Biomedical subjects

I Stas

Publications and source records attributed to I Stas.

3 recordsLinked to original sources

PubMed1998

[Atopic dermatitis].

For the past decades, the prevalence of atopic dermatitis is on the rise. Three phases of the disease are recognized according to the age of the patient, either in the newborn age, in infancy or after puberty. A partial enzymatic defect in delta-6 desaturase has been reported. Such metabolic anomaly would be responsible for the alterations in both the skin barrier function and in the Th2 inflammatory reactions in part mediated through IgE. Some microorganisms colonizing the skin play an important causal role in the clinical exacerbations. The influence of food allergy on atopic dermatitis remains obscure and often unconvincing. By contrast, irritant and allergic challenges from the environment exhibit an undisputable worsening effect. The prevention relies on the eviction of predisposing factors and is favourably influenced by emollients specifically designed for atopic dermatitis. A food supplementation in alpha-linoleic acid and some specific chinese herbal remedies might well be useful. The treatment relies primarily on topical applications of corticoids. Puva-therapy, UVB phototherapy and immunomodulation by cyclosporine are indicated for difficult cases.

Administration, Topical↗

PubMed1996

Primary systemic amyloidosis. A report of 2 cases.

We report 2 cases of primary systemic amyloidosis. A monoclonal gammopathy was confirmed at the postmortem examination of the first patient. An extensive search for evidence of chronic infection, inflammation, neoplasms and paraproteinemia was conclusively negative in the other patient. The recognition of cutaneous signs of primary systemic amyloidosis is crucial to insure a rapid management aimed at postponing the fatal issue of the disease.

Aged↗

PubMed1994

Gelatinase A expression and localization in human breast cancers. An in situ hybridization study and immunohistochemical detection using confocal microscopy.

The gelatinase A (72 kDa type IV collagenase) is a matrix metallo-proteinase which degrades basement membrane collagens. Various studies emphasize its role in stromal invasion of cancers, but there is some controversy about its origin. Gelatinase A was localized by immunohistochemistry using confocal microscopy in 15 human mammary carcinomas. In addition, the cells responsible for the synthesis of this enzyme were detected by in situ hybridization. Most invasive and non-invasive tumour cells were labelled by immunohistochemistry. Of particular interest was the pattern observed in some pre-invasive areas. Gelatinase A was found in fibroblasts in close contact with pre-invasive tumour clusters. Confocal observation allowed a more precise localization of gelatinase A to the periphery of tumour clusters along the basement membranes and in peritumour fibroblasts. The malignant epithelial cells were negative by immunohistochemistry in these areas. By in situ hybridization, mRNAs encoding gelatinase A were detected only in fibroblasts in close contact with pre-invasive and well differentiated tumour clusters. These findings support the hypothesis that peritumour fibroblasts produce gelatinase A and that breast cancer cells may bind this enzyme to their cell surface and/or internalize it.

Amino Acid Sequence↗