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Gene Review

TFRC  -  transferrin receptor (p90, CD71)

Canis lupus familiaris

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Disease relevance of TFRC

  • PROCEDURE: Concentrations of TR alpha 2, beta 1, and beta 2 mRNA in the myocardium were determined for clinically normal dogs (n = 7) and dogs with heart failure caused by dilated cardiomyopathy (DCM; 7) or chronic valvular disease (CVD; 7) [1].

High impact information on TFRC

  • Early and recycling endosomes were resolved on Optiprep gradients and shown to be differentially associated with rab4, rab11, and transferrin receptor; rab4 was enriched on early endosomes and at least partially depleted from recycling endosomes, with the opposite being true for rab11 and transferrin receptor [2].
  • The endocytosis and recycling of E-cadherin and of the transferrin receptor were similarly inhibited by potassium depletion and by bafilomycin treatment, and both proteins were accumulated in intracellular compartments by an 18 degrees C temperature block, suggesting that endocytosis may occur via a clathrin-mediated pathway [3].
  • The two populations were also pharmacologically distinct, with AlF4 selectively blocking export of transferrin receptor from recycling endosomes to the basolateral plasma membrane [2].
  • At 20 degreesC dIgA-pIgR internalize to interconnected groups of vacuoles and tubules that comprise the endosomal compartment and in which they codistribute with internalized transferrin receptors (TR) and epidermal growth factor receptors (EGFR) [4].
  • We have characterized the polarity of the transferrin receptor in the epithelial Madin-Darby canine kidney (MDCK) cell line [5].

Biological context of TFRC

  • We used the recycling of transferrin receptor in filter-grown MDCK cells to evaluate the accuracy of the sorting of a basolateral protein during endocytosis [5].
  • Here we show that trypanosomes can also adapt to dilute dog serum without switching but by replacing the ESAG7 gene in the 221 ES by one from another ES, by deleting ESAG7 from the 221 ES with concomitant upregulation of transcription of ESAG7 in 'silent' ESs, by grossly overproducing the 221 Tf-R or by combinations of these alterations [6].
  • CONCLUSIONS AND CLINICAL RELEVANCE: Altered regulation of transcription of the TR beta gene may be one facet of the myocardial phenotype in heart failure [1].

Anatomical context of TFRC


Analytical, diagnostic and therapeutic context of TFRC


  1. Upregulation of thyroid hormone receptor beta 1 and beta 2 messenger RNA in the myocardium of dogs with dilated cardiomyopathy or chronic valvular disease. Shahrara, S., Tidholm, A., Drvota, V., Häggstöm, J., Sylvén, C. Am. J. Vet. Res. (1999) [Pubmed]
  2. The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. Sheff, D.R., Daro, E.A., Hull, M., Mellman, I. J. Cell Biol. (1999) [Pubmed]
  3. Recycling of E-cadherin: a potential mechanism for regulating cadherin dynamics. Le, T.L., Yap, A.S., Stow, J.L. J. Cell Biol. (1999) [Pubmed]
  4. Sorting mechanisms regulating membrane protein traffic in the apical transcytotic pathway of polarized MDCK cells. Gibson, A., Futter, C.E., Maxwell, S., Allchin, E.H., Shipman, M., Kraehenbuhl, J.P., Domingo, D., Odorizzi, G., Trowbridge, I.S., Hopkins, C.R. J. Cell Biol. (1998) [Pubmed]
  5. Transferrin receptor polarity and recycling accuracy in "tight" and "leaky" strains of Madin-Darby canine kidney cells. Fuller, S.D., Simons, K. J. Cell Biol. (1986) [Pubmed]
  6. Trypanosomes change their transferrin receptor expression to allow effective uptake of host transferrin. van Luenen, H.G., Kieft, R., Mussmann, R., Engstler, M., ter Riet, B., Borst, P. Mol. Microbiol. (2005) [Pubmed]
  7. Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal. Wang, X., Ma, D., Keski-Oja, J., Pei, D. J. Biol. Chem. (2004) [Pubmed]
  8. Identification of syntenin as a protein of the apical early endocytic compartment in Madin-Darby canine kidney cells. Fialka, I., Steinlein, P., Ahorn, H., Böck, G., Burbelo, P.D., Haberfellner, M., Lottspeich, F., Paiha, K., Pasquali, C., Huber, L.A. J. Biol. Chem. (1999) [Pubmed]
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