Histopathologic study of accessory orbital band in type I Duane syndrome

Background/Aims: Accessory orbital bands are relatively rare and very few reports detail histopathology. Cases in the literature describe the composition of the bands as muscular and/or fibrous. The composition of the supernumerary band lying deep in the medial rectus muscle in a patient with type I Duane syndrome was investigated. Methods: Histochemical stains were used in conjunction with polarized light for differentiating compressed collagen from muscle. Immunohistochemistry was used for verification of the presence of muscle. Results: Compressed collagen appeared red using Masson trichrome staining. Collagen was positively identified by illumination with polarized light on several stains including the underutilized Sirius red dye. Conclusions: The findings of dense collagen fibers in the fibrotic band with focal striated muscle correlated with the restrictive strabismus. In concert with other cases in the literature, it is proposed that the fibrous bands are generally associated with restrictive strabismus. Bands that are muscular may or may not be associated with strabismus. Special techniques are needed to positively identify compressed collagen.

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Heat-Etching with a Bullivant Type II Simple Freeze-Cleave Device

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100067522 ◽

1970 ◽

Vol 28 ◽

pp. 106-107 ◽

Cited By ~ 1

Author(s):

Ronald S. Weinstein ◽

N. Scott McNutt

Keyword(s):

New Zealand ◽

General Hospital ◽

Massachusetts General Hospital ◽

Type I ◽

Type Ii ◽

Collaborative Effort ◽

Temperature And Pressure ◽

The University

The Type I simple cold block device was described by Bullivant and Ames in 1966 and represented the product of the first successful effort to simplify the equipment required to do sophisticated freeze-cleave techniques. Bullivant, Weinstein and Someda described the Type II device which is a modification of the Type I device and was developed as a collaborative effort at the Massachusetts General Hospital and the University of Auckland, New Zealand. The modifications reduced specimen contamination and provided controlled specimen warming for heat-etching of fracture faces. We have now tested the Mass. General Hospital version of the Type II device (called the “Type II-MGH device”) on a wide variety of biological specimens and have established temperature and pressure curves for routine heat-etching with the device.

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Two Distinct Types of Microfilaments in the Cytoplasm of Human Adenohypophysial Cells

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100073787 ◽

1973 ◽

Vol 31 ◽

pp. 668-669

Author(s):

E. Horvath ◽

K. Kovacs ◽

I. E. Stratmann ◽

C. Ezrin

Keyword(s):

Pituitary Tumors ◽

Average Diameter ◽

Anterior Lobe ◽

Uranyl Acetate ◽

Type I ◽

Breast Cancer Patients ◽

Human Pituitary ◽

Severe Diabetes ◽

Pituitary Glands ◽

Membrane Bound

Surgically removed human pituitary glands as well as pituitary tumors fixed in glutaraldehyde, postfixed in osmium tetroxide, embedded in epon resin, stained with uranyl acetate and lead citrate have been investigated by electron microscopy in order to correlate ultrastructure with functional activity. In the course of this study two distinct types of microfilaments have been identified in the cytoplasm of adenohypophysiocytes.Type I microfilaments (Fig. 1) were found in the cytoplasm of anterior lobe cells of five female subjects with disseminated mammary cancer and two patients with severe diabetes mellitus. The breast cancer patients were treated pre-operatively for various periods of time with different doses of oxysteroids. The microfilaments had an average diameter of JO A, formed parallel bundles, were scattered irregularly in the cytoplasm and were frequently located in the perikaryon. They were not membrane-bound and failed to show any periodicity.

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The diagnosis of metabolic storage disease in skin biopsies (a light-, electronmicroscopic, and analytical study)

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100084119 ◽

1978 ◽

Vol 36 (2) ◽

pp. 648-649

Author(s):

W. Jurecka ◽

W. Gebhart ◽

H. Lassmann

Keyword(s):

Storage Disease ◽

Hunter Syndrome ◽

Histochemical Demonstration ◽

Sweat Glands ◽

Type I ◽

Storage Material ◽

Scheie Syndrome ◽

Storage Products ◽

Skin Biopsies ◽

Type V

Diagnosis of metabolic storage disease can be established by the determination of enzymes or storage material in blood, urine, or several tissues or by clinical parameters. Identification of the accumulated storage products is possible by biochemical analysis of isolated material, by histochemical demonstration in sections, or by ultrastructural demonstration of typical inclusion bodies. In order to determine the significance of such inclusions in human skin biopsies several types of metabolic storage disease were investigated. The following results were obtained.In MPS type I (Pfaundler-Hurler-Syndrome), type II (Hunter-Syndrome), and type V (Ullrich-Scheie-Syndrome) mainly “empty” vacuoles were found in skin fibroblasts, in Schwann cells, keratinocytes and macrophages (Dorfmann and Matalon 1972). In addition, prominent vacuolisation was found in eccrine sweat glands. The storage material could be preserved in part by fixation with cetylpyridiniumchloride and was also present within fibroblasts grown in tissue culture.

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Methionine-Specific Staining of Collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010005408x ◽

1982 ◽

Vol 40 ◽

pp. 294-295

Author(s):

E.M. Kuhn ◽

K.D. Marenus ◽

M. Beer

Keyword(s):

Amino Acids ◽

Collagen Fibers ◽

Type Iii Collagen ◽

Type I ◽

Electron Microscopic ◽

Good Correspondence ◽

Specific Staining ◽

Type Iii ◽

Different Types ◽

Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

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