Biomedical subjects

A Bateman

Publications and source records attributed to A Bateman.

21 records · Page 2Linked to original sources

PubMed1977

Effects of erythrocyte lysate and erythrocyte-conditioned medium on erythroid cells in vitro.

A component of erythrocyte-conditioned medium has been shown to inhibit the incorporation of tritiated thymidine into erythroblasts from fetal mouse liver, proliferating in vitro. This component, however, has no detectable effect on the growth of colonies of erythroid cells stimulated to grow in viscous culture media by the hormone erythropoietin. Erythrocyte lysate and preparations of haemoglobin derived from the lysate increase the number and size of the colonies growing in vitro. Results are discussed in terms of possible control mechanisms in erythropoiesis.

Animals↗

PubMedDate not supplied

Non-ACTH components of adult human pituitary extracts which stimulate adrenal steroidogenesis.

Human pituitary extracts were fractionated by chromatography on Sephadex G-50 and G-25, and low molecular weight components were further separated by HPLC. Eluates were tested for their activity in stimulating steroidogenesis in suspensions of rat adrenal capsule (largely zona glomerulosa) and inner zone (fasciculata/reticularis) cells. Several biologically active components were reproducibly isolated. Three stimulated glomerulosa cells specifically, and one of these was tentatively identified by HPLC and RIA criteria as desacetyl-alpha-MSH. Alpha-MSH was not detected. One component stimulated both cell types but two others stimulated inner zone cells, and were without effect on glomerulosa cells: this type of activity has not previously been described, and is not associated with any peptide derived from pro-opiomelanocortin which has so far been tested. The data suggest that, in addition to corticotrophin, further pituitary peptides may be involved in the control of adrenocortical function.

Adrenal Glands↗

PubMedDate not supplied

The levels and biologic action of the human neutrophil granule peptide HP-1 in lung tumors.

HP-1 is the most abundant human representative of a recently discovered class of neutrophil cystine- and arginine-rich peptides. These peptides have many potentially regulatory activities expressed at nanomolar concentrations. To establish the levels of HP-1 that can accumulate in human lung tumors and nondiseased lung fragments, tissues were extracted for their peptide content. The extracts were purified on reverse phase HPLC, and HP-1 and related peptides were identified by sequence analysis and their concentrations in the tissue quantitated by amino acid analysis. Immunohistochemistry was performed and strongly suggests that HP-1 is confined to granulocytes under most circumstances, and indicates that the levels of HP-1 measured in the tumors reflect the levels obtained when solid tissue is infiltrated by neutrophils. The maximum observed levels were 26 nanomoles per gram wet weight of tissue. Attempts were then made to correlate this level to the cytotoxic potential of HP-1 by performing in vitro cytotoxicity dose-response curves on several cell lines. Most cells were killed at between 1 and 8 microM, and the response depended on the growth conditions of the cells. The levels of HP-1 that accumulate in tumors can exceed the in vitro cytolytic concentrations. The levels are also considerably in excess of those required to exert in vitro regulatory actions.

Amino Acid Sequence↗