An electron microscopic and spectroscopic study of murine epiphyseal cartilage: Analysis of fine structure and matrix vesicles preserved by slam freezing and freeze substitution

1988 ◽  
Vol 98 (1) ◽  
pp. 32-47 ◽  
Author(s):  
A. Larry Arsenault ◽  
F. Peter Ottensmeyer ◽  
I. Brent Heath
Keyword(s):  
Fine Structure ◽  
Spectroscopic Study ◽  
Freeze Substitution ◽  
Matrix Vesicles ◽  
Epiphyseal Cartilage ◽  
Electron Microscopic

Electron microscopic studies on ultrathin frozen sections of lactating mouse mammary gland

1978 ◽  
Vol 36 (2) ◽  
pp. 46-47
Author(s):  
Jan Zarzycki ◽  
Joseph Szroeder
Keyword(s):  
Mammary Gland ◽  
Protein Denaturation ◽  
Chemical Constituents ◽  
Freeze Substitution ◽  
Electron Microscopic Examination ◽  
Mouse Mammary Gland ◽  
Electron Microscopic ◽  
Preparation Methods ◽  
Microscopic Studies ◽  
Ultrathin Frozen Sections

The mammary gland ultrastructure in various functional states is the object of our investigations. The material prepared for electron microscopic examination by the conventional chemical methods has several limitations, the most important are the protein denaturation processes and the loss of large amounts of chemical constituents from the cells. In relevance to this,one can't be sure about a degree the observed images are adequate to the realy ultrastructure of a living cell. To avoid the disadvantages of the chemical preparation methods,some autors worked out alternative physical methods based on tissue freezing / freeze-drying, freeze-substitution, freeze-eatching techniqs/; actually the technique of cryoultraraicrotomy,i,e.cutting ultrathin sections from deep frozen specimens is assented as a complete alternative method. According to the limitations of the routine plastic embbeding methods we were interested to analize the mammary gland ultrastructure during lactation by the cryoultramicrotomy method.

Fine structure of early degenerating myofibers in the tibialis anterior of young ‘MDX’ mouse

1988 ◽  
Vol 46 ◽  
pp. 322-323
Author(s):  
H.D. Geissinger ◽  
C.K. McDonald-Taylor
Keyword(s):  
Fine Structure ◽  
Muscle Regeneration ◽  
Tibialis Anterior ◽  
Genetic Defect ◽  
Mdx Mouse ◽  
Mdx Mice ◽  
Histopathological Changes ◽  
Electron Microscopic ◽  
Dystrophic Mouse ◽  
Preliminary Study

A new strain of mice, which had arisen by mutation from a dystrophic mouse colony was designated ‘mdx’, because the genetic defect, which manifests itself in brief periods of muscle destruction followed by episodes of muscle regeneration appears to be X-linked. Further studies of histopathological changes in muscle from ‘mdx’ mice at the light microscopic or electron microscopic levels have been published, but only one preliminary study has been on the tibialis anterior (TA) of ‘mdx’ mice less than four weeks old. Lesions in the ‘mdx’ mice vary between different muscles, and centronucleation of fibers in all muscles studied so far appears to be especially prominent in older mice. Lesions in young ‘mdx’ mice have not been studied extensively, and the results appear to be at variance with one another. The degenerative and regenerative aspects of the lesions in the TA of 23 to 26-day-old ‘mdx’ mice appear to vary quantitatively.

Effects of EDTA, Hyaluronidase and Collagenase on Epiphyseal Cartilage Matrix

1968 ◽  
Vol 26 ◽  
pp. 56-57
Author(s):  
H. Clarke Anderson ◽  
Priscilla R. Coulter
Keyword(s):  
Light And Electron Microscopy ◽  
Matrix Vesicles ◽  
Cartilage Matrix ◽  
Collagen Fibrils ◽  
Epiphyseal Cartilage ◽  
Dense Matrix ◽  
Type Iv ◽  
Bovine Testicular Hyaluronidase ◽  
The Matrix ◽  
Testicular Hyaluronidase

Epiphyseal cartilage matrix contains fibrils and particles of at least 5 different types: 1. Banded collagen fibrils, present throughout the matrix, but not seen in the lacunae. 2. Non-periodic fine fibrils <100Å in diameter (Fig. 1), which are most notable in the lacunae, and may represent immature collagen. 3. Electron dense matrix granules (Fig. 1) which are often attached to fine fibrils and collagen fibrils, and probably contain protein-polysaccharide although the possibility of a mineral content has not been excluded. 4. Matrix vesicles (Fig. 2) which show a selective distribution throughout the epiphysis, and may play a role in calcification. 5. Needle-like apatite crystals (Fig. 2).Blocks of formalin-fixed epiphysis from weanling mice were digested with the following agents in 0.1M phosphate buffer: a) 5% ethylenediaminetetraacetate (EDTA) at pH 8.3, b) 0.015% bovine testicular hyaluronidase (Sigma, type IV, 750 units/mg) at pH 5.5, and c) 0.1% collagenase (Worthington, chromatograhically pure, 200 units/mg) at pH 7.4. All digestions were carried out at 37°C overnight. Following digestion tissues were examined by light and electron microscopy to determine changes in the various fibrils and particles of the matrix.

The use of 1nm silver enhanced gold probes for the detection of skin antigens

1990 ◽  
Vol 48 (3) ◽  
pp. 902-903
Author(s):  
J.P Cassella ◽  
H. Shimizu ◽  
A. Ishida-Yamamoto ◽  
R.A.J. Eady
Keyword(s):  
Type Iv Collagen ◽  
Freeze Substitution ◽  
Collagen Type Iv ◽  
Electron Microscopic ◽  
Normal Human Skin ◽  
Type Iv ◽  
Type Vii Collagen ◽  
Keratin Filaments ◽  
Normal Human ◽  
Phosphate Buffered Saline

1nm colloidal gold with silver enhancement has been used in conjunction with a low-temperature post-embedding (post-E) technique for the demonstration of skin antigens at both the light microscopic (LM) and electron microscopic (EM) levels.Keratin filaments and basement membrane zone (BMZ) associated antigens in normal human skin (NHS) were immunolabelled using antibodies against keratin 14, 10, and 1, the carboxy-terminus and collagenous portion of type VII collagen, type IV collagen and bullous pemphigoid antigen (BP-Ag).Fresh samples of NHS were cryoprotected in 15% glycerol, cryofixed in propane at -190°C, subjected to freeze substitution in methanol at -80°C and embedded in Lowicryl K11M at -60°C. Polymerisation of the resin was initiated under UVR at - 60°C for 48 hours and continued at room temperature for a further 48 hours. Semith in sections were air dried onto slides coated with 3-aminopropyltriethoxysilane. The following immunolabelling protocol was adopted: Primary antibody was applied for 2 hours at 37°C or overnight at 4°C. Following washing in Dulbecco’s phosphate buffered saline (PBSA) a biotinylated secondary antibody was applied for 2 hours at 37°C. The sections were further washed in PBSA and 1nm gold avidin was applied. Sections were finally washed in PBSA and silver enhanced.

scholarly journals The Ascus Apex in Lichenized Fungi III. The Pertusaria-Type

1982 ◽  
Vol 14 (3) ◽  
pp. 205-217 ◽  
Author(s):  
Rosmarie Honegger
Keyword(s):  
Fine Structure ◽  
Side Branch ◽  
Functional Type ◽  
Electron Microscopic ◽  
Considerable Heterogeneity ◽  
Transmission Electron ◽  
Transmission Electron Microscopic ◽  
Scanning Electron Microscopic ◽  
Elongation Process ◽  
Scanning Electron

AbstractOn the basis of light microscopic (LM), scanning electron microscopic (SEM) and transmission electron microscopic (TEM) investigations the Pertusaria-type of ascus is described as a particular functional type. The functionally unitunicate Pertusaria-type is characterized by its structure, staining properties, and by its particular mode of dehiscence. Tripartite ascus walls were observed in LM and TEM. The non-amyloid ascus wall is surrounded by a thin, amyloid outer layer. Both become amorphous at maturity and partly disintegrate. An apically thickened, amyloid inner layer reaches the base of the ascus. In its fine structure this amyloid inner layer resembles the material of the amyloid dome of Lecanora-type asci. It plays an important role during dehiscence and spore discharge. An elongation process was observed prior to dehiscence, at the end of which the ascus tip is situated above the hymenial surface. Dehiscence occurs by bursting or splitting of the whole ascus tip. The Pertusaria-type might represent a side-branch of evolution from bitunicate to unitunicate forms within the Lecanorales.Pertusaria-type asci are restricted to a small number of genera within the Pertusariaceae. A considerable heterogeneity in ascus structure and staining properties was observed within the Pertusariineae sensu Henssen & Jahns (1973) and Henssen (1976).

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