A receptor-mediated mechanism to support clinical observation of altered albumin variants [2]

Clinical Chemistry

Volumn 53, Issue 12, 2007, Pages 2216-

  Andersen, Jan Terje ^a   Sandlie, Inger ^a  

^a UNIVERSITY OF OSLO   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 MICROGLOBULIN; FC RECEPTOR; HUMAN SERUM ALBUMIN;

BLOOD FLOW; CARBOXY TERMINAL SEQUENCE; ELECTROPHORESIS; EXON; GENE EXPRESSION; GENE MUTATION; GENETIC POLYMORPHISM; HEAVY CHAIN; LETTER; MUTAGENESIS; PH; PINOCYTOSIS; PROTEIN FUNCTION; WILD TYPE;

ANIMALS; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN G; MUTATION; POLYMORPHISM, GENETIC; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, FC; SERUM ALBUMIN;

EID: 36649020460     PISSN: 00099147     EISSN: None     Source Type: Journal    
DOI: 10.1373/clinchem.2007.097071     Document Type: Letter

References (5)

1. Dolcini L, Caridi G, Dagnino M, Sala A, Gokce S, Sokucu S, et al. Analbuminemia produced by a novel splicing mutation. Clin Chem 2007;53:1549-52.
2. The Albumin Website. http://www.albumin.org (accessed August 2007).
3. Roopenian DC, Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 2007;7:715-25.
4. Anderson CL, Chaudhury C, Kim J, Bronson CL, Wani MA, Mohanty S. Perspective - FcRn transports albumin: relevance to immunology and medicine. Trends Immunol 2006;27:343-8.
5. Andersen JT, Dee Qian J, Sandlie I. The conserved histidine 166 residue of the human neonatal Fc receptor heavy chain is critical for the pH-dependent binding to albumin. Eur J Immunol 2006;36:3044-51.