{"id":1015,"date":"2017-10-27T16:41:54","date_gmt":"2017-10-27T16:41:54","guid":{"rendered":"https:\/\/courses.lumenlearning.com\/suny-nutrition\/?post_type=chapter&#038;p=1015"},"modified":"2017-11-14T17:40:46","modified_gmt":"2017-11-14T17:40:46","slug":"12-71-iron-uptake-absorption","status":"publish","type":"chapter","link":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/chapter\/12-71-iron-uptake-absorption\/","title":{"raw":"12.71 Iron Uptake &amp; Absorption","rendered":"12.71 Iron Uptake &amp; Absorption"},"content":{"raw":"<div class=\"__UNKNOWN__\">\r\n\r\nThere are 2 transporters for iron, one for heme iron and one for non-heme iron. The non-heme transporter is the divalent mineral transporter 1 (DMT1), which transports Fe2+ into the enterocyte. Heme iron is taken up through heme carrier protein 1 (HCP-1), and then metabolized to Fe2+. Fe2+ may be used by enzymes and other proteins or stored in the enterocyte bound to ferritin, the iron storage protein. To reach circulation, iron is transported through ferroportin<sup>1,2<\/sup>. This process is summarized in the figure below.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"970\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163850\/10000000000003CA0000024A0AA9F4EE.png\" alt=\"\" width=\"970\" height=\"586\" \/> Figure 12.711 Iron uptake into the enterocyte[\/caption]\r\n\r\n<\/div>\r\nSince only the reduced form of non-heme iron (Fe2+) is taken up, Fe3+ must be reduced. There is a reductase enzyme on the brush border, duodenal cytochrome b (Dcytb), that catalyzes the reduction of Fe3+ to Fe2+, as shown below. Vitamin C enhances non-heme iron absorption because it is required by Dcytb for this reaction. Thus, if dietary non-heme iron is consumed with vitamin C, more non-heme iron will be reduced to Fe2+ and taken up into the enterocyte through DMT<sup>1<\/sup>.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"512\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163852\/100000000000020000000220E06E2707.png\" alt=\"\" width=\"512\" height=\"544\" \/> Figure 12.712 Reduction of non-heme iron by Dcytb[\/caption]\r\n\r\n<\/div>\r\nIn addition to vitamin C, there is an unidentified factor in muscle that enhances non-heme iron absorption if consumed at the same meal<sup>3<\/sup>. This unidentified factor is referred to as meat protein factor (MPF). The table shows how MPF can increase non-heme iron absorption.\r\n\r\nTable 12.711 Non-heme iron absorption from chicken or beef muscle fraction<sup>3<\/sup>\r\n<table><colgroup> <col \/> <col \/> <col \/> <col \/> <col \/><\/colgroup>\r\n<tbody>\r\n<tr>\r\n<td><b>Mean Fe Absorption \u00a0<\/b>\r\n\r\n<b>(% of Dose)<\/b><\/td>\r\n<td><b>Egg Albumin<\/b><\/td>\r\n<td><b>Whole Muscle<\/b><\/td>\r\n<td><b>Whole Muscle Protein<\/b><\/td>\r\n<td><b>Heme-Free Muscle Protein<\/b><\/td>\r\n<\/tr>\r\n<tr>\r\n<td>Chicken<\/td>\r\n<td>8.41<\/td>\r\n<td>16.43<\/td>\r\n<td>26.98<\/td>\r\n<td>36.81<\/td>\r\n<\/tr>\r\n<tr>\r\n<td>Beef<\/td>\r\n<td>11.21<\/td>\r\n<td>31.52<\/td>\r\n<td>44.15<\/td>\r\n<td>38.29<\/td>\r\n<\/tr>\r\n<\/tbody>\r\n<\/table>\r\nAlbumin is a protein, so the egg albumin represents a non-meat protein standard for comparison. You can see that absorption is much higher with whole muscle. When only consuming muscle protein, there is a slight increase from muscle itself, and when they look at heme-free muscle iron, absorption is still higher than egg albumin<sup>3<\/sup>.\r\n\r\nInhibitors of non-heme iron absorption typically chelate, or bind, the iron to prevent absorption. Phytates (phytic acid), which also inhibit calcium absorption, chelate non-heme iron decreasing its absorption.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"800\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163853\/1000020100000320000001941C095BA8.png\" alt=\"\" width=\"800\" height=\"404\" \/> Figure 12.713 Structure of phytic acid4[\/caption]\r\n\r\n<\/div>\r\nOther compounds that inhibit absorption are:\r\n\r\nPolyphenols (coffee, tea)<sup>1<\/sup>\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"208\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163855\/10000201000000D0000000D1996100A3.png\" alt=\"\" width=\"208\" height=\"209\" \/> Figure 12.714 Structure of gallic acid, a polyphenol<sup>5<\/sup>[\/caption]\r\n\r\n<\/div>\r\nOxalate (spinach, rhubarb, sweet potatoes, and dried beans)<sup>2<\/sup>\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"304\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163855\/10000000000001300000014CF5304467.png\" alt=\"\" width=\"304\" height=\"332\" \/> Figure 12.715 Structure of calcium oxalate<sup>6<\/sup>[\/caption]\r\n\r\n<\/div>\r\nCalcium is also believed to inhibit iron uptake.\r\n\r\n<b>References &amp; Links<\/b>\r\n\r\n1. Gropper SS, Smith JL, Groff JL. (2008) Advanced nutrition and human metabolism. Belmont, CA: Wadsworth Publishing.\r\n\r\n2. Shils ME, Shike M, Ross AC, Caballero B, Cousins RJ, editors. (2006) Modern nutrition in health and disease. Baltimore, MD: Lippincott Williams &amp; Wilkins.\r\n\r\n3. Hurrell R, Reddy M, Juillerat M, Cook J. (2006) Meat protein fractions enhance nonheme iron absorption in humans. J Nutr 136(11): 2808-2812.\r\n\r\n4. http:\/\/en.wikipedia.org\/wiki\/File:Phytic_acid.png\r\n\r\n5. http:\/\/en.wikipedia.org\/wiki\/File:Gallic_acid.svg\r\n\r\n6. http:\/\/en.wikipedia.org\/wiki\/File:Calcium_oxalate.png\r\n\r\n<\/div>","rendered":"<div class=\"__UNKNOWN__\">\n<p>There are 2 transporters for iron, one for heme iron and one for non-heme iron. The non-heme transporter is the divalent mineral transporter 1 (DMT1), which transports Fe2+ into the enterocyte. Heme iron is taken up through heme carrier protein 1 (HCP-1), and then metabolized to Fe2+. Fe2+ may be used by enzymes and other proteins or stored in the enterocyte bound to ferritin, the iron storage protein. To reach circulation, iron is transported through ferroportin<sup>1,2<\/sup>. This process is summarized in the figure below.<\/p>\n<div>\n<div style=\"width: 980px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163850\/10000000000003CA0000024A0AA9F4EE.png\" alt=\"\" width=\"970\" height=\"586\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.711 Iron uptake into the enterocyte<\/p>\n<\/div>\n<\/div>\n<p>Since only the reduced form of non-heme iron (Fe2+) is taken up, Fe3+ must be reduced. There is a reductase enzyme on the brush border, duodenal cytochrome b (Dcytb), that catalyzes the reduction of Fe3+ to Fe2+, as shown below. Vitamin C enhances non-heme iron absorption because it is required by Dcytb for this reaction. Thus, if dietary non-heme iron is consumed with vitamin C, more non-heme iron will be reduced to Fe2+ and taken up into the enterocyte through DMT<sup>1<\/sup>.<\/p>\n<div>\n<div style=\"width: 522px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163852\/100000000000020000000220E06E2707.png\" alt=\"\" width=\"512\" height=\"544\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.712 Reduction of non-heme iron by Dcytb<\/p>\n<\/div>\n<\/div>\n<p>In addition to vitamin C, there is an unidentified factor in muscle that enhances non-heme iron absorption if consumed at the same meal<sup>3<\/sup>. This unidentified factor is referred to as meat protein factor (MPF). The table shows how MPF can increase non-heme iron absorption.<\/p>\n<p>Table 12.711 Non-heme iron absorption from chicken or beef muscle fraction<sup>3<\/sup><\/p>\n<table>\n<colgroup>\n<col \/>\n<col \/>\n<col \/>\n<col \/>\n<col \/><\/colgroup>\n<tbody>\n<tr>\n<td><b>Mean Fe Absorption \u00a0<\/b><\/p>\n<p><b>(% of Dose)<\/b><\/td>\n<td><b>Egg Albumin<\/b><\/td>\n<td><b>Whole Muscle<\/b><\/td>\n<td><b>Whole Muscle Protein<\/b><\/td>\n<td><b>Heme-Free Muscle Protein<\/b><\/td>\n<\/tr>\n<tr>\n<td>Chicken<\/td>\n<td>8.41<\/td>\n<td>16.43<\/td>\n<td>26.98<\/td>\n<td>36.81<\/td>\n<\/tr>\n<tr>\n<td>Beef<\/td>\n<td>11.21<\/td>\n<td>31.52<\/td>\n<td>44.15<\/td>\n<td>38.29<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p>Albumin is a protein, so the egg albumin represents a non-meat protein standard for comparison. You can see that absorption is much higher with whole muscle. When only consuming muscle protein, there is a slight increase from muscle itself, and when they look at heme-free muscle iron, absorption is still higher than egg albumin<sup>3<\/sup>.<\/p>\n<p>Inhibitors of non-heme iron absorption typically chelate, or bind, the iron to prevent absorption. Phytates (phytic acid), which also inhibit calcium absorption, chelate non-heme iron decreasing its absorption.<\/p>\n<div>\n<div style=\"width: 810px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163853\/1000020100000320000001941C095BA8.png\" alt=\"\" width=\"800\" height=\"404\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.713 Structure of phytic acid4<\/p>\n<\/div>\n<\/div>\n<p>Other compounds that inhibit absorption are:<\/p>\n<p>Polyphenols (coffee, tea)<sup>1<\/sup><\/p>\n<div>\n<div style=\"width: 218px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163855\/10000201000000D0000000D1996100A3.png\" alt=\"\" width=\"208\" height=\"209\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.714 Structure of gallic acid, a polyphenol<sup>5<\/sup><\/p>\n<\/div>\n<\/div>\n<p>Oxalate (spinach, rhubarb, sweet potatoes, and dried beans)<sup>2<\/sup><\/p>\n<div>\n<div style=\"width: 314px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27163855\/10000000000001300000014CF5304467.png\" alt=\"\" width=\"304\" height=\"332\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.715 Structure of calcium oxalate<sup>6<\/sup><\/p>\n<\/div>\n<\/div>\n<p>Calcium is also believed to inhibit iron uptake.<\/p>\n<p><b>References &amp; Links<\/b><\/p>\n<p>1. Gropper SS, Smith JL, Groff JL. (2008) Advanced nutrition and human metabolism. Belmont, CA: Wadsworth Publishing.<\/p>\n<p>2. Shils ME, Shike M, Ross AC, Caballero B, Cousins RJ, editors. (2006) Modern nutrition in health and disease. Baltimore, MD: Lippincott Williams &amp; Wilkins.<\/p>\n<p>3. Hurrell R, Reddy M, Juillerat M, Cook J. (2006) Meat protein fractions enhance nonheme iron absorption in humans. J Nutr 136(11): 2808-2812.<\/p>\n<p>4. http:\/\/en.wikipedia.org\/wiki\/File:Phytic_acid.png<\/p>\n<p>5. http:\/\/en.wikipedia.org\/wiki\/File:Gallic_acid.svg<\/p>\n<p>6. http:\/\/en.wikipedia.org\/wiki\/File:Calcium_oxalate.png<\/p>\n<\/div>\n\n\t\t\t <section class=\"citations-section\" role=\"contentinfo\">\n\t\t\t <h3>Candela Citations<\/h3>\n\t\t\t\t\t <div>\n\t\t\t\t\t\t <div id=\"citation-list-1015\">\n\t\t\t\t\t\t\t <div class=\"licensing\"><div class=\"license-attribution-dropdown-subheading\">CC licensed content, Shared previously<\/div><ul class=\"citation-list\"><li>Kansas State University Human Nutrition Flexbook. <strong>Authored by<\/strong>: Brian Lindshield. <strong>Provided by<\/strong>: Kansas State University. <strong>Located at<\/strong>: <a target=\"_blank\" href=\"http:\/\/goo.gl\/vOAnR\">http:\/\/goo.gl\/vOAnR<\/a>. <strong>License<\/strong>: <em><a target=\"_blank\" rel=\"license\" href=\"https:\/\/creativecommons.org\/licenses\/by\/4.0\/\">CC BY: Attribution<\/a><\/em><\/li><\/ul><\/div>\n\t\t\t\t\t\t <\/div>\n\t\t\t\t\t <\/div>\n\t\t\t <\/section>","protected":false},"author":311,"menu_order":27,"template":"","meta":{"_candela_citation":"[{\"type\":\"cc\",\"description\":\"Kansas State University Human Nutrition Flexbook\",\"author\":\"Brian Lindshield\",\"organization\":\"Kansas State University\",\"url\":\"goo.gl\/vOAnR\",\"project\":\"\",\"license\":\"cc-by\",\"license_terms\":\"\"}]","CANDELA_OUTCOMES_GUID":"","pb_show_title":"on","pb_short_title":"","pb_subtitle":"","pb_authors":[],"pb_section_license":""},"chapter-type":[],"contributor":[],"license":[],"class_list":["post-1015","chapter","type-chapter","status-publish","hentry"],"part":883,"_links":{"self":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1015","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters"}],"about":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/types\/chapter"}],"author":[{"embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/users\/311"}],"version-history":[{"count":4,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1015\/revisions"}],"predecessor-version":[{"id":1845,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1015\/revisions\/1845"}],"part":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/parts\/883"}],"metadata":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapters\/1015\/metadata\/"}],"wp:attachment":[{"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/media?parent=1015"}],"wp:term":[{"taxonomy":"chapter-type","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/pressbooks\/v2\/chapter-type?post=1015"},{"taxonomy":"contributor","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/contributor?post=1015"},{"taxonomy":"license","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/suny-herkimer-nutritionflex\/wp-json\/wp\/v2\/license?post=1015"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}