PubMed · 4875821
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K Koto. 1967-11-10. [Adrenocortical estrogens].. https://pubmed.ncbi.nlm.nih.gov/4875821/
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The tyrosine hydroxylase (TH) gene is expressed exclusively in cells and neurons that synthesize and release L-DOPA or catecholamines. To further understand the molecular genetic mechanisms that regulate this cell-type specific expression, a chimeric gene was prepared by linking 3.6 kb of the 5' flanking DNA of the mouse TH gene, including the +1 initiation site for transcription, to an E. coli beta-galactosidase reporter. This fusion gene (TH3.6LAC) was used to prepare transgenic mice, and the tissue distribution of expression of TH3.6LAC was determined by the measurement of beta-galactosidase enzymatic activity and/or by the detection of the transcription product of the chimeric gene by RNase protection assays. In two separate founder lines, TH3.6LAC expression was observed in every region of the brain that was examined, including the olfactory bulb, brainstem, cerebellum, diencephalon, hippocampus, striatum, and cerebral cortex. Expression of TH3.6LAC was observed in the adrenal gland of one founder line but not in the other. TH3.6LAC activation was undetectable in peripheral organs that were examined, including the liver, heart, salivary gland, kidney, lung, and spleen. Although 3.6 kb of the 5' regulatory DNA of the mouse TH gene is sufficient to activate the TH fusion gene in the mouse, it is not enough to restrict its expression to catecholaminergic cells.
The tissue distribution of neurotrophin-3 (NT-3) was investigated in rats at 1 month of age using a newly established, sensitive two-site enzyme immunoassay system for NT-3, as well as the immunocytochemical localization of this protein. The immunoassay for NT-3 enabled us to quantify NT-3 at levels > 3 pg per assay. In the rat brain, NT-3 was detectable only in the olfactory bulb (0.54 ng/g wet weight), cerebellum (0.71 ng/g), septum (0.91 ng/g), and hippocampus (6.3 ng/g). By contrast, NT-3 was widely distributed in peripheral tissues. Appreciable levels of NT-3 were also found in the thymus (31 ng/g), heart (38 ng/g), diaphragm (21 ng/g), liver (45 ng/g), pancreas (892 ng/g), spleen (133 ng/g), kidney (40 ng/g), and adrenal gland (46 ng/g). An antibody specific for NT-3 bound to pyramidal cells in the CA2-CA4 regions of the hippocampus, to A cells in the islets of Langerhans in the pancreas, to unidentified cells in the red pulp of the spleen, to liver cells, and to muscle fibers in the diaphragm from rats at 1 month of age. Molecular masses of NT-3-immunoreactive proteins in the hippocampus and pancreas were 14 and 12 kDa, respectively. Thus, in rats, NT-3 was detected in restricted regions of the brain and in the visceral targets of the nodose ganglia at high concentrations. Our present results suggest that NT-3 not only functions as a classical target-derived neurotrophic factor but also can play other roles.
To assess the ability of proteins of the thrombospondin family to inhibit angiogenesis, recombinant murine thrombospondin-2, bovine thrombospondin-2/CISP and thrombospondin-5/COMP were purified and tested for ability to block the migration of capillary endothelial cells towards a variety of inducers and to inhibit neovascularization induced in the rat cornea. Both preparations of thrombospondin-2 were active inhibitors in vitro and in vivo whereas thrombospondin-5/COMP was inactive. These results define thrombospondin-2 as a newly identified naturally occurring inhibitor of angiogenesis and suggest that the properdin-like type 1 modules that it shares with antiangiogenic thrombospondin-1 and are missing in thrombospondin-5/COMP could contribute to this activity.