Control of the bioavailability of a topical steroid; comparison of desonide creams 0.05% and 0.1% by vasoconstrictor studies and clinical trials.
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Biomedical subjects
Publications and source records attributed to O Fyrand.
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Forty-eight patients with acne vulgaris in the face were treated with a water-based (Basiron) and an alcohol-based (Panoxyl) 5% benzoyl peroxide preparation. A randomized double-blind, contralateral study was used. No difference in clinical effect was found. Treatment for 8 weeks resulted in at least 50% reduction in the number of closed comedones, papules and pustules in over 80% of the patients. In more than 70% of the patients, the reduction exceeded 75%. The water-based Basiron caused significantly less skin irritation than the alcohol-based preparation of Panoxyl.
Fibronectins are important glucoproteins of mesenchymal tissue. Fibronectins are also found in the human skin, and tissue cultures demonstrate the production of soluble dimers and insoluble fibrous polymers from dermal fibroblasts. Under the influence of different glucocorticoids, inhibited production of these fibronectins from cultured human skin cells is demonstrated.
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In the present study, cell cultures of fibroblasts from normal skin have been investigated regarding the production of fibronectin. The development of multimeric insoluble fibronectin is demonstrated as small dots at the cell surface, developing into a branched meshwork of fibrous structures in parallel arrays. Soluble dimeric fibronectin is also found in the culture medium.
Fibronectin is a normal glycoprotein in the human organism. It is important in cell/cell and cell/fiber interactions, and demonstrates a specific affinity to collagen. Fibronectin is abundantly present in the skin, mainly in the dermoepidermal junction area, and in the papillary dermis. In lesional skin in dermatitis herpetiformis, the distribution of fibronectin is affected resulting in haziness, gradual degradation and total disintegration, often with the formation of globular droplets. Intraepidermal deposition of fibronectin is found in lesional skin as inter- and intracellular accumulations, mainly in the stratum corneum area. The possible pathophysiological significance of fibronectin is discussed.
Fibronectin is an important constituent of normal human skin, mediating cell/cell and cell/fibre interactions. In affected skin in discoid and systemic LE, changes in the distribution of fibronectin in the dermo-epidermal junction and in the papillary dermis are observed with homogenization and degenerative changes, IF negative gaps and slit formation in the dermo-epidermal region, together with IF positive globular bodies and transport of fibronectin into the epidermis. Unaffected skin in LE demonstrates the pattern of fibronectin as found in normal human skin.
The fibronectins are a group of glycoproteins present in plasma and cellular tissues. They are produced by fibroblasts and endothelial cells, and are of importance in cellular adhesion and spreading. Fibronectin has a special affinity to fibrous proteins such as collagen and elastin, and is abundantly present in normal skin in the dermo-epidermal junction area, dermis, and subcutis. Fibronectin is not found in the epidermis. In a number of diseases fibronectin can be demonstrated in the epidermis of lesional skin, with or without affection of the dermo-epidermal junction area. Such changes are found in psoriasis vulgaris, lupus erythematosus, bullous pemphigoid and dermatitis herpetiformis, and represent the exoserosis of plasma and/or transepidermal elimination of degenerated tissue structure with fibronectin from the dermo-epidermal junction and the papillary dermis.
In twelve synovial fluid/serum pairs from patients with various types of seronegative polyarthritis, homogeneous gamma-bands by agarose gel electrophoresis were found in seven of the synovial fluids and in only one of the sera. In six of the fluids with gamma-bands, smooth muscle antibodies (SMA) were also present, usually in a titre identical to that in serum. In fluids with no gamma-bands, no SMA were detected. In forty synovial fluid/serum pairs from paitients with seropositive rheumatoid arthritis, no gamma-bands were detected in the synovial fluids, and SMA were present in only three pairs. Absorption and inhibition experiments did not give evidence that the SMA activity in seronegative polyarthritis was confined to the gamma-bands in the synovial fluids. The SMA activity in the fluids seemed to be directed against both actin and 'non-actin' muscular antigens. The association between locally produced oligoclonal immunoglobulins and possible locally produced SMA with differnet electrophoretic mobility suggests that in some of thes patients there is a local synovial production of oligoclonal antibodies with different specificities. Thus, even if the results may indicate a local virus infection in some arthritic joints, they may also be dur to an unspecific local stimulation of B cells or to a specific antigen stimulation combined with an unspecific co-activation of other antibody-producing cells.
Affected and unaffected skin from patients with vulgar psoriasis and normal skin from a control group were investigated for the presence of fibronectin with an indirect immunofluorescence technique. In the control group, fibronectin is missing in the epidermis, but is found in the basement membrane zone of the dermo-epidermal junction area, in the papillary and the reticular dermis, and in the vascular and neural systems of the skin. The same distribution is also found in unaffected psoriatic skin, whereas in affected skin a change in the distribution of fibronectin is found in the dermis and in the basement membranes, together with the presence of fibronectin in the epidermis, mainly in the cornified layers.
Fibronectin is a glycoprotein mediating contact between cellular elements and collagen. As judged by indirect immunofluorescence studies fibronectin is abundantly present in normal human skin. It is located in the dermo-epidermal junction area, in the papillary and reticular dermis, about epidermal appendages (pilosebaceous units and eccrine sweat glands) and in the vascular and neural structures.
Synovial tissue from 8 patients with psoriatic arthritis (PSA) were investigated by direct immunofluorescence technique with FITC-conjugated anti-F(ab')2 antiserum, and with a specific rabbit anti-human T-lymphocyte antiserum by indirect immunofluorescence method with FITC-conjugated goat-anti-rabbit Ig antiserum as the second layer. The majority of the lymphocytes in the tissue displayed membrane fluorescence with the anti-T antiserum. Staining with the conjugated anti-F(ab')2 antiserum revealed both intra- and extracellular immunoglobulins. These results indicate that the majority of the lymphocytes in the synovial tissue of PSA are T-lymphocytes, and that a minor number of the cells belong to the B-cell line.
Psoriatic arthritis (PA) is included in the seronegative arthritis group, though it is now generally considered to represent a clinical entity. In PA, in contrast to psoriasis vulgaris and to other types of rheumatoid arthritis, only a few immunological studies have been reported. In the present report synovial joint membranes from patients with PA and control groups have been studied for the presence of (a) vascular changes, (b) fibrin, (c) immunoglobulins and complement factor C3.
Fibronectin is a glycoprotein which is responsible for a varity of functions in the human organism, such as mediation of contact between cells and between cells and fibres, opsonic qualities, interaction in the stabilization of fibrin, etc. Fibronectin is an important constituent of the ground substance having a special affinity to collagen. In indirect immunofluorescence studies its presence has been abundantly demonstrated in normal human skin, in collagen-rich structures such as the basement membranes, the papillary and reticular dermis, and in the vascular and neural structures, demonstrable by its characteristic staining patterns. Fibronectin is not found in the epidermis. In lichen planus, the distribution in unaffected skin is identical with that in normal skin, whereas in affected skin, changes in the pattern of fibronectin are found. The basement membrane zone becomes broader and hazy, later undergoing disintegration and destruction, concomitant with swelling and homogenization of the reticular distribution of fibronectin in the papillary dermis. Globular structures containing fibronectin are found in the basement membrane area, together with an intensified immunofluorescence in the vascular system. Fibronectin has certain adhesional properties and changes in the distribution of this glycoprotein may result in loss of tissue stability. The pathophysiological significance of the changes of fibronectin in lichen planus is, however, difficult to evaluate at present.
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Cold insoluble globulin (CIG) is a normal glycoprotein of human serum and plasma. The physiological significance of this protein is unknown, but is shows a temperature-dependent relation to fibrinogen and fibrin. It is possible that it represents a substrate for activated fibrin-stabilising factor in the polymerisation of fibrin. CIG is found on the surface of fibroblasts. In the present study CIG was estimated in citrated plasma in 115 patients with rheumatic diseases. Increased amounts were found in patients with systemic lupus erythematosus, secondary amyloidosis in classical and definite rheumatoid arthritis, and in male patients with juvenile rheumatoid arthritis.
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