Hereditary stomatocytosis: consistent association with an integral membrane protein deficiency

Eber, Stefan; Lande, William M.; Iarocci, T. A.; Mentzer, William C.; Höhn, Patrick; Wiley, James S.; Schröter, W.

doi:10.1111/j.1365-2141.1989.tb07731.x

Cited by 45 publications

(15 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, this topography has not been directly demonstrated. Importantly, mutations leading to the absence of stomatin result in osmotically fragile cells with increased cation fluxes and elevated intracellular sodium concentrations [65–68]. Moreover, observations that Milan hypertensive rats, which carry a mutation in both β and α adducin genes, also display increased erythrocyte cation fluxes [69] have suggested that regulation of cation transport may depend on an interaction between adducin and stomatin.…”

Section: Protein Interactions Of Erythrocyte Adducinmentioning

confidence: 99%

Erythrocyte adducin: A structural regulator of the red blood cell membrane

Franco

Low

2010

Transfusion Clinique et Biologique

View full text Add to dashboard Cite

Adducin is an α, β heterotetramer that performs multiple important functions in the human erythrocyte membrane. First, adducin forms a bridge that connects the spectrin–actin junctional complex to band 3, the major membrane-spanning protein in the bilayer. Rupture of this bridge leads to membrane instability and spontaneous fragmentation. Second, adducin caps the fast growing (barbed) end of actin filaments, preventing the tetradecameric protofilaments from elongating into macroscopic F-actin microfilaments. Third, adducin stabilizes the association between actin and spectrin, assuring that the junctional complex remains intact during the mechanical distortions experienced by the circulating cell. And finally, adducin responds to stimuli that may be important in regulating the global properties of the cell, possibly including cation transport, cell morphology and membrane deformability. The text below summarizes the structural properties of adducin, its multiple functions in erythrocytes, and the consequences of engineered deletions of each of adducin subunits in transgenic mice.

show abstract

Section: Protein Interactions Of Erythrocyte Adducinmentioning

confidence: 99%

Erythrocyte adducin: A structural regulator of the red blood cell membrane

Franco

Low

2010

Transfusion Clinique et Biologique

View full text Add to dashboard Cite

show abstract

“…This leak can be "plugged" by treatment of the cells with the cross-linker dimethyl adipimate (327), strongly suggesting that a transmembrane protein channel is responsible for this leak. Hereditary stomatocytosis patients have no detectable levels of the stomatin protein in their red cells (129,263). Thus, the absence of stomatin appears to correlate with a transmembrane cation link, suggesting the stomatin is a regulator of some ion channel.…”

Section: Stomatinmentioning

confidence: 99%

Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton

Morrow

Rimm

Kennedy

et al. 1997

Comprehensive Physiology

View full text Add to dashboard Cite

The sections in this article are: The Red Cell Membrane Skeleton How Does the Spectrin Membrane Skeleton Stabilize the Red Cell? The Trilayer Couple—Spectrin as A Membrane Organizer Components of the Erythrocyte Membrane Skeleton Spectrin Actin Ankyrin Protein 4.1 Adducin Dematin (Protein 4.9) Pallidin (Protein 4.2) p55 (an Erythrocyte Membrane‐Associated Guanylate Kinase) Stomatin Tropomyosin and Tropomodulin Dynamin Interactions with Phospholipids The Spectrin Skeleton of Non‐Erythroid Cells Spatial and Temporal Polarization Proteins Interacting with Spectrin in Non‐Erythroid Cells Cytoskeletal Elements Adhesion Proteins Evolving Concepts Conclusions: The Linked Mosaic Model

show abstract

“…Attention was drawn to the protein by its absence from the red cell membrane in the dominantly-inherited haemolytic anaemia, hereditary stomatocytosis, in which the red cells show a catastrophic leak to the univalent cations Na+ and K+ (Lock et al 1961;Lande et al 1982;Eber et al 1989;Stewart and Turner 1999;Stewart and Fricke 2003). However, the stomatin gene is not mutated in this condition, and this anaemia does not represent the phenotype of a human stomatin 'knock out' (Wang et al 1992.…”

Section: Introductionmentioning

confidence: 98%

Stomatin immunoreactivity in ciliated cells of the human airway epithelium

Fricke

Stewart

Treharne

et al. 2003

Anatomy and Embryology

View full text Add to dashboard Cite

Stomatin is a widely distributed 32kD membrane protein of unknown function. In biochemical studies it is associated with cholesterol+sphingomyelin-rich 'rafts' in the cytomembrane. Genetic studies in C. elegans, supported by microscopic studies in mammalian tissue and co-expression studies in oocytes, suggest a functional link with the DEG/ENaC (degenerin/epithelial Na+ channel) superfamily of monovalent ion channels. Since ENaC channels play a prominent role in the physiology of the respiratory epithelium, we have studied the immunolocalization of stomatin in mature and developing human airway epithelium by means of Western blot analysis, immunocytochemistry, and immunoelectron microscopy. Stomatin immunoreactivity (stomatin-IR) was found in the ciliated cells of the conductive airway epithelium in a distinct distribution pattern with the strongest signal along the cilia. Immunogold labelling revealed immunogold particles at the basal bodies, along the cilia, and at the membrane of the microvilli. The presence of stomatin-IR paralleled the stages of ciliogenesis in airway development, and its appearance preceded the elongation of the axoneme and the cilial outgrowth. Due to its presence in the different cellular locations in the ciliated cell, we suggest that stomatin is involved in various cellular functions. From its ultrastructural position, stomatin could be a candidate for a membrane-associated mechanotransducer with a role in the control of ciliary motility. Stomatin as a raft protein might be a microtubule associated protein moving along the outer surface of the microtubules to its terminal site of action in the cilia. Stomatin-IR in microvilli supports the hypothesis of a co-localization with beta- and gamma- ENaC and, in conclusion, their potential functional interaction to control the composition of periciliary mucus electrolytes.

show abstract

Hereditary stomatocytosis: consistent association with an integral membrane protein deficiency

Cited by 45 publications

References 14 publications

Erythrocyte adducin: A structural regulator of the red blood cell membrane

Erythrocyte adducin: A structural regulator of the red blood cell membrane

Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton

Stomatin immunoreactivity in ciliated cells of the human airway epithelium

Contact Info

Product

Resources

About