scholarly journals Iron uptake by human upper small intestine microvillous membrane vesicles. Indication for a facilitated transport mechanism mediated by a membrane iron-binding protein.

1990 ◽  
Vol 86 (6) ◽  
pp. 2145-2153 ◽  
Author(s):  
R Teichmann ◽  
W Stremmel
Blood ◽  
1993 ◽  
Vol 81 (2) ◽  
pp. 517-521 ◽  
Author(s):  
ME Conrad ◽  
JN Umbreit ◽  
RD Peterson ◽  
EG Moore ◽  
KP Harper

Abstract A mechanism for the absorption of inorganic iron in the small intestine is described in which integrins appear to play an important role in the passage of iron across microvillous membranes. Biochemical isolates from microvillous preparations of duodenum from rats dosed with radioiron showed radioactivity concentrated in integrins. The presence of integrins on mucosal surfaces of duodenal cells was confirmed by immunofluorescent microscopy using anti-integrin monoclonal antibodies. Immunoprecipitation methods were used to show that microvillous radioiron was precipitated with anti-integrin antibodies and that mobilferrin, a 56-Kd cytosol iron-binding protein, coprecipitated with integrins. We postulate from these data that the mucosal uptake of iron from the gut lumen is mediated via an integrin-mobilferrin pathway.


Blood ◽  
1992 ◽  
Vol 79 (1) ◽  
pp. 244-247 ◽  
Author(s):  
ME Conrad ◽  
JN Umbreit ◽  
EG Moore ◽  
CR Rodning

Studies were undertaken using human duodenal mucosa to determine whether it contained a counterpart to a newly identified iron-binding protein recently isolated from rat duodenum and named mobilferrin. Water-soluble homogenates were prepared from duodena of patients undergoing surgery for pancreatic carcinoma. An iron-binding protein with an approximate molecular mass of 56 Kd was purified to homogeneity using 60% ammonium sulfate and serial chromatographic steps. The protein was biochemically and immunologically distinct from transferrin and ferritin, and competitively bound to zinc, cobalt, and lead. Each molecule bound one molecule of iron with a kd of 8.9 x 10(-5). Human isolates reacted in an enzyme-linked immunosorbent assay with a polyclonal antibody raised in rabbits against a similar duodenal protein isolated from rat duodenum. It is postulated that mobilferrin plays a significant role in the absorption of iron and other metals and may explain partially the competition between certain metals for absorption in the small intestine.


Blood ◽  
1993 ◽  
Vol 81 (2) ◽  
pp. 517-521 ◽  
Author(s):  
ME Conrad ◽  
JN Umbreit ◽  
RD Peterson ◽  
EG Moore ◽  
KP Harper

A mechanism for the absorption of inorganic iron in the small intestine is described in which integrins appear to play an important role in the passage of iron across microvillous membranes. Biochemical isolates from microvillous preparations of duodenum from rats dosed with radioiron showed radioactivity concentrated in integrins. The presence of integrins on mucosal surfaces of duodenal cells was confirmed by immunofluorescent microscopy using anti-integrin monoclonal antibodies. Immunoprecipitation methods were used to show that microvillous radioiron was precipitated with anti-integrin antibodies and that mobilferrin, a 56-Kd cytosol iron-binding protein, coprecipitated with integrins. We postulate from these data that the mucosal uptake of iron from the gut lumen is mediated via an integrin-mobilferrin pathway.


Blood ◽  
1992 ◽  
Vol 79 (1) ◽  
pp. 244-247 ◽  
Author(s):  
ME Conrad ◽  
JN Umbreit ◽  
EG Moore ◽  
CR Rodning

Abstract Studies were undertaken using human duodenal mucosa to determine whether it contained a counterpart to a newly identified iron-binding protein recently isolated from rat duodenum and named mobilferrin. Water-soluble homogenates were prepared from duodena of patients undergoing surgery for pancreatic carcinoma. An iron-binding protein with an approximate molecular mass of 56 Kd was purified to homogeneity using 60% ammonium sulfate and serial chromatographic steps. The protein was biochemically and immunologically distinct from transferrin and ferritin, and competitively bound to zinc, cobalt, and lead. Each molecule bound one molecule of iron with a kd of 8.9 x 10(-5). Human isolates reacted in an enzyme-linked immunosorbent assay with a polyclonal antibody raised in rabbits against a similar duodenal protein isolated from rat duodenum. It is postulated that mobilferrin plays a significant role in the absorption of iron and other metals and may explain partially the competition between certain metals for absorption in the small intestine.


1973 ◽  
Vol 16 (2) ◽  
pp. 186-190 ◽  
Author(s):  
Robert M Bennett ◽  
A C Eddie-Quartey ◽  
P J L Holt

1947 ◽  
Vol 1 ◽  
pp. 770-776 ◽  
Author(s):  
C.-B Laurell ◽  
B. Ingelman

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