Localization of the prostaglandin F2 alpha receptor in rat tissues

The localization of the prostaglandin F_2α (FP) receptor was examined in rat tissues by immunohistochemistry and in situ hybridization. Immunohistochemistry on paraffin sections was performed with a rabbit polyclonal antiserum raised against a synthetic peptide derived from the rat FP receptor sequence. In situ hybridization on cryosections was done with ³⁵S-labelled rat FP receptor antisense and sense riboprobes. The most intense FP receptor-like immunoreactivity was observed in granulosa luteal cells, muscle and epithelial cells, e.g. cardiac, skeletal and smooth muscle, and hepatocytes. Weaker immunoreactivity was found in connective tissue fibroblasts. In the eye, intense immunostaining was associated with the corneal and conjunctival epithelium and moderate staining with the ciliary body, retina, iris and connective tissues. In situ hybridization generally confirmed the results. The riboprobe hybridized weakly with the heart, skeletal muscle, uterus, liver, lung and corpus luteum. Thus, the prostaglandin FP receptor was found to be widely distributed in rat tissues.     

Glycine oxidation in mitochondria isolated from light grown and etiolated plant tissue

Mitochondria were isolated from light grown and dark grown monocotyledonous (wheat- Triticum aestivum and barley- Hordeum vulgare ) and dicotyledonous (pea- Pisum sativum ) plants and their capacity to oxidize glycine was measured. In all of the studied plant species the rate of mitochondrial glycine oxidation was high in light grown leaves. Glycine oxidation in mitochondria from etiolated leaves was also very substantial; the rate of glycine oxidation relative to the oxidation of other substrates was about half as compared to green tissue. In etiolated non-photosynthetic tissues the relative glycine oxidation was only ca 20% of that measured in green leaves. The effect of light on the development of glycine oxidation capacity was studied using etiolated barley which was transferred to light for 6 to 24 h. During this time the rate of glycine oxidation as compared to the oxidation of NADH and malate increased, approaching the ratio observed in light grown leaves. It is concluded that the synthesis of proteins involved in glycine oxidation is regulated both in a light dependent and in a tissue specific manner. Monocotyledonous plants should be very useful for further studies of this aspect due to the relatively small developmental difference between etiolated and light grown leaf tissue.