ABSTRACT
Familial hereditary ventricular hypertrophy (HCM) is classified as a genetically determined disease (autosomal dominant trait) characterized by generalized ventricular hypertrophy, specific heart sounds and echocardiography images, characteristic ECG changes. Sudden death occurs in some cases. Clinical data and laboratory findings in a family of twelve, in which three brothers (aged 17, 21 and 25) displayed typical features of hypertrophic cardiomyopathy, are presented. In addition to the HCM symptoms, all brothers displayed unique, characteristic phenotype: long upper and lower extremities, microcephaly and different in degree mental retardation. Echocardiography and Holter monitoring revealed types III and IV (according to Maron's classification) with complex ECG disturbances. In other members of the family the following changes were found: supra and ventricular arrhythmias appeared in the ECG of the mother (45 years old) in the forth decade of her life and ST disturbances ("silent ischaemia") in the ECG of the father (44 years old). Arrhythmias were present in the father's brother and sister, but without any clinical signs of HCM. Cytogenetic analysis was performed on the peripheral blood lymphocytes derived from the mother and all her sick sons--the karyotypes were normal. Additional cytogenetic studies detecting the presence of chromosome fra (16) were negative. Analyses of the HLA antigens were performed on 13 members of the three generations in the family. The HLA antigens of classes I-A, B and C were identified and results suggest some linkage between HCM and B12 (44) antigen. To our knowledge, the present study provides the first description of a family displaying simultaneously ventricular hypertrophy and a specific phenotype with mental retardation.
Subject(s)
Cardiomyopathy, Hypertrophic/diagnosis , Intellectual Disability/diagnosis , Adolescent , Adult , Cardiomyopathy, Hypertrophic/genetics , Cardiomyopathy, Hypertrophic/immunology , Echocardiography , Family , Female , Genetic Linkage , HLA Antigens/analysis , Humans , Intellectual Disability/genetics , Intellectual Disability/immunology , Male , Middle Aged , Pedigree , PhenotypeABSTRACT
Proteolytic activity of sea trout hatching liquid was examined towards casein and azocazein as a function of pH and temperature. The optimum pH for caseinolytic and azocaseinolytic activities were 9.4, and 9.0, respectively. At alkaline pH the enzyme was activated by low concentrations of Zn(2+) ions (10(-5) M). Maximum proteolytic activity of the hatching liquid was observed at 25°C. Temperatures exceeding 30°C caused a rapid reduction in enzyme activity. Proteolytic activity observed at 10°C was approximately 50% of that observed at 25°C. In general, a pseudo-Arrhenius plot indicated a Q10 of 1.6 between 6 and 25°C.
Subject(s)
Metalloendopeptidases/metabolism , Peptide Hydrolases/metabolism , Salmonidae/embryology , Animals , Chemical Phenomena , Chemistry, Physical , Environment , Hydrogen-Ion Concentration , Metalloendopeptidases/physiology , Osmolar Concentration , Peptide Hydrolases/physiology , Salmonidae/metabolism , Salmonidae/physiology , TemperatureABSTRACT
A specific proteinase (chorionase) was isolated from the hatching liquid, obtained by electric stimulation of the hatching glands in Coregonus peled embryos. The enzymatic preparation was electrophoretically homogeneous, and showed proteolytic activity towards the egg membranes. Ions of Na+ at concentration from 10(-5) to 10(-4) M activated the chorionase of C. peled, whereas ions of K+, Na+, Ca2+ and Mg2+ at concentrations above 10(-4) M inhibited the enzyme. Addition of EDTA to the incubation mixture significantly reduced the enzyme activity. The chorionase was not inhibited by the natural soybean trypsin inhibitor.
Subject(s)
Endopeptidases/metabolism , Metalloendopeptidases/metabolism , Protease Inhibitors/pharmacology , Animals , Calcium/pharmacology , Chorion , Electric Stimulation , Embryo, Nonmammalian , Fishes , Kinetics , Magnesium/pharmacology , Metalloendopeptidases/isolation & purification , Potassium/pharmacology , Sodium/pharmacologyABSTRACT
Carnosinase of swine uterus reacts strongly to Mn2+ ions with an increase of the activity: in the presence of 0.25 MnCl2 the activity increases over 5-fold, while at 1 and 2 mM--the increase is 8- and 10-fold respectively. The enzyme is characterized by low stability during storage, especially in the presence of manganese ions. Kinetic properties of uterus carnosinase change depending on a phase of the oestrous cycle of the sow. In the peak luteal phase (5th-13th day of the cycle) Km values were twice as high as in the follicular phase (zero day--beginning of the rut, and 19th day--preoestrus). Two molecular forms of carnosinase were found in the extracts from uterus in the luteal phase of the oestrous cycle, analysed with the method of Sephadex G-100 gel filtration. These were A and B forms, with predominating content of the latter form. This form was characterised by a 2-fold higher Km value compared to the form A.
