Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.49 (reverse transcriptase)
 31,746 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Vitronectin is an adhesion protein present within the acrosomal cap region of human spermatozoa and is liberated during the acrosome reaction. The purpose of this study was to determine if vitronectin mRNA was synthesized in the male genital tract using the reverse transcriptase in-situ polymerase chain reaction (PCR) technique. Twelve genital tract tissues, which included six testes, one showing Sertoli cells only and one from a 3 year old boy, as well as sections from the prostate, seminal vesicles, and epididymis, were analysed for vitronectin transcripts. PCR-amplified vitronectin cDNA was detected in the seminiferous tubules of the four adult testes that showed normal spermatogenesis and localized to the spermatocytes and round spermatids. PCR-amplified vitronectin cDNA was not detected in the tissues of the prostate, epididymis, and seminal vesicles from the men whose testes did contain the message, nor in the testes with Sertoli cells only or that of the prepubertal boy. It is concluded that, in the male genital tract, vitronectin is transcribed exclusively in the germ cells at the spermatocyte and round spermatid stages. This demonstrates that the translated protein present in the spermatozoon is being produced in situ. Further study is needed to determine the role of this protein in the dynamics of sperm-oocyte interaction.
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PMID:PCR-amplified vitronectin mRNA localizes in situ to spermatocytes and round spermatids in the human testis. 856 71

Glycodelin is a 28 kDa glycoprotein of the lipocalin family that was previously considered to be specific for the reproductive tract. Glycodelin is found in the secretory glandular epithelium of endometrium and in seminal vesicles. Given the cyclic differentiation of normal endometrial epithelium, we studied by immunohistochemistry a possible expression of glycodelin in other tissues displaying stroma-to-epithelium maturation. We report here that 11/11 biphasic synovial sarcomas expressed glycodelin in the cells exhibiting epithelial or glandular differentiation while the sarcomatous spindle cells remained negative. Glycodelin was also found in secreted material in the lumina of the gland-like structures. In only 1 of the 7 monophasic synovial sarcomas studied, focal glycodelin reactivity was seen in some flattened spindle cells. The expression of glycodelin in biphasic synovial sarcoma tissue was further verified by the demonstration of glycodelin mRNA by reverse transcriptase-polymerase chain reaction. Considering the monoclonal origin of synovial sarcomas, our findings raise the intriguing possibility that activation of expression of the glycodelin gene is involved in the molecular regulation of mesenchyme-to-epithelium differentiation.
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PMID:Epithelial expression of glycodelin in biphasic synovial sarcomas. 959 Jan 22

Trypsinogen is a serine proteinase produced mainly by the pancreas, but it has recently been found to be expressed also in several cancers such as ovarian and colon cancer and in vascular endothelial cells. In this study, we found that trypsinogen-1 and -2 are present at high concentrations (median levels, 0.4 and 0.5 mg/L, respectively) in human seminal fluid and purified them to homogeneity by immunoaffinity and anion exchange chromatography. Purified trypsinogen isoenzymes displayed a M(r) of 25 to 28 kd in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting. Most of the trypsinogen-1 purified from seminal fluid was enzymatically active whereas trypsinogen-2 occurred as the proform, which could be activated by enteropeptidase in vitro. Immunohistochemically, trypsinogen protein was detected in the human prostate, urethra, utriculus, ejaculatory duct, seminal vesicles, deferent duct, epididymal glands, and testis. Expression of trypsinogen mRNA in the same organs was demonstrated by in situ hybridization. Trypsinogen mRNA was also detected in the prostate and seminal vesicles by reverse transcriptase-polymerase chain reaction and Northern blotting. Isolated trypsin was shown to activate the proenzyme form of prostate-specific antigen. These results suggest that trypsinogen isoenzymes found in seminal fluid are produced locally in the male genital tract and that they may play a physiological role in the semen.
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PMID:Expression and characterization of trypsinogen produced in the human male genital tract. 1110 74

Stra8 (Stimulated by Retinoic Acid 8) is considered a meiotic gatekeeper gene. Using reverse transcriptase PCR and rapid amplification of cDNA ends (RACE), the complete sequence of the pig Stra8 gene was cloned. Bioinformatics analyses of this sequence were performed. Using semi-quantitative methods, the expression characteristics of Stra8 in Testis, cauda epididymis, body epididymis, caput epididymis, seminal vesicles, prostate gland, Cowper's gland, heart, liver, spleen, lung, kidney, stomach, hypothalamus, pituitary gland, cerebrum, cerebellum, and hippocampus of adult Meishan boar and sow tissues were examined. The expression pattern in the testis of 2-, 30-, 60-, 90-, and 150-day old Meishan boars were analyzed using real-time PCR. We constructed a eukaryotic expression vector for the Stra8 gene and used it to transfect NIH-3T3 cells and third generation pig spermatogonial stem cells (SSCs) cultured in vitro. Testes weight and sperm count in the cauda epididymis were evaluated at various time points. The results showed that the length of the pig Stra8 gene cDNA was 1444 bp encoding 366 amino acids with one typical helix-loop-helix (HLH) domain. It is testes-specific expression. Expression was first detected in boar testis starting at day 2, and its expression significantly (p<0.05) increased with age and body weight. When NIH-3T3 cells and pig SSCs were transfected with the eukaryotic expression vector EGFP (enhanced green fluorescent protein)-N1-pStra8, it was expressed in the cytoplasm of NIH-3T3 cells. However, in SSCs, Stra8 was expressed predominantly in cytoplasm and few in nucleus. Our data suggest that perhaps Stra8 acts as a transcription factor to initiate meiosis in young boar.
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PMID:Cloning and expression characteristics of the pig Stra8 gene. 2502 39