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H Stöss

Publications and source records attributed to H Stöss.

At least 55 records · Page 3Linked to original sources
PubMed1992

Recurrence of a solitary bone cyst of the mandibular condyle in a bone graft. A case report.

The recurrence of a solitary bone cyst of the mandibular condyle in a costochondral bone graft is reported. A solitary bone cyst of the right condylar head and neck of a 10-year-old boy was treated by total resection and immediate reconstruction with a costochondral bone graft. Two years after the first operation, a recurrence of the solitary bone cyst within the bone graft was noted. An open treatment was performed. A review of the literature on solitary bone cysts and recurrences of solitary bone cysts shows that the case reported is unique. Possible reasons for the recurrence are discussed.

Bone Transplantation↗
PubMed1992

[Pleomorphic adenoma of the epiglottis. Case report and review of the literature].

A rare case of a pleomorphic adenoma of the epiglottis in an 82-year-old patient is presented. Resection of the tumor was accomplished by using the CO2-laser and required a partial epiglottectomy. Postoperatively there were no functional impairments. This is the third case of a pleomorphic adenoma of the epiglottis, published in literature, but the first case in which epiglottectomy was performed by endoscopic laser resection.

Adenoma, Pleomorphic↗
PubMed1991

In situ hybridization studies on the expression of type X collagen in fetal human cartilage.

Type X collagen is a short, non-fibril-forming collagen restricted to the hypertrophic, calcifying zone of growth plate cartilage. It is developmentally regulated and found exclusively in hypertrophic cartilage. Here we report on the structure and distribution of human type X collagen based on the cloning of a PCR fragment covering 292 bp of the carboxy-terminal, non-triple-helical domain. Seventy-five percent of the sequence are identical to that of chicken type X collagen at nucleic acid level and 84% at amino acid level. This probe was used for in situ hybridization analyses of type X collagen expression in a human growth plate. Human fetal cartilage, which is different from the avian cartilage-bone transition zone, showed strong type X collagen expression confined to the lower hypertrophic zone of the growth plate. The upper zone of hypertrophic chondrocytes did not contain alpha 1(X) transcripts, indicating that type X collagen expression follows cellular hypertrophy. The distribution of type X collagen mRNA has been previously unreported in chondrocytes from zones of secondary ossification and in chondrocytes associated with endochondral bone trabecules containing calcified cartilage. In situ hybridization analyses with probes for type I and II collagen on consecutive sections indicated a spatial gradient in chondrocyte differentiation in the human epiphysis. Chondrocytes of low type II collagen expression in the resting zone are followed by proliferating columnar chondrocytes with strong type II collagen expression and a zone of hypertrophic chondrocytes synthesizing type X and type II collagen. In contrast to findings in avian growth cartilage in some of our samples of human epiphyseal cartilage hypertrophic chondrocytes continued to strongly express type II collagen down to the chondro-osseous junction. Transcripts of the alpha 2(I) collagen gene, however, were detected only in perichondrium, vascular cavities, and bone, but not in hypertrophic or any other chondrocytes. The above observations demonstrate that the isolation of the human type X collagen DNA will contribute to studies of pathways of chondrocyte differentiation in the mammalian growth plate.

Amino Acid Sequence↗
PubMed1991

Schimke immuno-osseous dysplasia: a newly recognized multisystem disease.

On the basis of five cases personally observed and one previously reported, we describe a disorder characterized by skeletal dysplasia, rapidly progressive nephropathy, episodes of lymphopenia, and pigmentary skin changes. Defects of T-cell function were compatible with an autoimmune process. The disorder is probably of genetic origin and inherited as an autosomal recessive trait.

Antigens, CD↗
PubMed1990

[Pathologic anatomy of osteogenesis imperfecta. Light and electron microscopic studies of supportive tissue and skin].

Osteogenesis imperfecta (OI) is characterised by an abnormal fragility of the bones, and more or less marked blue sclerae. The mode of inheritance is both autosomal dominant and recessive. Facultatively, dentinogenesis imperfecta, abnormal laxness of joint ligaments, and, in early adulthood, deafness, may also be associated. In numerous cases, dwarfism, which may be very marked, and kyphoscoliosis of varying degrees, may also be found. The presumed cause of OI is a disturbance of collagen metabolism, which is associated with an insufficiency state of the osteoblasts; this leads to inadequate formation of osteoid and bone. The first detailed descriptions of the clinical picture were published by Ekman (1788) and Vrolik (1894). In the meantime, the original classification into OI congenital and OI tarda--with its better prognosis--has proved inadequate. In accordance with its genetic heterogeneity, the variations in the clinical symptomatology and its varying prognosis, the condition is, today, divided into four types in accordance with a proposal made by Sillence et al. (1979). The treatment of the genetically determined connective and supporting tissue disease, OI, presents something of a problem. Among the attempts at conservative therapy, treatment with the flavonoid, (+)-catechine, has so far provided the best results. Surgically, pronounced bowing of the tubular bones should be treated by the use of telescopic nails, with the aim of correcting and stabilising them. The diagnosis of OI, as also the differential diagnosis vis-a-vis other osteopenias, has to date been established almost exclusively on the basis of clinical and radiological findings. Differential-diagnostically, juvenile idiopathic osteoporosis, numerous to date unclassifiable osteopenias, and the lethal type II OI, must be distinguished. The aim of this investigation was to establish the diagnosis and differential diagnosis of OI on the basis of light- and electron-microscopic examinations of the supporting tissues. Further, an attempt was made to relate corresponding pathomorphological findings to the clinically different types of OI, and, in forms of OI with a particular course, with so-called hyperplastic callus formation or an increased tendency to develop pseudoarthrosis, to find morphological equivalents. In addition, tissue changes were investigated prior to and during treatment with catechine. Additional investigations of skin biopsies were performed with the aim of correlating morphological findings with the biochemical changes of collagen metabolism.(ABSTRACT TRUNCATED AT 400 WORDS)

Adolescent↗
PubMed1989

Cellular heterogeneity in cultured human chondrocytes identified by antibodies specific for alpha 2(XI) collagen chains.

Collagen type XI is a component of hyaline cartilage consisting of alpha 1(XI), alpha 2(XI), and alpha 3(XI) chains; with 5-10% of the total collagen content, it is a minor but significant component next to type II collagen, but its function and precise localization in cartilaginous tissues is still unclear. Owing to the homology of the alpha 3(XI) and alpha 1(II) collagen chains, attempts to prepare specific antibodies to native type XI collagen have been unsuccessful in the past. In this study, we report on the preparation and use for immunohistochemistry of a polyclonal antibody specific for alpha 2(XI) denatured collagen chains. The antibody was prepared by immunization with the isolated alpha 2(XI) chain and reacts neither with native type XI collagen nor type I, II, V, or IX by ELISA or immunoblotting, nor with alpha 1(XI) or alpha 3(XI), but with alpha 2(XI) chains. Using this antibody, it was possible to specifically localize alpha 2(XI) in cartilage by pretreating tissue sections with 6 M urea. In double immunofluorescence staining experiments, the distribution of alpha 2(XI) as indicative for type XI collagen in fetal bovine and human cartilage was compared with that of type II collagen, using a monoclonal antibody to alpha 1(II). Type XI collagen was found throughout the matrix of hyaline cartilage. However, owing to cross-reactivity of the monoclonal anti-alpha 1(II) with alpha 3(XI), both antibodies produced the same staining pattern. Cellular heterogeneity was, however, detected in monolayer cultures of human chondrocytes.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1988

Absence of fibula and ulna with oligodactyly, contractures, right-angle bowing of femora, abnormal facial morphology, cleft lip/palate and brain malformation in two sibs: a possibly new lethal syndrome.

Absence of fibulae, and unilateral absence of ulna, associated with lateral oligodactyly, and rectangular bowing of the femora are the prominent features of a lethal syndrome studied in two children of related parents. Other malformations are cleft lip and palate and posterior midline abnormalities of the brain. One similar though not identical MCA-syndrome was reported. The literature is reviewed with respect to ulno-fibular malformations.

Abnormalities, Multiple↗
PubMed1987

[Pathogenesis of chest wall abnormalities--electron microscopy studies and trace element analysis of rib cartilage].

In 71 patients with chest deformity (Group B) and in 43 patients who underwent thoracotomy due to heart disease (Group BN), cartilage of the ribs was removed intraoperatively. Analyses of trace elements showed a highly significant decrease in zinc, coupled with a significant increase in magnesium and calcium in Group B. Electron microscope studies in the cartilage of patients with chest deformity revealed chondrocytes with a normal structure only in some parts, but many degenerative altered chondrocytes with vacuoles of fat and osmiophilic depositions, as well as atypical fibrils and so-called "long-spacing collagen".

Adolescent↗
PubMed1986

Biochemical, morphological and immunological findings in a patient with a cutis laxa-associated inborn disorder (De Barsy syndrome).

Clinical symptoms of a male infant are described and compared with cases now classified as the De Barsy syndrome, a distinct disorder related to cutis laxa. Morphologically, elastic fibres in skin were frayed and reduced in number and density. The collagen fibril network was normal. Biochemical studies on collagen metabolism in a skin specimen and in cultured skin fibroblasts showed a normal amino acid content and a normal electrophoretic pattern of collagen constituents. The chemotactic migration of cultured fibroblasts was diminished when compared with fibroblasts from donors of different age groups. Immunological investigations revealed an imparied granulocyte function.

Chemotaxis↗
PubMed1986

Heterogeneity of osteogenesis imperfecta. Biochemical and morphological findings in a case of type III according to Sillence.

A male infant with pale-blue sclerae, who died at the age of 6 weeks through the aspiration of food, presented multiple fractures and deformation of the long tubular bones. The clinical and radiological findings and the course indicated osteogenesis imperfecta, type III, according to Sillence's classification. The family history was unremarkable. Light and electron microscopic studies of iliac crest bone obtained postmortem, showed an abrupt interruption of endochondral ossification, with an active periosteal ossification. In the region of the fractures, a mixed desmochondral callus was seen. The endoplasmic reticulum of the osteoblasts was markedly dilated, the mitochondria were swollen. The osteoid was reduced in quantity. A postmortem analysis of the collagen types I, II and III obtained from skin, cartilage and bone yielded chromatographically normal collagen constituents. An analysis of the amino acids of the collagen alpha-chains showed an increased hydroxylysine content. The radiological findings and the clinical course both indicated type III osteogenesis imperfecta: identical biochemical findings have been described only for type II. The morphological and biochemical findings described here may be a manifestation of a variable expressivity of type III osteogenesis imperfecta. On the other hand, heterogeneity of type II osteogenesis imperfecta cannot be ruled out.

Amino Acids↗
PubMed1986

[Aortic coarctation and osteogenesis imperfecta].

This is the report of a 4 year old patient with osteogenesis imperfecta tarda and aortic coarctation. The resection of the aortic coarctation was performed when the patient was 5 years old. Postoperative recovery and formation of scar tissue presented no problems. Increased operation risk due to osteogenesis imperfecta (White et al., 1983) and possible abnormal formation of scar tissue due to this collagen disorder necessitated detailed preoperative tests of collagen metabolism. We shall discuss the histological and biochemical results of these tests and evaluate the effect of therapy with catechin.

Aorta, Thoracic↗
PubMed1985

Structural changes of collagen fibrils in skeletal dysplasias. Ultrastructural findings in the iliac crest.

The skeletal dysplasias are constitutional, generalized or localized disorders of the skeletal system involving a disturbance of growth and/or bone density; their genetic transmission varies. Pathomorphologically, a combined functional-structural disturbance of the cartilaginous and/or bone tissue is present. Clinically, the result is varying degrees of dwarfism. Within the framework of a systematic examination of skeletal dysplasias, a total of 84 iliac crest specimens/biopsies obtained from stillborn infants and patients varying in age from a few days to 40 years, were investigated in the electron microscope. The sections prepared extended from the perichondrium through the proximal resting zone to the primary mineralization zone. The structure of the collagen fibrils was studied in diastrophic dysplasia, pseudoachondroplasia, the WOLCOTT-RALLISON syndrome, osteogenesis imperfecta, and idiopathic juvenile osteoporosis. In diastrophic dysplasia, pseudoachondroplasia and idiopathic osteoporosis, the cartilaginous ground substance contains collagen fibrils that can vary considerably in length, structure and diameter. In one case of WOLCOTT-RALLISON syndrome, the lacunae of the chondrocytes are found to contain very wide amianthoid-like and inadequately aggregated collagen fibrils. In numerous cases, osteogenesis imperfecta reveals very fine and also irregularly structured collagen fibrils with scarcely discernible cross-striation in the region of the osteoid, which is of varying width. In some of the cases, catechin has a favourable effect on the formation of collagen fibrils, resulting in broader and more densely packed fibrils. In addition, the conditions are associated with considerable intracellular changes in the rough endoplasmic reticulum, the Golgi apparatus and the mitochondria. The varying collagen fibril findings in the cartilage and bone tissue also represent a morphological marker of the combined functional-structural disorder of chondrocytes and/or osteoblasts, and an expression of the differing aetiopathogenesis.

Achondroplasia↗