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Biomedical subjects

K Hochstrasser

Publications and source records attributed to K Hochstrasser.

At least 91 records · Page 5Linked to original sources
PubMed1976

[Simultaneous estimations of flowrate, protein, immunoglobulin a and lysozyme secretion of human parotid glands with whartin tumours and scintigraphic and sialographic examinations (author's transl)].

7 patients with uni- and bilateral Whartin tumors are examined. In comparison to sialographic and scintigraphic findings simultaneous estimations of flowrate, total protein, immunoglobulin A and lysozyme excretion of these glands in rest and under stimulation are done. Thereby the following results were found: 1. Flowrate is normal like in glands with pleomorphic adenomas. 2. Total protein secretion is significant lower in stimulated secretions. 3. Immunoglobulin A secretion is diminished in stimulated secretions, lysozyme is diminished under rest and stimulation.

Adenolymphoma↗
PubMed1976

[The isoenzyme pattern of lactate-dehydrogenase in nasal secretions (author's transl)].

In the present study, the qualitative and quantitative isoenzyme pattern of lactate-dehydrogenase (LDH) in nasal secretions of 52 probands without disease in the nose is investigated electrophoretically. It was found that the LDH-isoenzyme pattern in nasal secretions does not only differ clearly from the distribution of LDH-isoenzymes is serum of the same probands but is characterized especially by a high percentage of LDH 3- and LDH 4-fractions; this corresponds to the monomeres H2M2 and HM3. These results differ completely from any other enzymatic pattern in the human organism. The results clearly indicate that LDH in nasal secretion is a product of the mucous membranes and does not originate from the serum by means of transsudation into the nasal secretion.

Humans↗
PubMed1976

[Simultaneous estimations of flowrate, total protein,- lysozyme- and immunglobulin-A-secretion in parotid glands with mixed tumours (author's transl)].

In comparison to normal gland secretions 28 patients with mixed tumors of the parotid glands are examined. Thereby fractionated secretions under rest and stimulation are collected and estimations of flowrate, protein-, lysozyme- and immunglobulin A-secretion are done. The following results are remarkable: 1. After pilocarpinstimulation response of the glands 20 to 30 min later than in normal glands. 2. Protein-secretion is diminished in rest and under stimulation. 3. Immunglobulin A and lysozyme secretion show a greater range than normal glands under rest and stimulation.

Adenoma, Pleomorphic↗
PubMed1976

[Experimental studies on the reaction of the immunological system during chronic otitis media and about the course of this disease (author's transl)].

During chronic otitis media intact immunoglobulins are split due to the proteolytic activity of extracellular bacterial proteinases into fragments of different molecular weight. The most malignant bacterial proteinases are the proteinases of pseudomonas aeruginosa (pyrocyanea). These proteinases can only be inhibited by alpha-2-macroblobulin of human blood serum. Because of its high molecular weight we find this inhibitor only in a very low concentration in the middle ear secretion. The destruction of the immunoglobulins is certainly one of the factors of weakening the immunological system in the middle ear. The inhibitory system with alpha-1-antitrypsin, inter-alpha-trypsin inhibitor and alpha-1-antichymotrypsin is unable to inhibit these bacterial proteinases of pseudomonas aeruginosa. The only possibility to get a high concentration of alpha-2-macroglobulin in the middle ear secretion is the liberation of this inhibitory by injuring blood vessels during a tympanoplasty. By this procedure the proteinases of pseudomonas aeruginosa with maximum activity at pH 7.8 and with a high proteolytic activity are almost completely inhibited. By blocking these proteinases combined with an appropriate antibiotic therapy and with the reconstruction of the destroyed parts of the middle ear by a tympanoplasty we can produce a preponderance of the immunological system as compared with the proteolytic activity of the proteinases. This high proteolytic activity can be a cause of the destruction of the small processes of the ossicular bones, especially of the lenticular process of incus. In order to demonstrate that there are proteolytic splitting processes of intact immunoglobulins, a quantitative analysis of the immunoglbulins IgG, IgA and IgM was done pre- and postoperatively. By these studies we found postoperatively a much higher level of intact immunoglobulins, particulary in cases of chronic otitis media associated with cholesteatoma. The blocking of the proteinases and the increase of the level of intact immunoglobulins combined with the reconstruction of physiological conditions in the chronically inflamed middle ear by a tympanoplasty lead to a stabilsation of the immunological and inhibitory system and create the prerequisites for a healing process in chronic otitis media. It is the purpose of further studies to learn about the capability of the split-products of the immunoglobulines to attach and to absorb antigens and toxins during a chronic inflammation in the middle ear.

Enzyme Inhibitors↗
PubMed1976

[The effect of ear surgery to the immunologic defense system of the middle ear during chronic otitis media (author's transl)].

Alpha-1-antitrypsin and alpha-2-macroglobuline are very important proteinase inhibitors for the healing process in chronic otitis media, because they can inhibit numerous bacterial and leukocytic proteinases: Alpha-2-macroglobuline can block the malignant proteinases of pseudomonas aeruginosa, staphylococcus aureus and proteus vulgaris. In 58 cases in the middle ear secretion was examined and the level of alpha-1-antitrypsin and alpha-2-macroglobulin investigated pre- and postoperatively. By these investigations we could demonstrate that the postoperative level of these two inhibitors is higher than preoperatively. In a couple of cases with cholesteatoma the postoperative concentration of alpha-2-macroglobuline was nearly three times higher than prior to the tympanoplasty. We believe that one of the causes for this high inhibitor level is the liberation of alpha-2-macroglobuline by injuring blood vessels during a tympanoplasty. It is our opinion that the increase of the inhibitor level in the postoperative phase is one of the prerequisites for the healing process in chronic otitis media.

Antibody Formation↗
PubMed1975

[Mucous membrane specific protease inhibitors in bronchial mucus in severe chronic obstructive bronchitis and in alpha 1-antitrypsin deficiency syndrome].

In the bronchial mucus of 40 patients with chronic obstructive airway diseases we measured proteolytic activities, the total protein concentrations, alpha1-antitrypsin, alpha1-antichymotrypsin, and the free and bound proteinase inhibitors together with the total proteinase inhibition against trypsin and chymotrypsin. Without exception we always found free proteinase inhibitors together with proteolytic activities. The free-to-bound inhibitor rate was approximately 1:1 alpha1-Antitrypsin and alpha1-antichymotrypsin was measured in sputum only in very low concentrations. One patient with alpha1-anti-trypsin deficiency had no alpha1-antitrypsin, but high concentrations of total proteinase inhibitor-free and bound being in the same relation - in his bronchial mucus. In the alveolar part of the lung, the humoral proteinase inhibitors were effective. In the bronchial part of the lung the specific mucosal inhibitors had the decided importance. The proteinase inhibition of the mucosa-specific inhibitors is probably of great importance for the pathogenesis of airway obstruction, while the humoral proteinase inhibitors are responsible for the pathogenesis of emphysema.

Adult↗
PubMed1975

The amino acid sequence of the double-headed proteinase inhibitor from canine submandibular glands, III. Sequencing studies.

Canine submandibular glands contain 3 polyvalent, double-headed proteinase inhibitors. The amino acid sequences of the two main inhibitors were determined. They differ only in the substitution of one Lys for a Glu residue. The inhibitor molecules are composed of two halves (domains), one antitryptic and one antichymotryptic. The two domains are covalently linked by 3 amino acid residues. The domains are structurally related to each other and to the sequenced monovalent secretory pancreatic trypsin inhibitors.

Amino Acid Sequence↗
PubMed1975

[Early recognition of a rejection crisis following kidney transplantation by determination of a low-molecular protease inhibitor in serum and urine].

The dynamic of the lowmolecular acid stable inhibitor in serum and urine was investigated in 10 patients with kidney transplants. The same was done with serum creatinin levels. In kidney transplantation changing serum levels and excretion of acid stable proteinase inhibitors early indicate the starting function of the kidney transplant. Rapid reduction of the inhibitors serum level and massive excretion are sign of the functioning of the kidney transplant even though creatinin levels remain elevated. An increasing inhibitor concentration in serum indicates the beginning of a rejection crisis. This is an easy check-up which takes only a few minutes.

Adolescent↗
PubMed1975

[The amino acid sequence of the double-headed protein proteinase inhibitor from dog submandibular glands, I. Structural homology to the pancreatic secretory trypsin inhibitors (author's transl)].

The primary structure of the broad specificity proteinase inhibitor from dog submandibular glands was elucidated. The inhibitor consists of a single polypeptide chain of 117 amino acids which is folded into two domains (heads) connected by a peptide of three amino acid residues. Both domains I and II show a clear structural homology to each other as well as to the single-headed pancreatic secretory trypsin inhibitors (Kazal type). The trypsin reactive site (-Cys-Pro-Arg-Leu-His-Glx-Pro-Ile-Cys-) is located in domain I and the chymotrypsin reactive center (-Cys-Thr-Met-Asp-Tyr-Asx-Arg-Pro-Leu-Tyr-Cys-) in domain II, cf. the Figure. The inhibitor is thus double-headed with two independent reactive sites. Whereas head I is responsible for the inhibition of trypsin and plasmin, head II is responsible for the inhibition of chymotrypsin, subtilisin, elastase and probably also Aspergillus oryzae protease and pronase. Remarkably, the structural homology exists also to the single-headed acrosin-trypsin inhibitors from seminal plasma[12] and the Japanese quail inhibitor composed of three domains[13].

Amino Acid Sequence↗
PubMed1975

[Identification of a methionine residue as the reactive site for chymotrypsin in the double-headed proteinase inhibitor from the canine submandibular gland (author's transl)].

The canine submandibular inhibitor is double-headed with two independent reactive sites. Whereas the trypsin-reactive center (-Ala-Cys-Pro-Arg26-Leu-His-) is located in domain I, the chymotrypsin-reactive site (-Met-Cys-Thr-Met78-Asp-Tyr-) is located in domain II. The presence of a methionine residue in this inhibition center is supported by the findings that nitration with tetranitromethane abolishes neither trypsin nor chymotrypsin inhibition, whereas after alkylation of the methione residues, only trypsin inhibition is retained. Remarkably, another inhibitor from microbial sources [10] which also contains a methionine residue in the presumed reactive site also inhibits subtilisin but not chymotrypsin (or trypsin).

Amino Acid Sequence↗
PubMed1975

[The inhibition of various bacterial proteinases with natural proteinase inhibitiors(author's transl)].

Proteus mirabilis, citrobacter intermedius, staphylococcus aureus haemolyticus and staphylococcus albus produce extracellualr proteinases with maximum activity at pH 7.8. These proteinases are inhibited practically completely by human and animal blood serum. This inhibitory activity of human serum is caused by alpha2-macroglobulin. Ovomucoid showed nearly the same inhibitory activity as alpha2-macroglobulin.

Animals↗
PubMed1975

[Exploration of parotid saliva proteins by means of one-and-two-dimensional immunelectrophoresis, immunodiffusion and discelectrophoresis (author's transl)].

The protein composition of human parotid saliva was explored by means of one- and two-dimensional immunelectrophoresis as well as by a modified Ouchterolony-technique and discelectrophoresis, where usually at least 14 components of parotid-saliva-proteins can be differentiated. According to the results of immunelectrophoresis and discelectrophoresis, the kind and number of protein components are interindividually constant, yet, there are great interindividual differences concerning the concentration of the single components.

Adolescent↗
PubMed1975

[Simultaneous determination of lysozyme and IgA-content in human parotid saliva, compared with flow-rate and totalprotein-secretion during rest and stimulation (author's transl)].

Parotid saliva was collected in 10-minutes-fractions during rest and stimulation from 66 healthy individuals. The time of collection was 80 minutes, in every sample flow-rate, total-protein-concentration, IgA- and Lysozyme-content were determined. According to sex and age of the individuals, the results obtained were classified in four groups. Stimulation produced characteristic changes in the flow-rates, which seemed to be correlated with the age of the persons. The total-protein-concentration of the single samples showed great differences; yet, regarding flow-rate and proteinconcentration together, the so calculated secretion of protein of every gland was almost the same. Secretion of IgA was dependent on age and sex: the secretion-rate was greater in females than in males. Besides, younger people had lower IgA-concentrations than older ones. On the other hand, lysozyme-secretion was reciprocal to IgA-secretion. The concentration of lysozyme was much higher in young persons compared with the older group. The clinical importance of this findings is discussed.

Adolescent↗
PubMed1975

[Metabolic enzymes in human nasal mucus under physiological and pathophysiological conditions of the mucous membrane (author's transl)].

In the human nasal mucus several enzymes of the intermediary metabolism are present. Due to secreted albumin the enzyme-levels are determined in different diseases of the upper respiratory tract. It is possible to differentiate viral rhinitis from bacterial or allergic or atrophic rhinitis by a significant increase of the activities of GOT, LDH and CPK.

Acid Phosphatase↗
PubMed1975

[Detection of split products of the immunoglobulins IgG, IgA and IgM during chronic otitis media (author's transl)].

Proteolytic enzymes such as pepsine or papaine are able to split IgG antibodies into large fragments in vitro. These immunoglobulin fragments (IgG, IgA, IgM) were now detected in vivo from the purulent secretions of cholesteatoma, chronic otitis media and radical mastoid cavities. During chronic otitis media the intact immunoglobulins are split due to the proteolytic activity of neutral proteinases. These fragments were qualitatively and quantitatively investigated by means of various immunological procedures. After the immunoelectrophoretic separation of the purulent middle-ear-secretions and after diffusion against anti-IgG-, anti-IgA- and anti-IgM- serum double precipitate lines could be observed especially in middle-ear-secretion with a bacterial flora of pseudomonas aeruginosa (pyocyanea) and of the proteus-providencia-group. This was the first proof of the presence of split products of the immunoglobulins. The exact demonstration of these split products could be carried out by gel-filtration and fractionation of the intact and split immunoglobulins. During chronic otitis media intact immunoglobulins are split by leucocytic and extracellular bacterial proteinases into fragments of different molecular weight. The most malignant extracellular proteinases with the greatest proteolytic activity against intact immunoglobulins are the bacterial proteinases of pseudomonas aeruginosa. These proteinases can not be inhibited by the other serum proteinaseinhibitors except for alpha-2-macroglobulin of the human blood serum. This inhibitor has a very high molecular weight so that we can not find it in a higher concentration in the middle-ear-secretion. We can liberate this inhibitor by injuring the blood vessels during a tympanoplasty. In this way we get an inhibitory effect against these proteinases and combined with an appropriate antibiotic therapy we can cure a chronic otitis media.

Exudates and Transudates↗