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Biomedical subjects

E Heidemann

Publications and source records attributed to E Heidemann.

At least 55 records · Page 3Linked to original sources
PubMed1981

[Alcohol induced changes in hemopoiesis (author's transl)].

In a prospective trial with 120 chronic alcoholics (July, 1978 to January, 1980) on admission the following haematological values significantly different from those of the normal population were found: elevated erythrocyte mean corpuscular volume (64%), increased mean corpuscular hemoglobin (32%), thrombocytopenia (48%), increased percentage of bone marrow sideroblasts (35%), decreased percentage of sideroblasts (37%), megaloblastic bone marrow changes (55%) including nuclear abnormalities (32%), and vacuolization in red cell (20%) and white cell (16%) precursors. These changes were independent of liver cirrhosis with hypersplenism (increased mean corpuscular volume in 52% of the patients who did not have liver cirrhosis, increased mean corpuscular volume in 76% of the patients who were cirrhotic but not suffering from major bleeding). Platelets returned to normal values within 6 days of discontinuation of alcohol ingestion. In respect to iron metabolism we found the following changes: decreased serum iron concentration (32%), increased iron concentration (42%), increased total iron binding capacity (54%), increased ferritin (41%), decreased transferrin (20%). In contrast to data from the Anglo-American literature, serum folate concentrations were mostly normal in our patients (87%). This may be due to different eating and drinking habits. The percentage of bone marrow sideroblasts was also lower in our patients than those described in the literature mentioned above. The changes in maturation are likely to be caused partially by a toxic effect of alcohol on nuclear metabolism of bone marrow cells.

Adult↗
PubMed1980

[Humoral factors in the regulation of cell proliferation in haematopoiesis. II. Erythropoiesis, megakaryopoiesis, multipotent stem cell (author's transl)].

Diffusible factors probably play an important role in the control of cell proliferation during haematopoiesis. Several stimulators of erythropoiesis including erythropoietin are to be found in sera. Inhibitors are found in erythrocyte supernatants, in the urin of newborn children, and in plasma of patients with renal insufficiency. Stimulators of megakaryopoiesis have been shown to be present in conditioned media of lymphoid cells and bone marrow cells. Inhibitors have been detected in various sera. Proliferation of multipotent stem cells is probably also regulated by a humoral mechanism. Stimulators and inhibitors are present in bone marrow extracts. Clinical relevance of these factors is discussed.

Cell Division↗
PubMed1980

[Humoral factors in the regulation of cell proliferation in haematopoiesis. I. Granulopoiesis and lymphopoiesis (author's transl)].

Humoral Factors obviously play an important role in the maintenance of the steady state in haematopoiesis. There has been work on stimulators and inhibitors for several years. Colony-stimulating factor is the best characterized chemically and biologically. Interest in more or less cell-line-specific stimulators and inhibitors of lymphopoiesis is now growing. Various tissue extracts and cell culture supernatants have been partially purified and characterized biologically and chemically. Monocytes, producing stimulators and inhibitors, have a central function in the regulation of cell proliferation in haematopoiesis. Experiments performed in vitro can help better to understand data so far difficult to explain regarding patients with disturbed haematopoiesis. The in vivo relevance of these experiments, however, remains unclear.

Alpha-Globulins↗
PubMed1979

[Further purification of a tissue specific inhibitor in lymphopoiesis (lymphocyte chalone?) (author's transl)].

A partially purified calf spleen extract, which exhibits the properties of a lymphocyte chalone (tissue-specific, species non-specific, non-toxic and reversible acting, endogenous inhibitor of cell proliferation) as concerning biological activities, has been described earlier. This fraction has been further purified by ion exchange chromatography with DEAE-Sephacel to a 10,000-fold purification. The most active fraction inhibited 3H-thymidine incorporation into phytohemagglutinin- or pokeweed-mitogen-stimulated lymphocytes by 86% resp. 70%, when given in a concentration of 100 ng/ml. Ehrlich-ascites-cells were not inhibited by the same concentration. The inhibiting activity is compared to other published lymphocyte inhibitors.

Animals↗
PubMed1979

Tissue-specific inhibitor of lymphocyte proliferation extracted and purified from calf spleen. Biological and chemical properties.

A partly purified calf spleen extract which inhibits lymphocyte proliferation in a tissue-specific, species-nonspecific, nontoxic, and reversible way, and may thus contain a chalone-like activity, has been further characterized. Our results show that the inhibitor works in G1-phase. The activity is resistant to heat, trypsin- and ribonuclease-treatment. It appears to be an acidic molecule and it does not appear to contain ribonucleic acid. These properties are compared to the characteristics which have been described for tissue-specific inhibitors of lymphocyte proliferation by other authors.

Animals↗
PubMed1976

[Tissue specific inhibition of lymphocyte proliferation by spleen extract (lymphocyte chalone) (author's transl)].

Aqueous spleen extracts were purified using acetone precipitation, membrane filtration, affinity chromatography, and dialysis. These extracts were able to inhibit thymidine incorporation into lymphoid cells (MKT-CH and PHA-stimulated lymphocyte cultures). They did not influence non lymphoid tissue (melanoma cells Mel Ei 78 and Ehrlich ascites cells). The inhibition was reversible and the purified extracts were not cytotoxic. The extracts correspond to a chalone. Their importance for prevention of graft versus host reaction and for treatment of lymphoproliferative diseases is discussed.

Animals↗
PubMed1976

Dityrosine in collagen.

Dityrosine was formed by the action of peracetic acid and sodium peroxide on soluble collagens. Dityrosine was also detected in native insoluble collagen, but only from old animals. Dityrosine was identified by amino acid analysis, fluorescence absorption and mass spectra.

Amino Acids↗