Eintrag weiter verarbeiten
Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation
Gespeichert in:
| Zeitschriftentitel: | American Journal of Physiology-Gastrointestinal and Liver Physiology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | American Journal of Physiology-Gastrointestinal and Liver Physiology, 286, 2004, 4, S. G588-G595 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
|
| Schlagwörter: |
| author_facet |
Townsend, Justin H. Davis, Steven R. Mackey, Amy D. Gregory, Jesse F. Townsend, Justin H. Davis, Steven R. Mackey, Amy D. Gregory, Jesse F. |
|---|---|
| author |
Townsend, Justin H. Davis, Steven R. Mackey, Amy D. Gregory, Jesse F. |
| spellingShingle |
Townsend, Justin H. Davis, Steven R. Mackey, Amy D. Gregory, Jesse F. American Journal of Physiology-Gastrointestinal and Liver Physiology Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation Physiology (medical) Gastroenterology Hepatology Physiology |
| author_sort |
townsend, justin h. |
| spelling |
Townsend, Justin H. Davis, Steven R. Mackey, Amy D. Gregory, Jesse F. 0193-1857 1522-1547 American Physiological Society Physiology (medical) Gastroenterology Hepatology Physiology http://dx.doi.org/10.1152/ajpgi.00454.2003 <jats:p>Little is known about homocysteine metabolism in intestine. To address this question, we investigated homocysteine metabolism under conditions of folate adequacy and folate deprivation in the Caco-2 cell line, a model of human intestinal mucosal cells. Caco-2 cells were cultured in media enriched with [3-<jats:sup>13</jats:sup>C]serine and [U-<jats:sup>13</jats:sup>C<jats:sub>5</jats:sub>]methionine tracers, and enrichments of intracellular free amino acid pools of these amino acids as well as homocysteine, cystathionine, and cysteine were measured by using gas chromatography/mass spectrometry. Homocysteine transsulfuration plus folate-dependent and total remethylation were quantified from these amino acid enrichments. Homocysteine remethylation accounted for 19% of the intracellular free methionine pool in cells cultured with supplemental folate, and nearly all one-carbon units used for remethylation originated from the three carbon of serine via folate-dependent remethylation. Labeling of cystathionine and cysteine indicated the presence of a complete transsulfuration pathway in Caco-2 cells, and this pathway produced 13% of the intracellular free cysteine pool. Appearance of labeled homocysteine and cystathionine in culture medium suggests export of these metabolites from intestinal cells. Remethylation was reduced by one-third in folate-restricted cell cultures ( P < 0.001), and only ∼50% of the one-carbon units used for remethylation originated from the three carbon of serine under these conditions. In conclusion, the three carbon of serine is the primary source of one-carbon units used for homocysteine remethylation in folate-supplemented Caco-2 cell cultures. Remethylation is reduced as a result of folate restriction in this mucosal cell model, and one-carbon sources other than the three carbon of serine contribute to remethylation under this condition.</jats:p> Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation American Journal of Physiology-Gastrointestinal and Liver Physiology |
| doi_str_mv |
10.1152/ajpgi.00454.2003 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie Medizin |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTE1Mi9hanBnaS4wMDQ1NC4yMDAz |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTE1Mi9hanBnaS4wMDQ1NC4yMDAz |
| institution |
DE-D275 DE-Bn3 DE-Brt1 DE-D161 DE-Zwi2 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 |
| imprint |
American Physiological Society, 2004 |
| imprint_str_mv |
American Physiological Society, 2004 |
| issn |
0193-1857 1522-1547 |
| issn_str_mv |
0193-1857 1522-1547 |
| language |
English |
| mega_collection |
American Physiological Society (CrossRef) |
| match_str |
townsend2004folatedeprivationreduceshomocysteineremethylationinahumanintestinalepithelialcellculturemodelroleofserineinonecarbondonation |
| publishDateSort |
2004 |
| publisher |
American Physiological Society |
| recordtype |
ai |
| record_format |
ai |
| series |
American Journal of Physiology-Gastrointestinal and Liver Physiology |
| source_id |
49 |
| title |
Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_unstemmed |
Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_full |
Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_fullStr |
Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_full_unstemmed |
Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_short |
Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_sort |
folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| topic |
Physiology (medical) Gastroenterology Hepatology Physiology |
| url |
http://dx.doi.org/10.1152/ajpgi.00454.2003 |
| publishDate |
2004 |
| physical |
G588-G595 |
| description |
<jats:p>Little is known about homocysteine metabolism in intestine. To address this question, we investigated homocysteine metabolism under conditions of folate adequacy and folate deprivation in the Caco-2 cell line, a model of human intestinal mucosal cells. Caco-2 cells were cultured in media enriched with [3-<jats:sup>13</jats:sup>C]serine and [U-<jats:sup>13</jats:sup>C<jats:sub>5</jats:sub>]methionine tracers, and enrichments of intracellular free amino acid pools of these amino acids as well as homocysteine, cystathionine, and cysteine were measured by using gas chromatography/mass spectrometry. Homocysteine transsulfuration plus folate-dependent and total remethylation were quantified from these amino acid enrichments. Homocysteine remethylation accounted for 19% of the intracellular free methionine pool in cells cultured with supplemental folate, and nearly all one-carbon units used for remethylation originated from the three carbon of serine via folate-dependent remethylation. Labeling of cystathionine and cysteine indicated the presence of a complete transsulfuration pathway in Caco-2 cells, and this pathway produced 13% of the intracellular free cysteine pool. Appearance of labeled homocysteine and cystathionine in culture medium suggests export of these metabolites from intestinal cells. Remethylation was reduced by one-third in folate-restricted cell cultures ( P < 0.001), and only ∼50% of the one-carbon units used for remethylation originated from the three carbon of serine under these conditions. In conclusion, the three carbon of serine is the primary source of one-carbon units used for homocysteine remethylation in folate-supplemented Caco-2 cell cultures. Remethylation is reduced as a result of folate restriction in this mucosal cell model, and one-carbon sources other than the three carbon of serine contribute to remethylation under this condition.</jats:p> |
| container_issue |
4 |
| container_start_page |
0 |
| container_title |
American Journal of Physiology-Gastrointestinal and Liver Physiology |
| container_volume |
286 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792334669672349708 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T14:32:20.162Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Folate+deprivation+reduces+homocysteine+remethylation+in+a+human+intestinal+epithelial+cell+culture+model%3A+role+of+serine+in+one-carbon+donation&rft.date=2004-04-01&genre=article&issn=1522-1547&volume=286&issue=4&pages=G588-G595&jtitle=American+Journal+of+Physiology-Gastrointestinal+and+Liver+Physiology&atitle=Folate+deprivation+reduces+homocysteine+remethylation+in+a+human+intestinal+epithelial+cell+culture+model%3A+role+of+serine+in+one-carbon+donation&aulast=Gregory&aufirst=Jesse+F.&rft_id=info%3Adoi%2F10.1152%2Fajpgi.00454.2003&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792334669672349708 |
| author | Townsend, Justin H., Davis, Steven R., Mackey, Amy D., Gregory, Jesse F. |
| author_facet | Townsend, Justin H., Davis, Steven R., Mackey, Amy D., Gregory, Jesse F., Townsend, Justin H., Davis, Steven R., Mackey, Amy D., Gregory, Jesse F. |
| author_sort | townsend, justin h. |
| container_issue | 4 |
| container_start_page | 0 |
| container_title | American Journal of Physiology-Gastrointestinal and Liver Physiology |
| container_volume | 286 |
| description | <jats:p>Little is known about homocysteine metabolism in intestine. To address this question, we investigated homocysteine metabolism under conditions of folate adequacy and folate deprivation in the Caco-2 cell line, a model of human intestinal mucosal cells. Caco-2 cells were cultured in media enriched with [3-<jats:sup>13</jats:sup>C]serine and [U-<jats:sup>13</jats:sup>C<jats:sub>5</jats:sub>]methionine tracers, and enrichments of intracellular free amino acid pools of these amino acids as well as homocysteine, cystathionine, and cysteine were measured by using gas chromatography/mass spectrometry. Homocysteine transsulfuration plus folate-dependent and total remethylation were quantified from these amino acid enrichments. Homocysteine remethylation accounted for 19% of the intracellular free methionine pool in cells cultured with supplemental folate, and nearly all one-carbon units used for remethylation originated from the three carbon of serine via folate-dependent remethylation. Labeling of cystathionine and cysteine indicated the presence of a complete transsulfuration pathway in Caco-2 cells, and this pathway produced 13% of the intracellular free cysteine pool. Appearance of labeled homocysteine and cystathionine in culture medium suggests export of these metabolites from intestinal cells. Remethylation was reduced by one-third in folate-restricted cell cultures ( P < 0.001), and only ∼50% of the one-carbon units used for remethylation originated from the three carbon of serine under these conditions. In conclusion, the three carbon of serine is the primary source of one-carbon units used for homocysteine remethylation in folate-supplemented Caco-2 cell cultures. Remethylation is reduced as a result of folate restriction in this mucosal cell model, and one-carbon sources other than the three carbon of serine contribute to remethylation under this condition.</jats:p> |
| doi_str_mv | 10.1152/ajpgi.00454.2003 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie, Medizin |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTE1Mi9hanBnaS4wMDQ1NC4yMDAz |
| imprint | American Physiological Society, 2004 |
| imprint_str_mv | American Physiological Society, 2004 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 0193-1857, 1522-1547 |
| issn_str_mv | 0193-1857, 1522-1547 |
| language | English |
| last_indexed | 2024-03-01T14:32:20.162Z |
| match_str | townsend2004folatedeprivationreduceshomocysteineremethylationinahumanintestinalepithelialcellculturemodelroleofserineinonecarbondonation |
| mega_collection | American Physiological Society (CrossRef) |
| physical | G588-G595 |
| publishDate | 2004 |
| publishDateSort | 2004 |
| publisher | American Physiological Society |
| record_format | ai |
| recordtype | ai |
| series | American Journal of Physiology-Gastrointestinal and Liver Physiology |
| source_id | 49 |
| spelling | Townsend, Justin H. Davis, Steven R. Mackey, Amy D. Gregory, Jesse F. 0193-1857 1522-1547 American Physiological Society Physiology (medical) Gastroenterology Hepatology Physiology http://dx.doi.org/10.1152/ajpgi.00454.2003 <jats:p>Little is known about homocysteine metabolism in intestine. To address this question, we investigated homocysteine metabolism under conditions of folate adequacy and folate deprivation in the Caco-2 cell line, a model of human intestinal mucosal cells. Caco-2 cells were cultured in media enriched with [3-<jats:sup>13</jats:sup>C]serine and [U-<jats:sup>13</jats:sup>C<jats:sub>5</jats:sub>]methionine tracers, and enrichments of intracellular free amino acid pools of these amino acids as well as homocysteine, cystathionine, and cysteine were measured by using gas chromatography/mass spectrometry. Homocysteine transsulfuration plus folate-dependent and total remethylation were quantified from these amino acid enrichments. Homocysteine remethylation accounted for 19% of the intracellular free methionine pool in cells cultured with supplemental folate, and nearly all one-carbon units used for remethylation originated from the three carbon of serine via folate-dependent remethylation. Labeling of cystathionine and cysteine indicated the presence of a complete transsulfuration pathway in Caco-2 cells, and this pathway produced 13% of the intracellular free cysteine pool. Appearance of labeled homocysteine and cystathionine in culture medium suggests export of these metabolites from intestinal cells. Remethylation was reduced by one-third in folate-restricted cell cultures ( P < 0.001), and only ∼50% of the one-carbon units used for remethylation originated from the three carbon of serine under these conditions. In conclusion, the three carbon of serine is the primary source of one-carbon units used for homocysteine remethylation in folate-supplemented Caco-2 cell cultures. Remethylation is reduced as a result of folate restriction in this mucosal cell model, and one-carbon sources other than the three carbon of serine contribute to remethylation under this condition.</jats:p> Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation American Journal of Physiology-Gastrointestinal and Liver Physiology |
| spellingShingle | Townsend, Justin H., Davis, Steven R., Mackey, Amy D., Gregory, Jesse F., American Journal of Physiology-Gastrointestinal and Liver Physiology, Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation, Physiology (medical), Gastroenterology, Hepatology, Physiology |
| title | Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_full | Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_fullStr | Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_full_unstemmed | Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_short | Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_sort | folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| title_unstemmed | Folate deprivation reduces homocysteine remethylation in a human intestinal epithelial cell culture model: role of serine in one-carbon donation |
| topic | Physiology (medical), Gastroenterology, Hepatology, Physiology |
| url | http://dx.doi.org/10.1152/ajpgi.00454.2003 |