Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.14.16.2 (tyrosine hydroxylase)
 14,760 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sensory neurons of adult rat lumbar dorsal root ganglia were labeled in cryostat sections with antisera against tyrosine hydroxylase (TH), substance P (SP), and somatostatin (SOM), and with a monoclonal antibody (RT97) that labels the 145- and 200-kilodalton (kd) subunits of neurofilaments. These neurons were also histochemically stained for fluoride-resistant acid phosphatase (FRAP), and the size and distribution of each population were determined. In addition, the double-label immunoperoxidase technique of Sternberger and Joseph (Sternberger, L.A., and S.A. Joseph (1979) J. Histochem. Cytochem. 27: 1424-1429) was employed to determine whether these antibodies labeled distinct or overlapping populations of neurons. The results indicate that the dopaminergic (TH+) cells constitute a separate population from the SP+ and SOM+ neurons and that the size distributions of the SP+, SOM+, TH+, and FRAP+ cells are all different despite the fact that all of these subpopulations are part of the "small dark" subpopulation as indicated by their size and by the fact that they are RT97-. RT97 is a putative marker for the "large light" population (Anderton, B., H.B. Coakham, J. A. Garson, A.A. Harper, and S.N. Lawson (1982) J. Physiol. (Lond.) 334: 97-98P). Furthermore, the distribution data indicate that all of the "small dark" cell subpopulations are not evenly distributed within the ganglion, and the staining with RT97 and with another antibody which recognizes the 68-kd neurofilament subunit indicates heterogeneity among the "large light" population. These results are discussed in terms of the significance of the "small dark"-"large light" classification.
 ...
PMID:An immunohistochemical and quantitative examination of dorsal root ganglion neuronal subpopulations. 241 May 79

We reported recently that the gene that encodes tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of catecholamines, is regulated by hypoxia in the dopaminergic cells of the mammalian carotid body (Czyzyk-Krzeska, M. F., Bayliss, D. A., Lawson, E. E. & Millhorn, D. E. (1992) J. Neurochem. 58, 1538-1546) and in pheochromocytoma (PC12) cells (Czyzyk-Krzeska, M. F., Furnari, B. A., Lawson, E. E. & Millhorn, D. E. (1994) J. Biol. Chem. 269, 760-764). Regulation of this gene during low O2 conditions occurs at both the level of transcription and RNA stability. Increased transcription during hypoxia is regulated by a region of the proximal promoter that extends from -284 to + 27 bases, relative to transcription start site. The present study was undertaken to further characterize the sequences that confer O2 responsiveness of the TH gene and to identify hypoxia-induced protein interactions with these sequences. Results from chloramphenicol acetyltransferase assays identified a region between bases -284 and -150 that contains the essential sequences for O2 regulation. This region contains a number of regulatory elements including AP1, AP2, and HIF-1. Gel shift assays revealed enhanced protein interactions at the AP1 and HIF-1 elements of the native gene. Further investigations using supershift and shift-Western analysis showed that c-Fos and JunB bind to the AP1 element during hypoxia and that these protein levels are stimulated by hypoxia. Mutation of the AP1 sequence prevented stimulation of transcription of the TH-chloramphenicol acetyltransferase reporter gene by hypoxia.
 ...
PMID:Hypoxia-induced protein binding to O2-responsive sequences on the tyrosine hydroxylase gene. 755 51