Identification of folate binding proteins in rat liver.

Zamierowski, Marilyn M.; Wagner, Conrad

doi:10.1016/s0021-9258(19)75187-4

Cited by 69 publications

(6 citation statements)

References 29 publications

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“…A number of years ago, extracts from rat liver mitochondria were shown to contain two proteins, which when taken through several purification steps still contained bound H4PteGlu" (Zamierowski & Wagner, 1977). More recently, these proteins have been identified as sarcosine dehydrogenase and dimethylglycine dehydrogenase (Wittwer & Wagner, 1981), which like serine hydroxymethyltransferase are involved in glycine metabolism.…”

Section: Resultsmentioning

confidence: 99%

Interaction of tetrahydropteroylpolyglutamates with two enzymes from mitochondria

Strong¹,

Cook²,

Schirch³

1989

Biochemistry

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The dissociation constants of tetrahydropteroylpolyglutamates, having from one to six glutamate residues, have been determined for the two mitochondrial enzymes serine hydroxymethyltransferase and dimethylglycine dehydrogenase. The ratios of the dissociation constants for the mono- and hexaglutamate forms of the coenzyme were 200 and less than 10 for serine hydroxymethyltransferase and dimethylglycine dehydrogenase, respectively. Km and kcat values were determined for the reversible interconversion of serine and glycine as a function of the number of glutamyl residues on the coenzyme. The values in the serine to glycine direction did not significantly change with the number of glutamyl residues, but in the glycine to serine direction, there was a 9-fold increase in the kcat/Km when the longer chain polyglutamates were used as the coenzyme substrate. A sensitive and rapid method for determining the dissociation constants of proteins which bind either tetrahydropteroylpolyglutamates or their 5-methyl and 5-formyl conjugates is described.

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Section: Resultsmentioning

confidence: 99%

Interaction of tetrahydropteroylpolyglutamates with two enzymes from mitochondria

Strong¹,

Cook²,

Schirch³

1989

Biochemistry

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“…Previous studies by Zamierowski & Wagner (1977) indicated that FBP-CI contained a tightly bound folate polyglutamate which was not a 5-CH3-H4PteGlu derivative. In these studies, we have identified the principal form of folate which is bound as H4PteGlu5.…”

Section: Discussionmentioning

confidence: 95%

“…Purification of Folate Binding Protein-Cytosol I Chromatography on Sephacryl S-200. Zamierowski & Wagner (1977) previously showed that Sephadex G-150 chromatography of liver cytosol prepared from rats injected with [3H]-…”

Section: Resultsmentioning

confidence: 99%

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Purification and partial characterization of rat liver folate binding protein: cytosol I

Cook¹,

Wagner²

1982

Biochemistry

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The high molecular weight folate binding protein of rat liver cytosol has been purified to apparent homogeneity. Purification was achieved by using a combination of gel filtration, O-(diethylaminoethyl)cellulose chromatography, and affinity chromatography. This folate binding protein was initially identified during purification by an in vivo labeling procedure involving intraperitoneal injection of [3H]folic acid prior to sacrifice and subsequently by its ability to bind naturally reduced [3H]folate polyglutamates in vitro. A molecular weight of 210 000 was estimated by gel chromatography. This is distinct from the trifunctional formyl-methenyl-methylene synthetase of rat liver which has a molecular weight of 225 000. Sodium dodecyl sulfate electrophoresis revealed a single band with a molecular weight of about 100 000 which suggests the native protein is composed of two identical subunits. The partially purified protein contains bound tetrahydropteroylpentaglutamate.

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“…Folate supplementation effectively decreased the degree of DNA hypomethylation of the rectal mucosa, but only in patients with a single polyp (Cravo et al, 1998). Similar to many other metabolites, folate can be detected in the nucleus (Zamierowski and Wagner, 1977). In the nucleus, folate is bound to LSD1 and protects LSD1 from inhibition by formaldehyde (Luka et al, 2011;Luka et al, 2014).…”

Section: Metabolic Control Of (Histones) Proteins and Dna Methylationmentioning

confidence: 99%

Metabolic reprogramming and epigenetic modifications on the path to cancer

2021

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Metabolic rewiring and epigenetic remodeling, which are closely linked and reciprocally regulate each other, are among the well-known cancer hallmarks. Recent evidence suggests that many metabolites serve as substrates or cofactors of chromatin-modifying enzymes as a consequence of the translocation or spatial regionalization of enzymes or metabolites. Various metabolic alterations and epigenetic modifications also reportedly drive immune escape or impede immunosurveillance within certain contexts, playing important roles in tumor progression. In this review, we focus on how metabolic reprogramming of tumor cells and immune cells reshapes epigenetic alterations, in particular the acetylation and methylation of histone proteins and DNA. We also discuss other eminent metabolic modifications such as, succinylation, hydroxybutyrylation, and lactylation, and update the current advances in metabolism- and epigenetic modification-based therapeutic prospects in cancer.

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Identification of folate binding proteins in rat liver.

Cited by 69 publications

References 29 publications

Interaction of tetrahydropteroylpolyglutamates with two enzymes from mitochondria

Interaction of tetrahydropteroylpolyglutamates with two enzymes from mitochondria

Purification and partial characterization of rat liver folate binding protein: cytosol I

Metabolic reprogramming and epigenetic modifications on the path to cancer

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