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K Hochstrasser

Publications and source records attributed to K Hochstrasser.

At least 55 records · Page 3Linked to original sources
PubMed1983

[Comparative cytologic studies of human nasal secretions (differential smears of secretions in patients following laryngectomy and patients with rhinitis sicca in comparison with healthy subjects)].

Using a new method, exfoliative cytologic examinations were performed in patients after laryngectomy and in patients with rhinitis sicca in comparison to normal nasal mucosa. In patients after laryngectomy an increased rate of nasal secretion can be seen. In the nasal smear the main fraction of cells are ciliated epithelial cells. Contrariwise, in patients with rhinitis sicca many squamous epithelial cells can be found. The new method enables the preparation of quantitative cytograms.

Adult↗
PubMed1983

[Diagnostic value of nasal secretions, current state: normal values. 1].

Separation of pure nasal secretions has been very difficult until now. Therefore, examinations were performed only with a small number of patients. Employing a new method to separate pure nasal secretions it is now possible to perform routine examinations. In this paper the protein composition and electrolyte patterns of normal human nasal secretion is reported. The amount of nasal secretion depends from the location and region of human nasal mucosa. The average amount is between 135 and 75 microliters. The protein concentration shows a very wide variation in the normal secretion between 200 and 3500 mg%. The average concentration in the upper nasal meatus is 950 mg%, in the lower nasal meatus 1100 mg%. Selective glycoprotein stainings show that the main part of nasal secret proteins are glycoproteins. The electrolyte concentrations were calculated for sodium 90-148 mval, potassium 6-28 mval and calcium 2-3.5 mval.

Adolescent↗
PubMed1982

Disturbances of selected plasma proteins in hyperdynamic septic shock.

This study was performed on patients (n = 18) suffering from strictly defined hyperdynamic septic shock. Plasma factors (C-reactive protein, acid alpha 1-glycoprotein, fibrinogen, fibrinopeptide A, fibrinogen-fibrin split products, factor XIII, antithrombin III, complement factors C3 and C4, inter-alpha-trypsin-inhibitor and alpha 2-macroglobulin) measured during hyperdynamic septic shock were highly abnormal. The activation and consumption of clotting, fibrinolytic and complement factors due to system-specific proteinases (such as thrombokinase or plasminogen activators) seemed to be intensified by the nonspecific proteolytic activity of granulocytic proteinases probably released by the action of endotoxins. Possible therapeutic measures to maintain the endogeneous defence mechanism against enhanced proteolysis during septic shock are discussed.

Alpha-Globulins↗
PubMed1981

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, IV. The amino acid sequence of the human urinary trypsin inhibitor isolated by affinity chromatography.

An acid-resistant trypsin inhibitor from human urine and serum is released in vivo by limited proteolysis from the high molecular acid-labile inter-alpha-trypsin inhibitor. The inhibitor shows an apparent molecular mass of 30 000 Da and is composed of two Kunitz-type domains. The domains are released in vitro by prolonged tryptic hydrolysis. The C-terminal domain is responsible for antitryptic activity. For the other domain no inhibitory activity towards proteinases, i.e. chymotrypsin, trypsin, pancreatic and leucocytic elastase has been demonstrated so far. The polypeptide chain comprising both domains consists of 122 residues and has a molecular mass of only 13 400 Da. In this work we have found that both, the N-terminal extension peptide with 21 residues and the "inactive" domain are linked O-glycosidically and N-glycosidically, respectively, with large carbohydrate moieties. The N-terminal amino acid sequence of the human urinary trypsin inhibitor was determined by solid-phase Edman degradation of a single peptide. The molecular mass calculated for the total polypeptide chain of 143 residues should be 15 340 Da; from the difference to the measured value (30 000 Da) it is concluded that the glycopeptide contains a considerable carbohydrate moiety.

Alpha-Globulins↗
PubMed1981

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates in the human urinary trypsin inhibitor isolated by affinity chromatography.

The inhibitory active part of the inter-alpha-trypsin inhibitor with a known amino acid sequence is present as an acid-resistant inhibitor in human serum, in urine, in bronchial and in nasal mucus. The inhibitor molecule has a 50% carbohydrate content. Carbohydrate side chains are attached in two positions. One chain is linked to the polypeptide O-glycosidically via the serine residue in position 10 in the N-terminal extension peptide. The second side chain is attached N-glycosidically via the asparagine residue in position 24, located in the inactive "inhibitory" Kunitz-type domain of the inhibitor. The composition of the carbohydrate side chains were determined.

Alpha-Globulins↗
PubMed1981

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor. VI. Detection of a complex between immunoglobulin g and the inhibitory active part of the inter-alpha-trypsin inhibitor.

A latent trypsin inhibitor is released from denatured human serum proteins by proteolytic digestion with thermolysin. The latent inhibitor was enriched by chromatography on DEAE-Sephacel, Sephadex G-200, and Protein A-Sepharose, respectively. Immunological cross-section identified the latent inhibitor as a complex between IgG and the inhibitory active part of the inter-alpha-trypsin inhibitor.

Alpha-Globulins↗
PubMed1981

An elastase-specific inhibitor from human bronchial mucus. Isolation and characterization.

It was shown previously that human bronchial mucus contains an acid-stable proteinase inhibitor directed against trypsin and chymotrypsin, polymorphonuclear granulocyte elastase and cathepsin G. In addition to this well-characterized inhibitor, designated here as BSI-ATE (identical with the inhibitor HUSI-I from human seminal plasma or antileucoprotease), another acid-stable inhibitor BSI-E is present in the mucus which exerts inhibitory activity towards porcine pancreatic and human granulocytic elastase, but not against trypsin, chymotrypsin, or granulocytic cathepsin G. This elastase-specific inhibitor was isolated by affinity chromatography. Its molecular mass and its amino acid composition are very similar to those of BSI-TE. An immunological cross-reactivity between both inhibitor species was not observed. In the mucus of patients suffering from obstructive airway disease the elastase-specific inhibitor is not present in the free form but can be liberated by acidification.

Amino Acids↗
PubMed1979

[Clinical-functional emphysema diagnostics and immunological correlations (author's transl)].

By application of the correlation flow resistance/intrathoracic gas volume the lung emphysema is differentiated in quality within the scope of chronic obstructive lung diseases. For these groups immunoglobulins, the alpha1-trypsin activity in serum and the activity of further protease inhibitors were determined. There are no substantial variables in the different groups with regard to immunoglobulins. In the emphysema group alpha1-antitrypsin was a little reduced. This group included 2 patients with an alpha1-antitrypsin deficit. The two-dimensional separation of the inter-alpha-trypsin big inhibitor shows 3 areas which decrease significantly in case of severe emphysemata. The irritation of the inter-alpha-trypsin big inhibitor, i.e. in its turnover, parallel to the increasing degree of emphysema formation, is discussed.

Adult↗
PubMed1979

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, I. Determination of the amino acid sequence of the antitryptic domain by solid-phase Edman degradation.

The acid-stable trypsin inhibitor of human serum and urine is released in vivo by limited proteolysis from the high molecular weight, acid-labile inter-alpha-trypsin inhibitor. When complexed with trypsin, both this acid-stable, active derivative and the inter-alpha-trypsin inhibitor can be degraded in vitro by prolonged digestion with trypsin to a low molecular weight "minimal" inhibitor. This minimal trypsin inhibitor was sequenced and found to be homologous to the known Kunitz-type inhibitors (e.g. the basic trypsin-kallikrein inhibitor from bovine organs). This indicates that the antitryptic activity of the big inter-alpha-trypsin inhibitor is due to a Kunitz-type domain.

Alpha-Globulins↗
PubMed1979

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, II. Characterization of a second inhibitory inactive domain by amino acid sequence determination.

A short digestion with excess of trypsin releases an inhibitor with an apparent molecular weight of 14,000 from both the inter-alpha-trypsin inhibitor and the ITI-related acid-stable inhibitor. The amino acid sequence of this inhibitor was determined. The inhibitor is composed of two covalently linked homologous Kunitz-type domains. One domain has antitryptic activity, as reported. This paper characterizes the second, inactive domain as also of the Kunitz type.

Alpha-Globulins↗
PubMed1979

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, III. Sequence of the two Kunitz-type domains inside the native inter-alpha-trypsin inhibitor, its biological aspects and also of its cleavage products.

The human inhibitor HI-14 consists of two Kunitz-type domains covalently connected. They are liberated from the human ITI by limited tryptic proteolysis. The inhibitor HI-14 is formed via a trypsin inhibitor complex. We have reported the amino acid sequences of the domain with antitryptic activity and the homologous domain without activity. Here we present the sequence of the domains as present in ITI. The domain lacking antitryptic activity is the N-terminal part of the inhibitor HI-14, whereas the domain with antitryptic activity represents the C-terminal part of HI-14 and probably the C-terminus of the ITI-molecule, too.

Alpha-Globulins↗
PubMed1979

Human inter-alpha-trypsin inhibitor. Limited proteolysis by trypsin, plasmin, kallikrein and granulocytic elastase and inhibitory properties of the cleavage products.

The acid-labile inter-alpha-trypsin inhibitor is cleaved enzymatically in vivo, liberating a smaller acid-stable inhibitor. The molar ratio of native inhibitor to this smaller inhibitor in plasma is significantly changed in some severe cases of inflammation and kidney injury. To clarify this observation on a molecular basis, the action of four different types of proteinases (trypsin, plasmin, kallikrein and granulocyte elastase) on the inter-alpha-trypsin inhibitor was studied. The initial rate of cleavage of the inter-alpha-trypsin inhibitor by a 1.3-fold molar excess of proteinase over inhibitor was found to be 4375 nM x min-1 with granulocyte elastase, 860 nM x min-1 with trypsin, 67 nM x min-1 with plasmin, and 0.3 nM X min-1 with kallikrein. Obviously, of the enzymes studied so far, the granulocyte elastase known to be released during severe inflammatory processes is by far the most potent proteinase in the transformation of the inter-alpha-trypsin inhibitor. The inter-alpha-trypsin inhibitor and its cleavage products inhibit bovine trypsin very strongly (Ki = 10(-9)--10(-11) M), porcine plasmin much less strongly, human plasmin very weakly and pancreatic kallikrein practically not at all.

Alpha-Globulins↗