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Biomedical subjects

K Ohlsson

Publications and source records attributed to K Ohlsson.

298 records · Page 17Linked to original sources
PubMedDate not supplied

Distribution of antileukoprotease in upper respiratory mucosa.

Human respiratory tract secretions contain enzyme inhibitors derived from plasma and a low molecular weight, acid-stable protease inhibitor, antileukoprotease. The distribution of antileukoprotease in normal upper respiratory tract mucosa has been studied using an immunohistologic technique. The inhibitor was localized to the serous parts of the submucosal glands of the maxillary sinus and the trachea but was not demonstrable in mucous glands and goblet cells. It is concluded that the antileukoprotease found in respiratory tract secretions is produced locally in the submucosal serous glands.

Humans↗
PubMedDate not supplied

Localization of antileukoprotease in middle ear mucosa.

The localization of antileukoprotease was studied immunohistologically in normal middle ear mucosa specimens obtained at autopsy and in chronically inflamed middle ear mucosa specimens obtained at middle ear surgery for chronic otitis media. In the sections of normal as well as in the sections of chronically inflamed middle ear mucosa, antileukoprotease localization was confined to PAS-positive goblet cells of surface epithelium and to PAS-positive goblet-like cells of submucosal glands and crypts, whereas ciliated mucosal cells and stratified squamous epithelial cells were devoid of anti-leukoprotease. In comparison with normal middle ear mucosa, an increased number of goblet cells--and thus an increased number of cells containing antileukoprotease--was present in the chronically inflamed middle ear mucosa. Since antileukoprotease is a potent inhibitor of granulocyte elastase and Cathepsin G, it was concluded that this proliferation of the respiratory epithelium during inflammatory processes in the middle ear indicates an increased activity of the biologic defence system against the action of granulocyte proteases.

Autopsy↗
PubMedDate not supplied

Granulocyte protease inhibition in acute and chronic middle ear effusion.

A comparative study was made of granulocyte proteases and protease inhibitors in middle ear effusions (MEE) from patients with acute otitis media (OMA) and serous otitis media (SOM). The mean concentrations of the granulocyte proteases, neutral protease and elastase were three- to fourfold higher in OMA as compared to SOM effusions. The mean concentration of granulocyte elastase in SOM effusions was approximately 1 400, and in OMA effusions 5 500 times higher than the corresponding plasma concentrations. In OMA patients the individual MEE/plasma ratios of the main plasma protease inhibitors, alpha 1-antitrypsin, antichymotrypsin and alpha 2-macroglobulin, showed a positive uniform correlation with corresponding albumin MEE/plasma ratios. In SOM effusions, the concentration of alpha 2-macroglobulin was low, indicating a restricted membrane passage in SOM. In SOM effusions both alpha 1-antitrypsin and the locally produced antileukoprotease showed a residual inhibitory capacity. In OMA effusions the inhibitory capacity of anti-leukoprotease was saturated, whereas there was a residual inhibitory capacity of alpha 1-antitrypsin. However, in those OMA effusions, where large amounts of alpha 1-antitrypsin complexes with granulocyte proteases were found, most of the remaining free alpha 1-antitrypsin was inactive.

Adolescent↗
PubMedDate not supplied

Localization of antileukoprotease in the parotid and the submandibular salivary glands.

Antileukoprotease is the dominating inhibitor of granulocyte elastase and cathepsin G in normal human mixed and parotid saliva. The distribution of antileukoprotease in the submandibular and parotid glands was analysed with an immunoperoxidase technique using specific antibodies against antileukoprotease. Antileukoprotease was demonstrated in the serous cells of both the submandibular and parotid glands. These findings suggest that there is a local production of the inhibitor in the parotid gland and submandibular gland and are in agreement with our previous work which demonstrated high concentrations of the inhibitor in parotid saliva.

Cytoplasm↗
PubMedDate not supplied

Reduced in vivo leucocyte migration and elastase and lysozyme concentrations in skin chamber experiments with piroxicam in healthy volunteers.

Leucocyte migration in vivo, studied with a skin chamber technique was inhibited in eight healthy volunteers after six days' medication with piroxicam, 20 mg a day, but not after only one day's medication. The inhibition was not correlated to the serum content of the drug. The median trough values of piroxicam in serum were 2.5 mg/l and in blister fluid 1.2 mg/l after six days' medication. Leucocyte migration in vitro under agarose was not inhibited after six days' medication with piroxicam. When normal polymorphonuclear leucocytes were incubated with piroxicam in vitro migration under agarose was inhibited but only at piroxicam concentrations higher than those attainable in clinical therapy. The concentrations of elastase and lysozyme in the skin chamber decreased after six days' medication with piroxicam.

Adult↗
PubMedDate not supplied

Kinetics of enzymes released from polymorphonuclear leucocytes in a skin chamber.

Ten healthy volunteers were investigated with a skin chamber technique developed for leucocyte migration studies. Chambers, filled with autologous serum, were harvested at 4, 8, 12, 22, and 30 hours. A marked increase was found both in the concentration of elastase in chamber serum as measured by RIA, and of lysozyme as measured both with lysoplate and electroimmuno assays. The immuno-reactive elastase was shown to consist exclusively of elastase-alpha 1-proteinase-inhibitor complexes. During the first 22 hours the concentrations of elastase and lysozyme were roughly proportional to the number of cells in the skin chamber (r = 0.92 and 0.85). At longer incubation times there was a decrease of relative concentration of elastase but not of lysozyme. Lactate dehydrogenase (LDH) was measured as a marker of the lysis of chamber leucocytes. Lysis was less than 1.5% at all incubation times. The present study shows a release of elastase from primary granules and of lysozyme when polymorphonuclear leucocytes migrate into a skin chamber.

Adult↗
PubMedDate not supplied

Protease inhibitors in rheumatoid synovial fluid: a quantitative analysis.

The concentrations of the main endogenous inhibitors of granulocyte proteases (anti-leukoprotease, alpha 1-antitrypsin, alpha 1-antichymotrypsin, and alpha 2-macroglobulin) were estimated in paired samples of synovial fluid and serum/plasma from seropositive rheumatoid arthritics and controls. Rheumatoid synovial fluid contained significantly higher levels of all inhibitors except antileukoprotease. The influence of the synovial membrane on these concentrations was taken into account by comparing the ratio between the observed concentration and that predicted from a certain regression curve fitted to a set of non-inhibitory reference proteins of extra-articular origin (orosomucoid, albumin, and ceruloplasmin). Divergences were interpreted as the net result of intra-articular production or consumption of the inhibitor in question. The results suggested a consumption of antileukoprotease and alpha 1-antitrypsin in the rheumatoid joint, while the increased levels of alpha 1-antichymotrypsin and alpha 2-macroglobulin probably reflected the altered trans-synovial membrane protein flux with some reservation for alpha 2-macroglobulin.

Adult↗
PubMedDate not supplied

Secretory leucocyte protease inhibitor in the male genital tract: PSA-induced proteolytic processing in human semen and tissue localization.

Secretory leucocyte protease inhibitor, SLPI, is a low-molecular-weight, acid-stable protein present in the liquid part of fresh human ejaculate but not demonstrable in the gel structure. No fragmentation of SLPI occurred during gel dissolution, but a slow proteolytic cleavage of SLPI was seen on incubation of the liquified semen at 37 degrees C. The same pattern of degradation products was seen after incubation of SLPI with prostatic secretion and also with purified prostate-specific antigen, PSA. We could identify Arg 20-Tyr 21 and Met 73-Leu 74 to be the primary cleavage sites upon proteolytic modification of SLPI by purified PSA. However, we did not find any inhibition of the enzymatic activity of PSA by SLPI, even at a 100-fold molar excess of the inhibitor. The slow degradation of SLPI facilitated sampling and the reliable determination of the normal level of SLPI in seminal plasma, which was about 20 mg/L. We investigated the glandular origin of SLPI in the genital tract by immunocytochemistry. A strong immunostaining for SLPI was demonstrated in epithelial cells within the glandular lumina of the prostate gland, seminal vesicles, and epididymis but not in the stromal parts of these glands. In addition the immunostaining was also detected in the deferent ducts and the germinal epithelium of the testes. Taking into account that SLPI is a strong inhibitor of several proteases, including leukocyte elastase and cathepsin G, the results suggest that SLPI has a local protective function against proteolytic degradation of the male reproductive tract tissues during inflammation.

Amino Acid Sequence↗