Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.4 (ribonuclease)
 6,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Alkaline phosphatase (ALP) in human choriocarcinoma cells (malignant trophoblasts) was characterized by its greater sensitivity to EDTA and L-leucine inhibition as compared with the placental isozyme. In addition, both the fully processed and the nonglycosylated forms of choriocarcinoma ALP migrated faster than the corresponding placental enzyme in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Choriocarcinoma cells express a 2.6-kilobase (kb) ALP mRNA unlike normal human placenta which expresses a 2.8-kb ALP mRNA. Administration of sodium butyrate to choriocarcinoma cells greatly increased the steady-state levels of the 2.6-kb choriocarcinoma ALP mRNA, which resulted in an increase in enzyme activity and biosynthesis. S1 nuclease analysis using probes derived from a placental ALP cDNA and ribonuclease protection assays employing probes derived from the germ cell ALP gene demonstrated that choriocarcinoma cells express the germ cell ALP gene. The germ cell ALP gene encodes the placental ALP-like isozyme that is primarily expressed in the thymus, testis, and germ cell tumors. The structures of the internal exons (II-X) of the germ cell ALP gene were determined previously based on their similarity to the placental ALP gene. However, the boundaries of exons I and XI (3' exon) of the germ cell ALP gene were not defined due to sequence divergence between the two genes at the 5' and 3' regions. Ribonuclease protection and primer extension assays demonstrated that exon I of this gene is 119 base pairs in length and that germ cell ALP mRNA contains one major transcription initiation site. The isolation and characterization of germ cell ALP cDNA clones from a butyrate-treated choriocarcinoma cDNA library showed that the germ cell ALP mRNA is 2487 bases in length and exon XI of this gene is 1135 base pairs long.
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PMID:Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. 274 60

Angiotensin I-converting enzyme (ACE) is known to be present at the surface of endothelial cells and also in the adventitia in large vessels. The presence of ACE in the vascular smooth muscle remains controversial. We microdissected segments of adventitia and media with or without endothelium from a region devoid of collateral arteries. The membrane-bound ACE activity in the media averaged 41% (pmol [glycine-1-14C]hippuryl-L-histidyl-L-leucine hydrolyzed.g tissue-1.min-1) of the values found in the whole aorta, whereas the adventitia contained only 6%. Immunoreactive ACE in media was characterized by Western blotting. ACE mRNAs were detected and characterized after polymerase chain amplification in isolated media. Angiotensin I and angiotensin II were equally able to contract medial rings, and the response to angiotensin I was blocked by enalaprilat. In aortas of two-kidney, one-clip hypertensive rats, there was an increase in ACE mRNA estimated by ribonuclease protection assay (P = 0.02) and in ACE activity at 15 days and 1 and 3 mo after clipping. This corresponded to a 1.5- to 2-fold increase in the ACE activity of both the media and the adventitia compared with sham-operated rats (P < or = 0.02). Thus ACE gene expression occurs in smooth muscle of rat aorta, which contains roughly the same amount of enzyme as the endothelium and readily converts angiotensin I to angiotensin II. ACE in the medial layer and the adventitia is upregulated in renovascular hypertension.
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PMID:ACE in three tunicae of rat aorta: expression in smooth muscle and effect of renovascular hypertension. 797 8