Glycosaminoglycan metabolism in atrophied skin from a patient treated with long-term administration of corticosteroids.
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Biomedical subjects
Publications and source records attributed to H Hatano.
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To elucidate the mechanism by which propranolol reportedly affects portal hemodynamics, we investigated the effect of propranolol on systemic and splanchnic hemodynamics in 15 patients with portal hypertension and esophageal varices by simultaneous catheterization of the portal vein and the right hepatic vein and measurement of portal venous flow using an ultrasound doppler system. Infusion of 5 mg of propranolol significantly decreased pulse rate (-12.6%), cardiac output (-24.5%), portal venous flow (-22.3%), portal venous pressure (-13.3%), and gradient between portal venous pressure and free hepatic venous pressure (-24.8%). Thus, propranolol seems to decrease portal venous pressure by reducing portal venous flow, at least in part, as a result of reduction of cardiac output due to its beta 1 adrenergic receptor blocking action.
Effects of two histamine H2 receptor antagonists, cimetidine and ranitidine, on systemic and splanchnic hemodynamics were studied in patients with chronic liver disease by simultaneous catheterization of the portal vein and the right hepatic vein and measurement of portal venous flow using the ultrasound doppler system or cineangiography. Neither infusion of 200 mg of cimetidine nor 50 mg of ranitidine reduced cardiac output, portal venous pressure, the gradient between wedged hepatic venous pressure and free hepatic venous pressure, hepatic blood flow, and portal venous flow. It is unlikely that histamine is an important modulator of flow via the H2 receptor.
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A 46-yr-old man with cirrhosis presented with mental confusion, headache, and nausea. Colloid liver scintigraphy showed a defect in the hilar area, and portograms after superior mesenteric arteriography demonstrated varicose veins in the same area. Computed tomography revealed a sausage-shaped low-density channel connecting the hepatic hilum and the inferior vena cava, and bolus injection contrast enhancement demonstrated transit of contrast medium from the portal vein directly into the inferior vena cava through this channel. Real-time ultrasound demonstrated a large conduit contiguous from the portal vein to the inferior vena cava through and behind the liver. The catheter introduced into the inferior vena cava opacified a large opening of this shunt below the right and left hepatic vein openings. Measurements of blood pressure, ammonia, and PaO2 clearly indicated that portal vein blood was being shunted through this channel. These findings are highly suggestive of a portosystemic shunt through a patent ductus venosus.
Normal human skin was sliced into five horizontal layers and distribution of type I and type III collagens, glycosaminoglycans, and non-collagenous glycoprotein(s) among the five layers was analyzed. No remarkable differences in the relative contents of type I and type III collagens and noncollagenous glycoprotein(s) were detected among the five layers. However, glycosaminoglycan content was higher in the upper layers than in the lower and the ratio of hyaluronic acid to dermatan sulfate was also higher in the upper layers. These results are compared and discussed with our previous data on calf skin.
Complement-fixing intercellular antibodies were detected in 10 of 17 sera from untreated pemphigus patients. The role of complement in the organ culture system was investigated using these sera. Ten sera possessing complement-fixing intercellular antibodies showed IgG binding to the intercellular substance in the organ-cultured skin and acantholysis-like changes were observed in eight cases. C3 deposition was not seen in any case. However, after treatment of the sections of cultured skin with fresh normal human serum, complement fixation of the intercellular substance by bound IgG was revealed in all the ten cases. No significant differences in the grade of acantholysis-like changes between the complement-depleted system and the complement-supplied system were observed. Complement does not appear to be necessary in the acantholytic process in the in vitro organ culture system, even though we considered the presence of complement-fixing intercellular antibodies.
High resolution 1H NMR spectroscopy at 360 and 400 MHZ was used to study the dynamic states of the three methionyl residues (Met 70, 73, and 103) of Streptomyces subtilisin inhibitor (SSI) in a neutral aqueous (2H2O) solution. Chemical modification and nuclear Overhauser effect studies show that one of the methyl groups exists in the interior of the protein and is surrounded by phenylalanyl residues. With reference to the crystal structure, this methyl group is assignable to that of Met 103 in the hydrophobic core. The other two methionyl residues (Met 70 and 73) are equally susceptible to chemical modifications, but their methyl signals are affected in a different manner by the alpha-chymotrypsin-cleavage of the peptide bond between Met 73 and Val 74 at the reactive site. The observed linewidths of the methyl groups are consistent with the assumption that the whole side-chain of both Met 70 and 73 are already undergoing rapid internal motions at 20 degrees C, whereas for Met 103 only the rotation of the methyl group is allowed, even above approximately 40 degrees C. The high-field shift of the methyl proton resonance of Met 103 by about 0.3 ppm is attributable to the ring current effect from the surrounding phenylalanyl residues. This shift is invariant in the temperature range of 40-90 degrees C, showing that the native environment of the methyl group of Met 103 persists up to 90 degrees C at neutral pH. Destruction of the native methionyl environments occurs only above 90 degrees C, and the rate of conversion between the native and the denatured conformations is slower than 10 s-1. When SSI is mixed with subtilisin BPN' in a one-to-one molar ratio, at least one of the methyl signals of Met 70 and 73 is completely broadened, showing that the side-chain of this methionine is directly involved in the interaction with the enzyme.
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