scholarly journals Folate Hydrolase 1 Measurement

2020 ◽  
Author(s):  
Keyword(s):  
2011 ◽  
Vol 24 (11) ◽  
pp. 1521-1529 ◽  
Author(s):  
Mary K Samplaski ◽  
Warren Heston ◽  
Paul Elson ◽  
Cristina Magi-Galluzzi ◽  
Donna E Hansel

2009 ◽  
Vol 296 (3) ◽  
pp. G476-G481 ◽  
Author(s):  
Tracy B. Shafizadeh ◽  
Charles H. Halsted

In humans and pigs, hydrolysis of dietary polyglutamyl folates is carried out by intestinal brush border folate hydrolase [glutamate carboxypeptidase II (GCPII)], whereas the transport of the monoglutamyl folate derivatives occurs via the intestinal brush border reduced folate carrier (RFC). The study objective was to measure the expression of intestinal GCPII and RFC during postnatal development of pigs and their effects on plasma and liver folate concentrations. Duodenum, jejunum, ileum, liver, and plasma samples were collected from female Yorkshire pigs at birth, 24 h, 1 wk, 3 wk, and 6 mo ( n = 6 at each time point). GCPII mRNA transcripts and protein (normalized using β-actin), and enzyme activity (normalized per mg mucosal protein) were highest in all segments of small intestine at birth and were undetectable in ileum after 1 wk, whereas jejunal protein and activity predominated at 6 mo. RFC mRNA transcripts were present in all segments of small intestine at birth and declined significantly throughout development to 6 mo. Conversely, RFC protein increased twofold during the first 24 h and remained constant throughout development in all segments of small intestine. Liver RFC mRNA transcripts were detected at birth but were reduced by 6 mo. Liver folate concentration increased throughout postnatal development, whereas plasma folate levels increased during the first 24 h but decreased over time, reflecting the pattern of RFC expression in small intestine. These findings show that intestinal GCPII and intestinal and hepatic RFC all exhibit ontogenic changes in the pig that are reflected in postnatal folate status.


2002 ◽  
Vol 184 (13) ◽  
pp. 3476-3484 ◽  
Author(s):  
Alex Studer ◽  
Craig McAnulla ◽  
Rainer Büchele ◽  
Thomas Leisinger ◽  
Stéphane Vuilleumier

ABSTRACT Methylobacterium chloromethanicum CM4 is an aerobic α-proteobacterium capable of growth with chloromethane as the sole carbon and energy source. Two proteins, CmuA and CmuB, were previously purified and shown to catalyze the dehalogenation of chloromethane and the vitamin B12-mediated transfer of the methyl group of chloromethane to tetrahydrofolate. Three genes located near cmuA and cmuB, designated metF, folD and purU and encoding homologs of methylene tetrahydrofolate (methylene-H4folate) reductase, methylene-H4folate dehydrogenase-methenyl-H4folate cyclohydrolase and formyl-H4folate hydrolase, respectively, suggested the existence of a chloromethane-specific oxidation pathway from methyl-tetrahydrofolate to formate in strain CM4. Hybridization and PCR analysis indicated that these genes were absent in Methylobacterium extorquens AM1, which is unable to grow with chloromethane. Studies with transcriptional xylE fusions demonstrated the chloromethane-dependent expression of these genes. Transcriptional start sites were mapped by primer extension and allowed to define three transcriptional units, each likely comprising several genes, that were specifically expressed during growth of strain CM4 with chloromethane. The DNA sequences of the deduced promoters display a high degree of sequence conservation but differ from the Methylobacterium promoters described thus far. As shown previously for purU, inactivation of the metF gene resulted in a CM4 mutant unable to grow with chloromethane. Methylene-H4folate reductase activity was detected in a cell extract of strain CM4 only in the presence of chloromethane but not in the metF mutant. Taken together, these data provide evidence that M. chloromethanicum CM4 requires a specific set of tetrahydrofolate-dependent enzymes for growth with chloromethane.


2017 ◽  
Vol 137 (10) ◽  
pp. S287
Author(s):  
B. Meier ◽  
M. Ramirez-Fort ◽  
N. Bander ◽  
L. French

2011 ◽  
Vol 24 (11) ◽  
pp. 1531-1531
Author(s):  
Mary K Samplaski ◽  
Warren Heston ◽  
Paul Elson ◽  
Cristina Magi-Galluzzi ◽  
Donna E Hansel

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