The red cell membrane is often used as a model of other biological membranes, since i) it is abundantly available in highly purified form, ii) it can be obtained from humans without harming the donor, iii) its structure is comparatively simple, iv) the major components are found in virtually all animal cell plasma membranes, and v) pathological lesions arising in other cell membranes are often manifested in the red cell (e.g. diabetes, muscular dystrophy, etc.). For this reason, a thorough understanding of the structure and regulation of the red cell membrane may be a logical stepping stone to unraveling the molecular bases of health problems affecting other cell membranes. We are seeking to elucidate the structure, regulation, biological functions, and pathological states of interactions involving the major membrane protein, termed band 3. Specifically we intend to i) examine the regulation of the association of band 3 with ankyrin (the major linkage between the cytoskeleton and the membrane), ii) characterize the interaction between band 3 and band 4.1, a second major cytoskeletal protein, iii) study the regulation of membrane- cytoskeletal interactions during cell swelling and shrinking, and iv) confirm our mechanisms which explains how the body distinguishes old from young red cells and selectively destroys the former. Research on this letter topic may provide clues for extending the life of stored blood. Research on the former projects should aid in understanding and eventually treating such diseases as sickle cell anemia, hereditary spherocytosis, hereditary elliptocytosis, and hereditary pyropoikilocytosis, as well as maladies of nonerythroid cells. Methods used to investigate the above issues involve predominately protein chemistry, with contributions from immunology and molecular biology.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM024417-15
Application #
2174256
Study Section
Hematology Subcommittee 2 (HEM)
Project Start
1977-07-01
Project End
1995-03-31
Budget Start
1994-04-01
Budget End
1995-03-31
Support Year
15
Fiscal Year
1994
Total Cost
Indirect Cost
Name
Purdue University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907
Giger, Katie; Habib, Ibrahim; Ritchie, Ken et al. (2016) Diffusion of glycophorin A in human erythrocytes. Biochim Biophys Acta 1858:2839-2845
Puchulu-Campanella, Estela; Turrini, Francesco M; Li, Yen-Hsing et al. (2016) Global transformation of erythrocyte properties via engagement of an SH2-like sequence in band 3. Proc Natl Acad Sci U S A 113:13732-13737
Franco, Taina; Chu, Haiyan; Low, Philip S (2016) Identification of adducin-binding residues on the cytoplasmic domain of erythrocyte membrane protein, band 3. Biochem J 473:3147-58
Wandersee, Nancy J; Maciaszek, Jamie L; Giger, Katie M et al. (2015) Dietary supplementation with docosahexanoic acid (DHA) increases red blood cell membrane flexibility in mice with sickle cell disease. Blood Cells Mol Dis 54:183-8
Sega, Martiana F; Chu, Haiyan; Christian, John A et al. (2015) Fluorescence assay of the interaction between hemoglobin and the cytoplasmic domain of erythrocyte membrane band 3. Blood Cells Mol Dis 55:266-71
Stefanovic, Marko; Puchulu-Campanella, Estela; Kodippili, Gayani et al. (2013) Oxygen regulates the band 3-ankyrin bridge in the human erythrocyte membrane. Biochem J 449:143-50
Puchulu-Campanella, Estela; Chu, Haiyan; Anstee, David J et al. (2013) Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane. J Biol Chem 288:848-58
Fernandez-Pol, Sebastian; Slouka, Zdenek; Bhattacharjee, Souvik et al. (2013) A bacterial phosphatase-like enzyme of the malaria parasite Plasmodium falciparum possesses tyrosine phosphatase activity and is implicated in the regulation of band 3 dynamics during parasite invasion. Eukaryot Cell 12:1179-91
Franco, Robert S; Puchulu-Campanella, M Estela; Barber, Latorya A et al. (2013) Changes in the properties of normal human red blood cells during in vivo aging. Am J Hematol 88:44-51
Sega, Martiana F; Chu, Haiyan; Christian, John et al. (2012) Interaction of deoxyhemoglobin with the cytoplasmic domain of murine erythrocyte band 3. Biochemistry 51:3264-72

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