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1.
J Invest Dermatol ; 111(6): 996-1002, 1998 Dec.
Article in English | MEDLINE | ID: mdl-9856807

ABSTRACT

Secretory leukocyte protease inhibitor (SLPI) is a small, cationic protein that is known to be constitutively expressed by several glandular epithelia. SLPI inhibits leukocyte-derived proteinases, has anti-HIV-1, antibacterial, and anti-fungal properties, and interferes with the induction of synthesis of proinflammatory mediators in monocytes and macrophages. We now report that at both the mRNA and the protein level, SLPI shows inducible expression in a nonglandular epithelium. A weak expression of SLPI was found in the stratum granulosum of adult normal human epidermis; however, in lesional psoriatic epidermis and in migrating keratinocytes of healing wounds, a strong cytoplasmic staining was seen in the suprabasal keratinocytes. Remarkably, in the dermis adjacent to SLPI-expressing keratinocytes, SLPI was found extracellularly associated with elastin fibers, whereas the dermis in normal skin was negative. In cell culture, SLPI was hardly expressed in monolayers of proliferating keratinocytes. Differentiating cultures with a phenotype of normal skin expressed low levels of SLPI, whereas cultures with a regenerative/psoriatic phenotype expressed high levels. Functional studies with recombinant SLPI indicated that its antibacterial spectrum and potency are distinct from other anti-microbial peptides such as lysozyme and defensins. In view of the multiple functions of SLPI and the inducibility, we propose that it acts as an important first line defence mechanism in cutaneous injury.


Subject(s)
Epidermal Cells , Keratinocytes/metabolism , Protein Biosynthesis , Serine Proteinase Inhibitors/biosynthesis , Adult , Antibodies, Monoclonal/analysis , Cell Differentiation , Cell Division , Cells, Cultured , Humans , Proteinase Inhibitory Proteins, Secretory , Proteins/immunology , Psoriasis/physiopathology , Secretory Leukocyte Peptidase Inhibitor , Skin/immunology , Skin/injuries , Up-Regulation , Wound Healing/physiology
2.
Digitale Bilddiagn ; 5(4): 187-9, 1985 Dec.
Article in German | MEDLINE | ID: mdl-4075704

ABSTRACT

Computed tomography can demonstrate most glenohumeral structures accurately. If the articular cavitz is filled with air, CT ist the method of choice in preoperative diagnosis to determine the capsular extension and to assess the destruction of the glenoid bone rim and glenoid labrum.


Subject(s)
Shoulder Dislocation/diagnostic imaging , Shoulder Injuries , Tomography, X-Ray Computed , Arthrography , Cartilage, Articular/injuries , Fractures, Bone/diagnostic imaging , Humans , Pneumoradiography , Recurrence , Shoulder Dislocation/surgery
3.
Rofo ; 136(4): 440-3, 1982 Apr.
Article in German | MEDLINE | ID: mdl-6212483

ABSTRACT

CT provides a clear, unobstructed and reproducible view of the shoulder joint. This permits, unlike conventional methods, for the first time a complete view of the anatomy and of the factors which predispose to a recurrent subluxation of the shoulder. In addition it is possible to see bone lesions resulting from the subluxation.


Subject(s)
Shoulder Dislocation/diagnostic imaging , Tomography, X-Ray Computed/methods , Chronic Disease , Diagnosis, Differential , Humans
4.
Z Orthop Ihre Grenzgeb ; 117(3): 355-64, 1979 Jun.
Article in German | MEDLINE | ID: mdl-463226

ABSTRACT

Using a Picker Echoview System 80 L, an Ultrasound Compound scanning instrument from Picker Roentgen GmbH, Espelkamp, Germany, some investigations on bones and joints were performed. In comparison with needle probe diameter measuring of muscles it could be shown that ultrasound tomography gives identical results without pain. Figuring of hip and knee joints outlines was possible. Alterations of muscles and tendon tissue were to be seen. Special meridians on the hip joint, along with the ultrasound probe had to be moved, were defined by anatomical marking points. So it became possible to reproduce some angles which usually had to be measured at X-ray pictures.


Subject(s)
Ultrasonography , Achilles Tendon , Adult , Aneurysm/complications , Bone Cysts/diagnosis , Child , Female , Femoral Neoplasms/diagnosis , Femur , Giant Cell Tumors/diagnosis , Hip Joint , Humans , Male , Middle Aged , Tomography
5.
Biochim Biophys Acta ; 434(1): 32-43, 1976 May 20.
Article in English | MEDLINE | ID: mdl-938670

ABSTRACT

Senile nuclear cataractous lenses were divided into three groups of increasing nuclear color. These groups were considered as successive stages in the development of senile nuclear cataract. The cortex and the nucleus of normal and cataractous lenses were separated into water-soluble, urea-soluble and urea-insoluble fractions. Fractionation on a Sephadex G-200 column of the water-soluble components revealed five protein fractions for both cortex and nucleus. Only minor quantitative differences in polypeptide chain composition were found by isoelectric focusing between corresponding protein fractions isolated from normal and cataractous lenses. The weight percentages of the water-soluble, urea-soluble, and urea-insoluble fractions of cortex and nucleus from the normal and cataractous lenses were determined. A decrease of the amounts of the water-soluble and urea-soluble fractions and a concomitant increase of the urea-insoluble fraction were observed in the nucleus as a function of cataract development. Lens wet weight and protein content did not change significantly. The carbohydrate content of the urea-soluble fractions increased, that of the urea-insoluble fraction decreased. A striking decrease of the phospholipid content in the urea-insoluble fraction was found.


Subject(s)
Cataract/metabolism , Crystallins/metabolism , Lens, Crystalline/metabolism , Aged , Crystallins/isolation & purification , Humans , Isoelectric Focusing , Middle Aged , Molecular Weight , Phospholipids/analysis , Urea
6.
Eur J Biochem ; 50(3): 503-9, 1975 Jan 15.
Article in English | MEDLINE | ID: mdl-1112267

ABSTRACT

Electron micrographs of high (40-S) and very-high-molecular-weight (240S) alpha-crystallin preparations show large aggregates with a random arrangement of individual low-molecular-weight alpha-crystallin molecules. The electron microscopic data are completed with viscosimetric and light-scattering experiments. All data obtained with higher-molecular-weight alpha-crystallins point to aggregates with non-spherical structures.


Subject(s)
Crystallins , Animals , Cattle , Chromatography , Isoelectric Focusing , Macromolecular Substances , Microscopy, Electron , Molecular Weight , Protein Conformation , Scattering, Radiation , Ultracentrifugation , Viscosity
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