title: Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C.
abstract: Human erythrocyte p55 is a peripheral membrane protein that contains three distinct domains in its primary structure: an N-terminal domain, an SH3 motif, and a C-terminal guanylate kinase domain. We used naturally mutated red blood cells (RBCs) with primary genetic defects resulting in the absence of protein 4.1 (4.1[-] hereditary elliptocytosis) or glycophorin C (Leach elliptocytosis). The absence of either protein was associated with the absence of p55. On a stoichiometric basis, the reduction in glycophorin C (about 80%) was concomitant to the lack of p55 in RBCs devoid of protein 4.1. Similarly, the reduction of protein 4.1 (about 20%) was equivalent to the absence of p55 in RBCs devoid of glycophorin C. These correlations suggest that p55 is associated, in precise proportions, with the protein 4.1-glycophorin-C complex, linking the skeleton and the membrane. The protein 4.1-glycophorin-C cross-bridge is known to be critically important for the stability and mechanical properties of human RBC plasma membrane. Because isoforms of protein 4.1, glycophorin C, and p55 exist in many tissues, these results provide evidence of a linkage between the skeleton and the membrane that may have implications in many nonerythroid cells.
authors.affiliation: CNRS URA 1171, Faculté de Médecine Grange-Blanche, Lyon, France.
authors.forename: N
authors.initials: N
authors.lastname: Alloisio
authors.forename: N
authors.initials: N
authors.lastname: Dalla Venezia
authors.forename: A
authors.initials: A
authors.lastname: Rana
authors.forename: K
authors.initials: K
authors.lastname: Andrabi
authors.forename: P
authors.initials: P
authors.lastname: Texier
authors.forename: F
authors.initials: F
authors.lastname: Gilsanz
authors.forename: J P
authors.initials: JP
authors.lastname: Cartron
authors.forename: J
authors.initials: J
authors.lastname: Delaunay
authors.forename: A H
authors.initials: AH
authors.lastname: Chishti
mesh_terms: D001798:Blood Proteins / Q000502:physiology*; D003598:Cytoskeletal Proteins; D004612:Elliptocytosis, Hereditary / Q000097:blood*; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006021:Glycophorins / Q000502:physiology*; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology*; D009479:Neuropeptides
chemical_list: D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D006021:Glycophorins; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1