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Biomedical subjects

M Sonenberg

Publications and source records attributed to M Sonenberg.

At least 73 records · Page 4Linked to original sources
PubMed1975

Beneficial effect of human growth hormone on stress ulcers.

Human growth hormone was effective in healing erosions and controlling hemorrhage in six of eight patients with stress ulcers. This approach was based on known beneficial effects of growth hormone on nucleic acid and protein synthesis, demonstration of deleterious effects of stress on nucleic acid and protein synthesis, and demonstrated protective effects of growth hormone on animals subjected to stress. Bleeding cessation within 24 hours of its administration in two patients suggests the possible role of additional mechanisms involved in hemostasis. In a comparable group of eight patients with stress ulcer hemorrhage not treated with this agent, six died with continued bleeding. This high mortality represented the usual outcome in our patients with stress ulcer hemorrhage. These observations need to be extended to additional patients with stress ulcers in a larger randomized study.

Blood Chemical Analysis↗
PubMed1971

Metabolic effects of the major component of bovine growth hormone.

Bovine growth hormone, subjected to DEAE-cellulose chromatography, yielded one major and several minor components. The various chromatographic fractions of bovine growth hormone were compared with the parent material for their ability to promote hormone effects in vivo and in vitro. The major component of bovine growth hormone was homogeneous by acrylamide-gel electrophoresis, rechromatography and sedimentation equilibrium. Its amino acid composition was similar to that of the parent hormone. The major component possessed all the qualitative activities present in the original heterogeneous material, including promotion of acute hypoglycaemia and hypolipaemia. In studies in vitro in adipose-tissue segments the major component of the hormone increased entry of glucose and its oxidation to CO(2), conversion of glucose into glyceride glycerol, release of glycerol and incorporation of histidine into adiposetissue protein. Other chromatographic fractions of bovine growth hormone were not homogeneous and possessed some but not all of the metabolic activities attributed to the hormone preparations or its major component. Thus, the metabolic effects obtained with bovine growth-hormone preparations in vivo and in vitro can be obtained with the major homogeneous component of the hormone. This observation precludes the possibility that the metabolic effects obtained with bovine growth-hormone preparations are due to the combined actions of a number of components found therein.

Acrylates↗
PubMed1971

Interaction of human growth hormone and human erythrocyte membranes studies by intrinsic fluorescence.

The intrinsic fluorescence of human erythrocyte membranes excited by unpolarized and polarized light has been studied with and without the addition of human growth hormone. The peak emission intensity of the membranes appeared at 332 nm, with a distinct shoulder at about 303 nm. Excitation spectra contained two peaks, at 282 and 225 nm. Fluorescence polarization was maximal (about 0.4) near 295 nm and decreased to approximately 0.18 near 225 nm. In the presence of 1 x 10(-15) M human growth hormone, or 70 molecules per membrane (1.45 x 10(-6) cm(2)), there was about a 20% decrease in peak membrane fluorescence. This occurred maximally with excitation at 282 and 225 nm, with little difference with excitation at 295 nm. Human growth hormone also decreased the fluorescence polarization from 0.34 to 0.25. The growth hormone effect was optimal at 37 degrees C and pH 7.4. No effect was noted at pH 6.0 or 8.0. Bovine growth hormone or bovine serum albumin was without effect. A biologically active fragment from a tryptic digest of bovine growth hormone produced effects on membrane fluorescence similar to human growth hormone. The data are consistent with the proposition that human growth hormone, by some cooperative mechanism, produces a conformational change in the membrane proteins with associated depolarization of fluorescence.

Erythrocytes↗