Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A series of deletions removing progressively larger parts of the 5' flanking region of the Escherichia coli pepD gene was constructed. After fusing the resulting promoter fragments to the chromosomal malPQ operon, their activities were determined by assaying for amylomaltase, the product of the malQ gene. Transcription from the pepD promoter region in exponentially growing cells was estimated to be about 5 times less efficient than transcription from the induced lac promoter. Approximately 115 bp preceding the translation start site of the pepD gene are important for regular promoter functioning, whereas the more distal sequences could be deleted without any significant effects. In bacterial cultures containing limiting amounts of inorganic phosphate, the rate of de novo synthesis of peptidase D, simultaneously with the derepression of alkaline phosphatase, increased about fivefold as a consequence of phosphate starvation. This regulation was shown to occur at the transcriptional level by the use of chromosomal pepD promoter-malPQ fusions. The inducibility by phosphate limitation was conserved in all of the deletion clones in which the pepD promoter region was still functional. As demonstrated by the use of phoB, R, and M mutants, the modulation of pepD expression is independent of the genetic system controlling the pho regulon.
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PMID:The promoter region of the Escherichia coli pepD gene: deletion analysis and control by phosphate concentration. 131 42

The activities of microvillus aminopeptidase (microsomal, EC 3.4.11.2), dipeptidyl peptidase IV (EC 3.4.14.-), glycyl-leucine dipeptidase (EC 3.4.13.11), proline dipeptidase (EC 3.4.13.9), sucrase (EC 3.2.1.48) and gamma-glutamyl transpeptidase (EC 2.3.2.2) were measured in peroral intestinal biopsies taken from patients with coeliac disease in the acute phase and in remission. A comparison with the amounts of corresponding activities from a reference group showed that all the measured activities were significantly decreased in the acute phase of the disease. In patients in remission only microvillus aminopeptidase and dipeptidyl dipeptidase IV displayed a substantial depression as compared to the reference group. It is suggested that a primary mucosal digestion defect will result in lack of substrate for other intestinal enzymes. This is a situation comparable to starvation and may explain the variation in the grade of restitution for the different enzymes.
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PMID:Intestinal peptidases and sucrase in coeliac disease. 700 82

Prolidase [E.C. 3.4.13.9] plays an important role in the recycling of proline for collagen synthesis and cell growth and this enzyme activity determines the rate of collagen turnover. It has been previously suggested that prolidase activity is regulated through signal mediated by the interaction of ECM proteins, with b1 integrin receptor and that this interaction is disturbed in MCF-7 cells. The potential candidates for mediating signal transduction are the nonreceptor tyrosine kinase p125FAK and two mitogen-activated protein (MAP) kinases, ERK-1 and ERK-2, which are activated upon attachment of cells to ECM. We found that serum starvation of MCF-7 cells for 24 hours contributed to a significant decrease (by about 30%) in prolidase activity and collagen biosynthesis. These phenomena were accompanied by suppression of MAP kinases expression without any effect on the expression of FAK. The data suggest that prolidase activity and collagen biosynthesis respond to signal mediated by MAP kinases, independently of FAK expression in MCF-7 cells.
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PMID:FAK-independent regulation of prolidase activity and collagen biosynthesis in MCF-7 cells. 1182 Jun 13