[Varicose veins of lower--how to recognize and treat]. / Zylaki konczyn dolnych--jak rozpoznac i leczyc.

Varicose veins of lower limbs are the most common symptom of chronic venous disorders. They are known for medicine since the Hippocrates time (460-375b.C.), but they were not treated as a serious problem for many years. At present century varicose veins are considered to be not only an esthetic problem, but also a social problem. Scientists from the around world still try to find the best way to treat them. In spite of development the phlebology as a separate science, patients very often don't know where they should ask for help. Usually they are treated by physicians, general practitioners or surgeons. That's why physicians should know very well what to do with patients who suffer from symptoms of chronic venous insufficiency. That's very important also to learn patients, especially with risk factors, how to changed bad habits which promote to development of venous insufficiency and varicose veins. Patients should know how to decrease symptoms of this disease and treat them or how to prevent serious complications.

[Antiheparin activity of the aneurysm wall and parietal thrombus and blood plasma of patients with aortic aneurysm]. / Aktywnosc antyheparynowa sciany i skrzepliny przysciennej tetniaka oraz osocza krwi chorych z tetniakiem aorty.

Aneurysm dilatation is filled by parietal thrombus. Its magnitude is determined by the ratio of coagulative to anticoagulative activities above all. The aim of the study was to assess antiheparin activity, contents of heparin neutralizing chemical compounds and glycosaminoglycans with anticoagulative activity as well in the aneurysm wall, parietal thrombus filling the aneurysm dilatation and blood plasma/blood serum of patients with aortic aneurysm. The studied material consisted of aneurysm walls and parietal thrombi extracts, as well as of blood plasma/serum of patients with aortic aneurysm. Extracts of normal aorta from organ donors and blood plasma/serum of healthy subjects were the control material. Antiheparin and antithrombin III activities, as well as contents of heparin neutralizing compounds and heparin-like acting glycosaminoglycans were evaluated in the investigated material with chemical methods. The aneurysm wall, parietal thrombus filling the aneurysm dilatation and blood plasma of patients with aortic aneurysm show high antiheparin activity and increased content of heparin neutralizing compounds. However differences in glycosaminoglycans content were not demonstrated. That can predispose to formation and enlargement of parietal thrombus in aneurysm dilatation.

[Lysosomal carboxypeptidase A]. / Lizosomalna karboksypeptydaza A.

Lysosomal carboxypeptidase A (cathepsin A) is synthetized in the form of preproenzyme, which undergoes to active enzyme as a result of post-translational modification. It splits off C-terminal amino acid residues from peptides and proteins and synergizes with other proteases in degradation of cellular proteins in lysosomes. Lysosomal carboxypeptidase A has an effect on peptide hormones and peptides of biological activity of tissues and body fluids as well. It forms complexes with some glycosidases that protects them against proteolytic degradation. Deficiency of this enzyme induces storage diseases. Lysosomal carboxypeptidase A as multifunctional enzyme plays an important regulatory role in organismal metabolism.

Thyroid volume and hormone response in the early kidney transplants.

BACKGROUND: Thyroid hormones could affect renal function, and conversely renal function disturbances may affect thyroid function. Disturbances of the thyroid hormone concentration are often connected with thyroid gland enlargement. The aim of study was to estimate the function and morphology of the thyroid and kidney graft after kidney transplantation. As the indicator of thyroid and renal function we have used thyroid gland volume, plasma concentration of T3, reverse rT3, creatinine concentration, and renal arteries RI. MATERIAL/METHODS: Studied group included 17 individuals after kidney transplantation, with stabile graft function. The control group included 18 individuals after various surgical procedures. The estimated parameters were: thyroid volume, renal arteries resistive index, concentrations of creatinine,T3 and rT3.The parameters were controlled before transplantation (surgery), the day after, and at 3rd, 6th and 10th day after surgery. RESULTS: All patients, before and after surgical procedure, were clinically euthyroid. Mean creatinine concentration showed tendency to diminish. Statistical analysis revealed positive correlation between Delta concentration of creatinine and Delta volume of thyroid (R Spearman=0.46, p=0.05). Till the 6th day after transplantation T3 concentration diminished, and at the 10th day presented tendency to rise. We found negative correlation between T3 concentration and renal arteries RI. The rT3 concentration during 10 days after transplantation was above the reference level. CONCLUSIONS: The FT3 level and thyroid volume correlates with kidney transplant function. The supplementary thyroid hormones administration should be considered before and after renal transplantation.

Effect of heavy metal cations on the activity of cathepsin D (in vitro study).

We studied the effect of heavy metal cations: Fe²âº, Cu²âº, Zn²âº, Cd²âº, Hg²âº, Pb²âº on the activity of cathepsin D in human aorta homogenate and blood serum. The concentration of cations was 1 mmol/l. Hemoglobin was the cathepsin D substrate. The activity of cathepsin D was determined at pH 3.5. Only Hg²âº cations inhibit the activity of cathepsin D. Cations Hg²âº damage lysosomes and release cathepsin D from these organelles.

Cathepsin E (EC 3.4.23.34)--a review.

Cathepsin E belongs to the third class of enzymes - hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that of cathepsin D. In a human organism, cathepsin E occurs in: erythrocytes, thymus, dendritic cells, epithelial M cells, microglia cells, Langerhans cells, lymphocytes, epithelium of gastrointestinal tract, urinary bladder, lungs, osteoclasts, spleen and lymphatic nodes. In human cells, loci of the gene of pre-procathepsin E are located on chromosome 1 in the region 1231-32. The catalytic site of cathepsin E is two residues of aspartic acid - Asp96 and Asn281, occurring in amino acid triads with sequences DTG96-98 and DTG281-283. To date, no particular role of cathepsin E in the metabolism of proteins in normal tissues has been found. However, it is known that there are many documented pathological conditions in which overexpression of cathepsin E occurs.