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Biomedical subjects

K Hochstrasser

Publications and source records attributed to K Hochstrasser.

At least 73 records · Page 4Linked to original sources

[Studies for proteolysis in malignant tumours (author's transl)].

It's well known that increased proteolytic activity in plasma as well as in interstitial fluids is often associated with malignant tumours. There are numerous reports that cell cultures of malignant origin contain plasminogen activators responsible for an increased proteolysis. Our studies showed that patients with a carcinoma excrete in their urine a significant higher amount of an acid-stable inhibitor than healthy patients. This urine inhibitor is a split product (MW: 30,000) of the Inter-alpha-trypsin inhibitor (MW: 180,000). We conclude that the increased amount of acid-stable split products is the result of increased proteolysis in patients with malignant tumours. In contrast to other authors we do not think that the activation of plasmin by plasminogen is responsible for the proteolytic cleavage of ITI. Otherwise proteolysis by Cathepsin G and granulocytic Elastase would be reasonable. So enhanced proteolysis seems to be a sign of general enzymatic change associated with transformation.

Carcinoma, Squamous Cell↗

Naturally occurring low molecular weight inhibitors of neutral proteinases from PMN-granulocytes and of kallikreins.

Human mucous secretions contain low molecular weight (Mr approximately 11,000) acid-stable inhibitors directed against elastase and cathepsin G from PMN-granulocytes. Important biochemical properties of these inhibitors are presented and their possible biological function is discussed. An inhibitor of glandular and plasma kallikreins preventing kinin-liberation from kininogen but not ester hydrolysis was obtained from rat kidney tubules. A molecular weight of about 4700 was estimated for this kallikrein-specific inhibitor (trypsin-induced kinin-liberation is not prevented).

Amino Acid Sequence↗

[Fibrin and fibrinogen degradation products in head- and neck-tumors (author's transl)].

Fibrinogen degradation products (FDP) in sera of patients with malignant tumors in the head-and neck-region are determined with Staphylococcal-Clumping-Test (Behring-Werke, Marburg/Lahn). Concentration of FDP in sera of tumor patients are compared to sera of normal patients. 40 cases out of 70 with malignant tumors showed higher concentration of FDP. The results are discussed.

Fibrin Fibrinogen Degradation Products↗

[Experimental investigations on the proportional inhibitory capacity of different proteinase inhibitors in cases of chronic otitis media and cholesteatoma (author's transl)].

Among the three investigated proteinase inhibitors alpha-1-antitrypsin ("acute phase protein") possesses the highest antiproteolytic capacity. Alpha-2-macroglobulin reaches as an average one fifth of the preoperative level of alpha-1-antitrypsin and postoperatively one quater of this inhibitor level. The average concentrations of the low molecular acid stable proteinase inhibitor of the mucous membrane in the preoperative phase are about equivalent to the concentrations of alpha-2-macroglobulin. In the postoperative phase the concentrations of the low molecular acid stable inhibitor are a slightly lower than those of alpha-2-macroglobulin. The samples of the middle ear secretions from cases with chronic otitis media or with cholesteatoma do not differ essentially in their concentrations of the different proteinase inhibitors.

Cholesteatoma↗

[The role of inter-alpha-trypsin-inhibitor (concentration of serum of childhood) (author's transl)].

The feeble monovalent, humoral protease inhibitor inter-alpha-trypsin inhibitor has to be regarded as inhibitogen for different secretory, low-molecular, polyvalent inhibitors. Kallikreine acts as inhibitor-releasing enzyme. The inhibitor levels in the serum were determined for children of different ages. Contrary to adult patients not showing a lack of inhibitogen as consequence of the disease, inhibitogen insufficiencies are rather frequent, particularly for prematures and newborns with respiratory distress and inflammatory diseases. Obviously, in early childhood the production of inhibitogen is not yet in full progress. In case of increased inhibitor consumption or excessive kallikrein consumption this condition results in an inhibitogen insufficiency.

Adolescent↗

[About degradation products of the inter-alpha-trypsin inhibitor in serum. I. The inter-alpha-trypsin inhibitor as precursor of the acid stable trypsin-plasmin-inhibitor of the serum (author's transl)].

The humoral inter-alpha-trypsin inhibitor is to define as precursor of the acid stable trypsin-plasmin-inhibitor in the serum. The inhibitor is filtrated by the glomerulum and excreted in the urine. The serum level of the inhibitor is increased in nephropathy. Using a new assay for the intact precursor it was found that during inflammation the decreased precursor level indicates an increased turnover, though the glomerular filtration of the acid-stable inhibitor is within normal range. The increase of the precursor level during nephropathy indicates that the kidney is the main degradation organe for the inter-alpha-trypsin inhibitor. Nevertheless, an increase of the acid-stable inhibitor is to be seen. This fact is only to explain if it is assumed that the inter-alpha-trypsin inhibitor is permanently degraded everywhere in the organism.

Fibrinolysin↗

[About degradation products of the inter-alpha-trypsin inhibitor in serum. II. Acid label derivatives of the inter-alpha-trypsin inhibitor (author's transl)].

Simultaneous to the liberation of the acid stable trypsin-plasmin-inhibitor from the inter-alpha-trypsininhibitor in vivo, acid labile degradation products are set free. The main product can be estimated by immunological methods. This product is not excreted by the kidney in contrast to the acid stable inhibitor. The product accumulates in serum in different diseases. An increased concentration of this product indicates also an increased turn-over of the inter-alpha-trypsin inhibitor in the case when the concentraton of the intact inter-alpha-trypsin inhibitor or of the filtrable derivative are within normal range.

Humans↗

[The investigation of a low molecular acid stable proteinase inhibitor in the middle ear secretion (author's transl)].

The proteolytic activity of different proteinases during chronic otitis media can be inhibited by alpha-2-macroglobulin and alpha-1-antitrypsin. A new low molecular (13,000) acid stable and polyvalent proteinase inhibitor could be investigated in the middle ear secretion from patients with cholesteatoma and chronic otitis media. We believe that this inhibitor is identical with the low molecular inhibitor of bronchial mucus and the nasal fluid. This inhibitor shows a high anti proteolytic capacity and can inactive trypsin, chymotrypsin, pronase and leucocytic preoteinases. The inhibitor is not detectable in any case. We could find it in 55 cases, three specimens of middle ear secretions obtained no acid stable inhibitor. It is present in the secretion in a masked form by in situ-reaction with leucocytic proteinases. By denaturating deproteinizing it is liberated out of the complex with proteinases and can be measured. The investigations demonstrate that the level of the inhibitor varies during the course of a chronic otitis media. In the postoperative phase the inhibitor concentrations were clearly higher than preoperatively. A steep drop of inhibitor can be observed in cases of chronic otitis with the symptomatology of an acute inflammation. In cases with a chronic inflammation the inhibitor level seems to remain low. The decrease of the inhibitor is explained as a using up effect during reaction between inhibitor and leucocytic proteinases. We believe that this inhibitor in the middle ear secretion results from a limited proteolysis and splitting of inter-alpha-trypsin inhibitor by a proteolytic enzyme, possibly by kallikrein.

Ear, Middle↗

[Biochemical findings in proteincomposition of secretions of human malignant parotid tumours, chronic parotitis and sialadenoses (author's transl)].

In comparison to former investigations in pleomorphic adenoms and Wharthin tumours in the present paper secretion of IgA, lysozyme in correlation to flowrate and total secretion in glands with malignant tumours, inflammations and Sialadenosis were estimated. Thereby 12 patients with malignomas of the parotid gland, 11 patients with chronic parotitis and 12 with sialadenoses were examined. The following results were found: 1. The concentration of protein, IgA and Lysozym is significantly higher than in normal glands and in glands with pleomorphic adenomas and Wharthin tumours. 2. Differentialdiagnosis of Sialadenitis and Sialadenosis of parotid glands is possible by estimating the examined parameters. Thereby in glands with sialadenosis flowrate is higher than in normal glands, and significant lower in glands with sialadenitis. Moreover concentrations of IgA and Lysozyme and protein in glands with sialadenitis are evaluated.

Chronic Disease↗

[The inter-alpha-trypsin inhibitor as precursor of the acid-stable proteinase inhibitors in human serum and urine].

A small amount of antitryptic activity is detectable in the supernatant of deproteinized human serum. Preincubation of serum with trypsin causes an increase in acid-stable antitryptic activity. This rise in activity depends on the inter alpha-trypsin inhibitor concentration. The native inhibitor present in normal sera, and in higher concentrations in sera of patients with nephropathies, and the trypsin-liberated inhibitor show immunological cross reaction with antibodies to the serum inter-alpha-trypsin inhibitor. The two inhibitors differ in molecular weight and electrophoretic mobility. The physiological inhibitor (I-34), with a molecular weight of 34 000 and a high carbohydrate content, can be transformed by trypsin into an inhibitor (I-17) with a molecular weight of 17 000. This inhibitor is identical with the inhibitors liberated by trypsin from serum or from purified inter-alpha-trypsin inhibitor. The acid-stable inhibitor from urine is identical with the physiological serum inhibitor. Analogously, this inhibitor is transformed by trypsin into the inhibitor with a molecular weight of 17 000. We conclude that the inter-alpha-trypsin inhibitor is the precursor of both the physiological and the trypsin-liberated inhibitor. By a mechanism as yet unknown, but most likely a limited proteolysis, the secreted inhibitor is liberated from the high molecular weight precursor. In contrast to the monospecific trypsin-inhibiting precursor, the physiological and artificially liberated inhibitors are trypsin/chymotrypsin/plasmin inhibitors.

Humans↗

The enzymology of nasal secretion.

Normal human nasal fluid contains several enzymes of the intermediary metabolism as well as a specific protease inhibitor, which inhibits trypsinm chymotrypsin and leucocytic proteases. During the course of acute and chronic nasal and paransal sinus infections the inhibitor level varies. The inhibitor level is an indicator of poor healing. It is possible too, to differentiate viral rhinitis from bacterial or allergic or atrophic rhinitis by a signigicant increase of the activities of the enzymes GOT, LDH and CPK.

Humans↗

[Experimental studies on the question of the enzymatic destruction of the ossicular bones during middle ear inflammations (author's transl)].

The proteolytic activity of purulent middle ear secretions from patients with cholesteatoma, chronic otitis media, acute otitis media and radical mastoid cavities were investigated. The proteolytic activity in the secretions from cases with cholesteatoma is higher than from patients with other chronic otitis media. The collagenolytic effect of the matrix of cholesteatoma combined with the high level of the bacterial and leukocytic proteinases in the middle ear secretions is undoubtedly one of the main factors in the destruction of the ossicular bones.

Cholesteatoma↗

[On the secretion of BAEE-esterase activity (kallikrein) in normal human parotid glands in rest and under stimulation (author's transl)].

Kallikrein is an important mediator in microcirculation. Therefore, this work has been concerned with the excretion of kallikrein from human parotid glands. In 40 healthy persons kallikrein concentrations in resting parotid saliva were estimated. Subsequently, the glands were stimulated either by ascorbic acid or by subcutaneous injection of pilocarpin and the changes in BAEE-esterase activity were measured. The results show a significant increase of excreted enzyme on stimulation. Continuous stimulation, however, leads to exhaustion of the capacity of the glands within 40 min. After cessation of stimulation basal secretion rates are restored in the next 15 min. Kallikrein secretion is compared to the secretion of total protein, lysozym and immunglobulin A.

Adolescent↗

[The proteincomposition of human parotid saliva in acute and chronic parotitis. Quantitativ densitometry of single protein-fractions in comparison to normal secretions].

By means of acrylamidgelectrophoresis parotid secretions of patients with acute and chronic parotitis were examined. Thereby significant changes in protein patterns of electrophoretic separation were found. Especially two bands are described in detail. One in the cathodal near gel region, the isoamylases, and the otherone in the anodal part of the gel, identified as albumin. In rest and under stimulation these bands show signficant changes compared to normal secretions. Furthermore information about the capacity of the parotid gland parenchyma is won by observing the changes of amylase bands in rest and under stimulation in chronic parotitis without actute exacerbations. The amylase shows a remarked decreased secretion in chronic parotitis under stimulation corresponding to parenchymalteration. The same happens with the albuminexcretion as parameter for ductlesions. In chronic parotitis albmuninexcretion goes parallel to duct changes in sialography. Therefore by discelectrophoretic separation of native parotid saliva a helpful mean for diagnostic use is given, besides sialography and scintigraphy.

Acute Disease↗