22-Kilodalton (kDa) protein cDNA clones were isolated from a rat prostatic library. Nucleotide sequence analysis revealed three different cDNA sequences encoding two somewhat different open reading frames of 176 amino acids. The N-terminal 24 amino acids of these sequences show the typical characteristics of signal peptides of secretory proteins. The C-terminal end of the derived protein sequences displays sequence similarity to a number of cysteine proteinase inhibitors, called cystatins, suggesting a common physiological function. Upon Northern blotting with a labeled cDNA fragment, three different 22-kDa protein mRNAs, i.e. 950 nucleotides (nt), 920 nt and 860 nt, could be detected in the rat ventral prostate and the lacrymal gland. In both tissues these messengers were regulated by androgens showing the most rapid androgen response for the 950 nt mRNA form. Administration of cycloheximide nearly completely abolished the observed androgen effect suggesting that a short-living protein is required for the full induction of the 22-kDa protein genes. Hybridization experiments with specific oligonucleotides which distinguish between the mRNAs encoding both 22-kDa protein variants indicate that one protein form is less androgen dependent in the ventral prostate and not expressed in the lacrymal gland.
Screening of a copy-DNA (cDNA) library constructed from RNA isolated from young developing ovaries of snowdrop (Galanthus nivalis) resulted in the isolation of five lectin clones which clearly differed from each other with regard to their nucleotide sequence and deduced amino-acid sequence. Sequence comparison between the coding regions of different lectin cDNAs revealed the highest homology between lectin clones LECGNA 3 and LECGNA 5, showing 96.4% and 93.6% similarity at the nucleotide level and at the deduced amino-acid level, respectively, whereas lectin clones LECGNA 1 and LECGNA 3 showed the lowest homology of 81.6% and 68.6% for the nucleotide sequence and the amino-acid sequence, respectively. Only very few lectin cDNA clones containing a polyadenylated tail could be isolated. Moreover all these cDNA clones were derived from isolectin 3 and showed some variability within the length of the 3' untranslated region. The major transcription initiation site was located 30 bases upstream from the AUG codon as could be deduced from primer-extension analysis. Taking into account the small 5' untranslated region of the lectin clones, the size of the lectin mRNA, which is approx. 780 nucleotides as determined by Northern blot analysis, is in good agreement with the length of the cDNA clones isolated. Besides the ovary tissue, both the leaf and the flower tissue were also shown to express the lectin mRNA in a flowering snowdrop plant.
The complete gene encoding the polypeptide Cl of the complex androgen-controlled prostatic binding protein was isolated from a rat genomic library. A new genomic fragment (C2B) containing only the 5\ m=' \ part of a C2-related gene was also purified. The segments containing exon 1 and a large part of the adjacent sequences were analysed and compared with the corresponding region of the C2A gene which has been completely sequenced previously. The high structural similarity extending over a large part of all three genomic fragments suggests the duplication of a common ancestral gene, followed by a more recent duplication of the C2-coding region. However, since the structural similarity upstream of position \m=-\150 between C2A and C2B abruptly disappears and no transcripts specific for the C2B region can be detected in prostate RNA, we propose that at a later stage in evolution the C2B region was disrupted and inactivated. Despite the common origin and the similar regulation of the two active genes, Cl and C2A, the only obvious conserved structural element is the homopurine stretch located at position \m=-\400, although sequence motifs resembling steroid hormone response elements are present at several locations.
The influence of an intravenous injection of ovine prolactin on circulating levels of thyroid hormones was studied in Rhode Island Red embryos and chicks after hatching. In the chick embryo, 2 h after injection of 0.1 microgram prolactin (on incubation day 19), serum triiodothyronine (T3) increased threefold; after 10 or 100 micrograms prolactin (on incubation day 18) serum T3 increased 15- to 25-fold. These profound increases were not observed in chicks after hatching. Serum concentrations and thyroid content of thyroxine (T4) in embryos and chicks of all ages studied were not influenced by the prolactin injections. Maximal serum concentrations of reverse T3 (rT3) were found on incubation day 18 (110.25 +/- 23.36 pmol/l; 71.66 +/- 15.18 pg/ml; n = 8), whereas after hatching no rT3 could be detected. An injection of 10 micrograms prolactin on day 18 depressed serum rT3 after 2 h to 5.68 +/- 3.20 pmol/l (3.69 +/- 2.08 pg/ml; n = 8; P less than 0.001); the effect of 100 micrograms prolactin was less pronounced. After hatching, chronic administration of prolactin resulted in decreased serum levels of T3, but not of T4, and hypertrophy of the follicles in the thyroid gland. It is concluded that prolactin plays a major role in the maturation of embryonic thyroid metabolism by changing the T4-5-monodeiodination into a T4-5'-monodeiodination. The hypertrophy of the thyroid gland observed after hatching following prolonged prolactin administration may be due to decreased negative feedback of T3 on the hypophysis.
The gene coding for rat ventral prostatic proline-rich polypeptides (PRRl) was mapped to chromosome region . 10q26→q31 by in situ hybridization. The high percentage (40%) of specific hybridization signal obtained is probably the result of the highly repetitive structure of the PRRl gene
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.