fig. 1c), and sometimes they are observed to “bud off” from the nucleolar surface.

Crystal Structures of Fragments D and Double-D from Fibrinogen and Fibrin

1999 ◽  
Vol 82 (08) ◽  
pp. 271-276 ◽  
Author(s):  
Glen Spraggon ◽  
Stephen Everse ◽  
Russell Doolittle
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Crystal Structures ◽  
Structure And Function ◽  
X Ray ◽  
Long Period ◽  
And Function

IntroductionAfter a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved. * Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide

Morphological and Biochemical Features Affecting the Antithrombotic Properties of the Aorta in Adult Rabbits and Rabbit Pups

1998 ◽  
Vol 79 (05) ◽  
pp. 1034-1040 ◽  
Author(s):  
E. Nitschmann ◽  
L. Berry ◽  
S. Bridge ◽  
M. W. C. Hatton ◽  
M. Richardson ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Gel Electrophoresis ◽  
Arterial Wall ◽  
Structure And Function ◽  
Wall Structure ◽  
Matrix Structure ◽  
Antithrombotic Activity ◽  
Antithrombin Activity ◽  
And Function ◽  
Biochemical Features

SummaryWe hypothesised that there are important physiologic differences in arterial wall structure and function with respect to antithrombotic activity in the very young (pre-puberty) compared to adults. Electron microscopy, gel electrophoresis, and activity assays were used to examine differences in aorta structure and function comparing prepubertal rabbits (pups) to adult rabbits. Differences in endothelial function, extracellular matrix structure, proteoglycan (PG) distribution and glycosaminoglycan (GAG) content and function were shown. In both intima and media, total PG, chondroitin sulfate (CS) PG and heparan sulfate (HS) PG content were significantly increased in pups compared to adult rabbits. These findings corresponded to increased concentrations by mass analyses of CS GAG and DS GAG in aortas from pups. There was also a significant increase in antithrombin activity in pups due to HS GAG. In conclusion, differences in both structure and antithrombin activity of aortas from pups compared to adult rabbits suggest that young arteries may have greater antithrombotic potential that is, at least in part, related to increased HS GAG.

Oxidative protein folding in the mammalian endoplasmic reticulum

2004 ◽  
Vol 32 (5) ◽  
pp. 655-658 ◽  
Author(s):  
C.E. Jessop ◽  
S. Chakravarthi ◽  
R.H. Watkins ◽  
N.J. Bulleid
Keyword(s):  
Endoplasmic Reticulum ◽  
Mammalian Cells ◽  
Redox State ◽  
Structure And Function ◽  
Reduced Form ◽  
Secretory Proteins ◽  
Oxidative Protein Folding ◽  
Disulphide Bonds ◽  
And Function ◽  
Substrate Proteins

Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. This review will discuss how these enzymes are maintained in either an oxidized redox state that allows them to form disulphide bonds in substrate proteins or a reduced form that allows them to perform isomerization and reduction reactions, how these opposing pathways may co-exist within the same compartment and why so many oxidoreductases exist when PDI alone can perform all three of these functions.

Evaluation of neutrophil structure and function by electron microscopy: cytochemical studies

1999 ◽  
Vol 232 (1-2) ◽  
pp. 169-178 ◽  
Author(s):  
John M Robinson ◽  
Toshihiro Kobayashi ◽  
Harumichi Seguchi ◽  
Toshihiro Takizawa
Keyword(s):  
Electron Microscopy ◽  
Structure And Function ◽  
And Function

Structure and Function of the Receptor for Immunoglobulin E (IgE) on Mast Cells

1981 ◽  
Vol 9 (2) ◽  
pp. 60P-60P
Author(s):  
H. Metzger ◽  
C. Fewtrell ◽  
A. Goetze ◽  
D. Holowka ◽  
J. Kanellopoulos
Keyword(s):  
Mast Cells ◽  
Immunoglobulin E ◽  
Structure And Function ◽  
And Function
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