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Biomedical subjects

G Bretzel

Publications and source records attributed to G Bretzel.

At least 37 records · Page 2Linked to original sources

[Leprosy--current aspects of a disease from biblical times].

95% of individuals who come in contact with M. leprae do not develop an overt disease. It begins as an indeterminate form that may undergo spontaneous cure or may progress to different forms of leprosy (TT, BT, unstable form of BB, BL, or LL). The clinical form of the disease correlates with the T cell mediated immune response rather than to the direct damage caused by the bacilli. The lack of cellular immunity in lepromatous patients relates specifically to M. leprae. Current aspects of etiology, transmission, epidemiology, classification, clinical features, immunopathology, chemotherapy, treatment of reactions, immunotherapy and vaccination are elucidated and discussed.

Bible↗

Modulation of the spontaneous G2 phase blockage in Fanconi anemia cells by caffeine: differences from cells arrested by X-irradiation.

The effect of caffeine on the endogenous G2 phase cell cycle blockage of Fanconi anemia (FA) cells was compared with the effect of caffeine on the G2 phase blockage induced in control cells by X-irradiation. The G2 phase accumulations in FA cells could be completely resolved by exposure to 1.5 mM caffeine. This was also observed in three brothers with endogenous G2 phase blockage due to unusual BrdU sensitivity. In contrast, G2 phase blockage induced by X-irradiation was only partially resolved by exposure to caffeine. The rescued G2 phase cells from FA patients were arrested within the following G1 phase compartments. This was not seen in X-irradiated cells from control donors. These results point towards a different nature and/or repair mechanism of the endogenous G2 phase lesion in FA cells compared to that induced by X-irradiation in control cells.

Caffeine↗

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↗

[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 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↗

[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↗

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↗

[Simultaneous estimation of flow rates, electrolyte and proteinconcentration and discelectrophoretic separation of fractionated human parotid saliva(author's transl)].

Fractionated human parotid saliva from normal persons was separated by column-acryamid-gel discelectrophoresis. Flow rates, electrolyte-concentrations and total protein content of the stimulated and unstimulated parotid-secretion were determined simultaneously. Significant patterns of proteincomposition were found for stimulated and unstimulated parotid saliva. Most typical changes of protein bands were found in the anodal near gel region, within a group of four bands, called by us f, g, h and i. In the cathodal near gel region as well significant changes in the bands a, b, c and d were found; by glycoprotein staining these bands showed good staining.

Adolescent↗

[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↗