Olavi Räsänen

A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat

The occurence of the human and rat epidermal SH-protease inhibitors in various human and rat tissues was studied by double radial immunodiffusion against specific antisera to the inhibitors. An immunoreactive protein was found in the extracts prepared from human and rat epidermis and from eosophageal and vaginal squamous epithelia, and from rat pro-ventricular squamous epithelium. No immunoreactive protein was found in man or rat in any other of their tissues, studied by us. The results strongly suggest that a protein reminiscent of the human or rat epidermal SH-protease inhibitor is present in squamous epithelia but not in other tissues. The identity of the epidermal inhibitor and the immunoreactive protein in the other squamous epithelia was confirmed by immunodiffusion, immunoelectrophoresis and gel chromatography, and by immunoinhibition of the papain inhibiting activity of the human epidermal and oesophageal inhibitors by gammaglobulins separated from antiserum to the human epidermal inhibitor.

Localization of the human SH-protease inhibitor in the epidermis: Immunofluorescent studies

Human epidermis contains a low molecular weight SH-protease inhibitor (Human Epidermal Inhibitor = HEI), whose epidermal localization was performed with the indirect immunofluorescence method. The fluorescence was most intensive in the cytoplasms of epidermal cells, often occurring perinuclearly. The fluorescent material in the frozen sections was often finely granular and occasionally extended outside the cytoplasm, while the fluorescence in fixed sections was more uniform, but weaker. Stratum basale generally stained poorly or not at all, as did also stratum lucidum. Stratum corneum stained fairly intensively throughout. In addition to fixation, the outcome of staining was also affected by the thickness of the epidermis, particularly stratum corneum. The significance of this inhibitor for the differentiation of epidermal cells and the keratinization of epidermis has therefore been discussed, and the authors assume it to be of considerable significance in these processes.

Acid and neutral cysteine proteinase inhibitor in normal uterine portio and in squamo-epithelial metaplasia, dysplasias and infiltrative carcinoma of the uterine portio.

Acid cysteine proteinase inhibitor (ACPI) and neutral cysteine proteinase inhibitor (NCPI) were localized in formalin-fixed normal human uterine portio as well as in the squamous cell carcinoma and dysplasias of the uterine portio. The peroxidase-antiperoxidase technique was used. In the squamous epithelium of normal uterine portio, ACPI and NCPI were localized in the cells of the upper and middle layers, mainly in the cytoplasm. In the precursors of cancer, immunoreactivity for ACPI and NCPI declined, and neither of the inhibitors was demonstrable immunohistochemically in the anaplastic squamo-epithelial carcinoma of the uterine portio. Our results suggest that ACPI and NCPI are associated with squamo-epithelial differentiation and that they may also be of significance for the regulation of cysteine proteinase activity in normal tissue and malignant growth.

Cystatin A and B in the development of human squamous epithelia.

The expression of cystatin A (Acid cysteine proteinase inhibitor) and B (Neutral cysteine proteinase inhibitor) during human embryogenesis was studied immunohistochemically by using the PAP-complex method. Both inhibitors were visible first in the developing mucosal tissue at the age of about 9 weeks. In the fetal epidermis (periderm), cystatin B was demonstrated at the age of 11 weeks and cystatin A at 12 weeks. In these young fetuses, the staining was visible in the basal cells, whereas in fetuses older than 17 weeks the staining of both inhibitors diminished in the basal cells. In the skin of 17 to 25 weeks old fetuses, the epidermal staining of cystatin B become weaker than that of cystatin A, and at the age of about 26 weeks, cystatin B disappeared totally. At this stage, cystatin A was localized in the cytoplasm of the middle to upper cell layers of the epidermis. In the squamous epithelia of the mucosal tissues, the staining of the both inhibitors reached their maximal intensity when the fetuses were about 16 weeks old. At the mature fetuses, infants as well as adults, both cystatin A and B seemed to be present in wet squamous epithelia while in the epidermis only cystatin A was expressed.

Ultrasound propagation speed in arthritic synovial tissue

Ultrasonic properties of knee synovial tissues destroyed by arthritis were studied by analysing 40 tissue specimens from 21 patients using an ultrasound echo meter and an optical microscope. The idea was to compare pathological findings to ultrasound propagation speeds, and to try to find any relation between them. The fresh specimens were first measured by the echo meter to collect data for statistical calculations of the propagation speed vs. different pathological properties. Before pathological studies, the specimens were fixed in formalin solution. The connective and fat tissues were evaluated within a resolution of 5% and expressed in percentages (0-100%). Inflammatory cells, edema and villus formation were also evaluated. As results, we obtained several charts of ultrasound propagation speed and their trends in the function of different properties. It could be seen that the trend of the propagation speed increased from 1515 m/s to 1565 m/s when the percentage amount of connective tissue increased from 30% to 90%. The trend of the speed decreased from 1560 m/s to 1480 m/s when the share of fat tissue increased from 0 to 60%. The same phenomenon is already well known from some other tissues. A special new result was that the speed varied in a remarkable range of 1490-1660 m/s in samples of 0% fat and high connective tissue content. The overall average of the ultrasound propagation speed in the specimens was 1548 m/s, and the average of the standard deviations of measurements (each specimen was measured at least twice) of each tissue specimen was 8.3 m/s.

Das Verhalten der kleinmolekularen Cysteinproteinase-Inhibitoren in Lungencarcinomen und den sie umgebenden Geweben

Summary In this work, we have studied the occurrence of acid and neutral cysteine proteinase inhibitors in 3 histologically different lung cancers. The acid cysteine proteinase inhibitor (ACPI) seems to be associated to squamous different at ion as our previous observations have shown. As a new observation we could show that the neutral cysteine proteinase inhibitor (NCPI) was localized in alveolar macrophages.

Localization of the rat epidermal SH-protease inhibitor in the proventricular squamous epithelium using the peroxidase-antiperoxidase (PAP) method.

The rat epidermal SH-protease inhibitor was localized by the PAP method in the squamous epithelium of rat proventricle. Brown accumulation due to the peroxidase reaction was seen in the superficial and middle layers of squamous epithelia. The localization of the inhibitor in squamous epithelium is the same as we have demonstrated with immunofluorescence staining.

Localization of the rat epidermal SH-protease inhibitor in proventricular and vaginal squamous epithelium An immunofluorescence study

The rat epidermal SH-protease inhibitor was localized with the indirect immunofluorescence method in the rat proventricle and vagina fixed in cold phosphate-buffered formalin. Bright fluorescence was seen in the cytoplasms of the superficial layers of these squamous epithelia only when a highly specific antiinhibitor serum was used. The fluorescence diminished when normal rabbit serum or a rabbit antiserum againts bovine serum albumin was used instead of the anti-inhibitor serum. When the anti-inhibitor serum was neutralized with the purified epidermal inhibitor, the fluorescence was again markedly weakened. The results confirm our previous observations showing that the epidermal SH-protease inhibitor also occurs in other squamous epithelia, especially in the cytoplasms of the cells in their upper layers.

Thymolipoma: Report of Case

Thymolipoma is a rare, benign, mediastinal tumour. Thirty-four cases have previously been reported in the literature available to us. One further case is described here. A symptomless 35-year-old man had been misdiagnosed for cardiac enlargement 20 years before he was sent to the hospital. A tumour of 2 000 g was surgically removed. It was asymptomatic, consisted of a large solid mass and extended as long branches in the loose tissue between the mediastinal organs. Histological examination revealed mature fat tissue with islets and strands of thymic tissue.