Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0035078 (renal failure)
 31,970 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum RNase (RNase I; ribonuclease 3'-pyrimidino-oligonucleotidohydrolase, EC 3.1.4.22) activity (mean +/- SD) with polycytidine as substrate was determined in normal individuals (24.9 +/- 3.0 units/ml) and in patients with pancreatic cancer (37.3 +/- 14.8), pancreatitis (38.5 +/- 12.6), nonpancreatic diseases (48.7 +/- 14.8), or renal failure (175.8 +/- 92.8). Patients with pancreatic cancer could not be distinguished from those with pancreatitis or with nonpancreatic disease, although the RNase activities in all of these differed from the activity in normal individuals. The serum RNase activities of four patients with resectable "curable") pancreatic carcinoma and two others with advanced pancreatic cancer without obstructive jaundice were normal. After total pancreatectomy, serum RNase activity remained in the high-normal range. The data presented here and data in the literature show that serum RNase cannot be of primarily pancreatic origin. The present study also demonstrates that measurement of its activity is not useful in early detection of pancreatic cancer.
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PMID:Serum RNase in the diagnosis of pancreatic carcinoma. 28 51

Serum ribonuclease of normal persons and of patients with renal impairment was determined with polycytidylic acid as substrate. There was a pronounced rise in the serum ribonuclease of patients with renal impairment. Average serum ribonuclease values of 25 normal persons and 25 patients with renal impairment, respectively were 110 and 2329 units per ml of serum. Serum ribonuclease, because of its unique specificity, stability and abnormal elevation in the sera of patients with renal failure, might serve as an additional indicator in the assessment of renal function.
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PMID:Serum ribonuclease of normal persons and patients with renal impairment. 70 4

The mechanisms by which renal failure causes hyperlipoproteinemia remain unclear. To investigate the potential role of the low-density lipoprotein (LDL) receptor in lipoprotein metabolism in uremia we measured LDL receptor function in peripheral blood mononuclear cells (PBMC) from uremic patients and control subjects using a functional assay in which proliferation of lectin-stimulated PBMC in the presence of lovastatin was dependent upon internalization of exogenous cholesterol via a functional LDL receptor. The amount of LDL required to reverse 50% of lovastatin-induced inhibition of proliferation in PBMC from uremic patients was significantly greater (3.6 +/- 1.8 micrograms/ml, N = 33, P < 0.05) than controls, (1.99 +/- 0.6 micrograms/ml, N = 37). Abnormal LDL receptor function in four uremic patients normalized following renal transplantation. To investigate the molecular basis for LDL receptor dysfunction, we directly quantitated LDL receptor messenger RNA (mRNA) in PBMC from uremic patients and control subjects using a ribonuclease protection assay. LDL receptor mRNA expression in uremic patients was 0.42 +/- 0.08 (N = 10), significantly lower (P < 0.015) than in normal subjects, 0.71 +/- 0.08 (N = 14). These data suggest that an acquired defect in LDL receptor function in PBMC from uremic patients exists which may be due to decreased LDL receptor expression. These abnormalities, if present in other tissues, could contribute to the aberrant lipoprotein metabolism which is a consistent feature of uremia.
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PMID:Decreased low-density lipoprotein receptor function and mRNA levels in lymphocytes from uremic patients. 145 9

Acid and alkaline ribonuclease (RNase) activities were measured in serum and urine using procedure based on assumption that all determined RNase activities, both at pH 6.5 and 7.8 represent values produced by overlapping of activities of acid leukocyte type RNase and alkaline pancreatic type RNase. The procedure requires simultaneous determining of RNase activity at pH 6.5 and 7.8 and further calculation of actual activities of acid and alkaline RNase activities using the elaborated experimental formula. Results of determining acid and alkaline RNases in human sera yielded on information on specific contribution of leukocyte type and pancreatic type RNases to increased RNase activity in such clinical conditions as terminal renal failure, myocardial infarction and chronic myelogenous leukemia. It was also found that there is in human urine a remarkably increased proportion of acid RNase activity if compared to this in serum.
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PMID:Determining of actual activities of acid and alkaline ribonuclease in human serum and urine. 184 95

The activities of serum acid ribonuclease (RNase) were determined in patients with malignant neoplasm or with renal failure. The levels were markedly increased in myelogenous leukemia and renal failure, and only slightly increased in solid cancers, lymphoid malignancies and multiple myeloma. These increases correlated significantly with serum LDH activity in myelogenous leukemia and with creatinine levels in other malignancies or renal failure. The acid RNase content of granulocytes was 22.7-fold higher than that of lymphocytes. The increase of serum acid RNase may suggest an increased granulocyte destruction in myelogenous leukemia and a reduced glomerular filtration in other malignant neoplasms and renal failure.
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PMID:Activities of serum acid ribonuclease in patients with malignant neoplasms or with renal failure. 658 Sep 78

A method for radioimmunoassay of human pancreatic RNase was developed. The method is sensitive, reproducible, and specific. Almost no cross-reactivity exists between human pancreatic and liver RNases. A good correlation was observed between the serum concentration of pancreatic RNase as measured by radioimmunoassay and its enzymatic activity using polycytidylic acid as substrate. The concentration of serum pancreatic RNase correlates well with age, blood urea nitrogen, and albumin contents but does not correlate with serum amylase activity. Using the data of 52 patients with malignant tumors except pancreatic cancer, serum RNase level could be expressed by a multiple regression equation: Immunoreactive RNase content in pancreatic cancer was elevated in patients with complications from renal failure. Serum pancreatic RNase contents in patients with pancreatic cancer measured by radioimmunoassay agreed well with the values calculated using the equation derived from the data of patients with other malignant tumors.
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PMID:Radioimmunoassay for human pancreatic ribonuclease and measurement of serum immunoreactive pancreatic ribonuclease in patients with malignant tumors. 671 12

The anemia of chronic renal failure was studied by assessing the effect of uremic serum on proliferation of human marrow erythroid stem cells into colonies in vitro. Of 50 sera tested, 46 inhibited "CFU-E" colony formation by a mean of 72%, and 42 inhibited "BFU-E" colonies by a mean of 53.5%, compared to normal sera. Analysis of the uremic sera revealed a striking increase of ribonuclease activity in every patient. Mean activity in the study group was 17,346 U/ml serum (range 6,700-36,250) compared to control mean of 1,047 +/- 247 U/ml. Purified ribonuclease added to marrow cultures in concentrations simulating uremic serum produced a dose-dependent decrease in CFU-E colonies suggesting that the substance has a role in the production of anemia of renal failure.
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PMID:Ribonuclease inhibition of erythropoiesis in anemia of uremia. 682 70

Differences in heart stability of human pancreatic ribonuclease (cRNase) and serum ribonuclease were abolished by aprotinin, suggesting that the pancreatic enzyme was similar to the serum enzyme, but was being destroyed by proteases. Serum ribonuclease levels in normal subjects correlated with age but were unaffected by meal ingestion. Serum ribonuclease was not found to be useful in the detection of pancreatic cancer and was more frequently abnormal in patients with other solid tumours or renal failure.
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PMID:Non-specificity of elevated serum ribonuclease as a pancreatic tumour marker. 727 5

The cellular effects of insulin-like growth factor I (IGF-I) are modified by a family of binding proteins (IGFBPs) that act as reservoirs in serum for the growth factor and are produced locally by tissues, including the kidney. Because regulation of these proteins may influence renal repair, either directly or by their interactions with IGF-I, we studied gene expression during the recovery from renal failure induced by folic acid and during the compensatory increase in renal function following uninephrectomy (UNX). Expression of IGF-I, the IGF-I receptor (IGF-IR), and all six IGFBPs was detected using an ribonuclease protection assay. IGFBP-5 was the most abundant binding protein mRNA present in kidney, whereas IGFBP-2 and -6 were the least abundant. During regeneration following folic acid-induced acute renal failure, IGF-I, IGFBP-3, and IGFBP-5 mRNAs declined in abundance approximately two- to threefold. On the other hand, IGF-IR, IGFBP-1, and IGFBP-2 were increased (approximately 2-, 6-, and 6-fold, respectively) in the first 24 h. IGFBP-1 mRNA remained elevated for at least 3 days. Despite the known increase in cellular RNA content following UNX, little difference in specific expression of mRNAs was observed. Because IGFBP-1 has been shown to stimulate cell migration and has previously been localized to the distal nephron, the site of greatest injury in the folic acid model, these data are compatible with the notion that this protein may function either directly to affect cellular repair or act as a reservoir for IGF-I under conditions of cellular damage.
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PMID:Differential mRNA expression of insulin-like growth factor system during renal injury and hypertrophy. 859 75

Xanthine dehydrogenase (XDH, EC 1.1.1.204) is a rate-limiting enzyme in the oxidative metabolism of purines and is thought to play a key role in a variety of pathophysiologic processes including ischemiasolidusreperfusion injury, viral pneumonia, and renal failure. We herein report the isolation and characterization of the human XDH gene. The gene is composed of 36 exons and 35 introns and spans at least 60 kb. The exon sizes range from 53 to 279 bp, and the intron sizes range from 0.2 to over 8 kb. Using primer extension and RNase protection analyses, two transcriptional initiation sites were identified 59 and 82 nucleotides upstream of the ATG start codon. One Goldberg-Hogness box (ATTTAT)-like sequence was found 24 bp upstream from the second transcriptional initiation site, and two inverted CCAAT sequences were found 19 and 42 bp upstream from the second transcriptional initiation sites. A relative GC-enriched region was found between -55 and -121. Approximately 2 kb of the 5'-flanking region was sequenced, and a variety of putative regulatory elements were identified including CsolidusEBP binding sites, IL-6 and NF-kappaB sites, and potential TNF-RE, IFN-gamma-RE, and IL-1-RE sites.
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PMID:Molecular cloning and characterization of the human xanthine dehydrogenase gene (XDH). 866 Oct 45


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