Board Member Profile

Douglas M. Fambrough

Professor Emeritus
Department of Biology
The Johns Hopkins University
411 Range Road
Baltimore, MD 21204
Voice: 410-842-7477
Email: fambro@jhu.edu
Scientific Director, Searle Scholars Program

Research Interests

The Fambrough lab at The Johns Hopkins University closed its doors in 2004. In the years just prior to that, Dr. Fambrough's research group studied the mechanisms by which cells regulate the number and spatial distribution of their membrane proteins, focusing upon integral membrane proteins that come to reside in the lysosomal membrane (LAMP-1and LAMP 2), the sarcoplasmic reticulum (Ca-ATPase), and the plasma membrane (Na,K-ATPase). The lab cloned encoding DNAs for each of these proteins from avian cDNA libraries and expressed these DNAs in tissue cultured mammalian cells, where each avian protein was correctly sorted and localized. Monoclonal antibodies specific for each avian protein were developed and used to quantify expression and to determine cellular distribution. Sorting signals and, for the Na,K-ATPase the sites for inter-subunit interaction, were mapped and further defined.

The monoclonal antibodies to these membrane proteins have been donated to the Developmental Studies Hybridoma Bank, a non-profit center for distribution of hybridoma cells and antibodies. To obtain antibodies, contact the center at:

http://dshb.biology.uiowa.edu

Monoclonal antibodies to a variety of extracellular matrix proteins and to human acetylcholinesterase were also developed and given to the Developmental Studies Hybridoma Bank.

Representative Publications

Na,K- and Ca-ATPases

  1. Campbell, A.M., Kessler, P.D. and Fambrough, D.M. 1992. The alternate carboxyl termini of avian cardiac and brain SR/ER Ca-ATPases are on opposite sides of the membrane. J. Biol. Chem. 267, 9321-9325.
  2. Hamrick, M., K. J. Renaud and D. M. Fambrough. 1993. Assembly of the extracellular domain of the Na,K-ATPase b subunit with the a subunit. Analysis of b subunit chimeras and carboxyl-terminal deletions. J. Biol. Chem., 268: 24367-24373.
  3. Campbell, A. M., F. Wuytack and D. M. Fambrough. 1993. Differential distribution of the alternative forms of the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase, SERCA2b and SERCA2a, in the avian brain. Brain Res. 605: 67-76.
  4. Takeyasu, K., M. Hamrick, A. M. Barnstein, and D. M. Fambrough. 1993. Structural analysis and expression of a chromosomal gene encoding an avian (Na+ + K+)- ATPase b1-subunit. Biochim. Biophys. Acta. 1172: 212-216.
  5. Lemas, M. V. and D. M. Fambrough. 1993. Sequence analysis of DNA encoding an avian Na+,K+-ATPase b2-subunit. Biochim. Biophys. Acta 1149: 339-342.
  6. Geering, K., P. Jaunin, F. Jaisser, A. M. Merillat, J. D. Horisberger, P. M. Mathews, V. Lemas, D. M. Fambrough and B. C. Rossier. 1993. Mutation of a conserved proline residue in the b-subunit ectodomain prevents Na,K-ATPase oligomerization. Am. J. Physiol., 265: C1169-C1174.
  7. Sumbilla, C., L. Lu, D. Lewis, G. Inesi, T. Ishii, K. Takeyasu, Y. Feng and D. M. Fambrough. 1993. Ca2+ dependence and thapsigargin inhibited phosphorylation of Na,K-ATPase catalytic domain following chimeric recombination with the Ca2+-ATPase. J. Biol. Chem., 268: 21185- 21190.
  8. Emerick, M.C. and Fambrough, D. M. 1993. Intramolecular fusion of Na pump subunits assures exclusive assembly of the fused a and b subunit domains into a functional enzyme in cells also expressing endogenous Na pump subunits. J. Biol. Chem. 268, 23455-23459.
  9. Lemas, M. V., Hamrick, M., Takeyasu, K and Fambrough, D. M. 1994. 26 Amnino acids of an extracellular domain of the Na,K-ATPase a-subunit are sufficient for assembly with the Na,K-ATPase b-subunit. J. Biol. Chem. 269, 8255-8259.
  10. Song, Y. and D. M. Fambrough. 1994. Molecular evolution of the calcium-transporting ATPases analyzed by the maximum parsimony method. In "Molecular Evolution of Physiological Processes" (D. M. Fambrough, ed.) Rockefeller University Press, N.Y., pp. 271-283.
  11. Lemas, M. V., H.-Y. Lu, K. Takeyasu, B. Kone and D. M. Fambrough. 1994. Assembly of the Na,K-ATPase a-subunit isoforms with the Na,K- and H,K-ATPase b-subunit isoforms. J. Biol. Chem., 269: 18651-18655.
  12. Fambrough, D.M., Lemas, M.V., Hamrick, M., Emerick, M., Renaud, K.J., & Inman, E.M., Hwang, B. and Takeyasu, K. 1994. Analysis of subunit assembly of the Na-K-ATPase. Am. J. Physiol. 266, C579-C589.
  13. Schubiger, M., Feng, Y., Fambrough, D. M. and Palka, J.1994. A mutation of the Drosophila sodium pump a-subunit gene results in bang-sensitive paralysis. Neuron 12, 373-381.
  14. Davis, M.W., Somerville, D., Lee, R.Y.N., Lockery, S., Avery, L. and Fambrough, D.M. 1995. Mutations in the Caenorhabditis elegans Na,K-ATPase a-subunit gene, eat-6, disrupt excitable cell function. J. Neuroscience 15, 8408-8418.
  15. Fambrough, D.M. and G. Inesi. 1996. Cation Transport ATPases. In "Molecular Biology of Membrane Disorders" (S. Schultz et al., Editors) Plenum Press. pp 223-241.
  16. Yu, H.-Y., S. Nettikadan, D.M. Fambrough and K. Takeyasu. 1996. Negative transcriptional regulation of the chicken Na+/K+-ATPase a1 subunit gene. Biochim. Biophys. Acta 1309: 239-252.
  17. Kaprielian, Z., S. W. Robinson, D.M. Fambrough and P.D. Kessler. 1996. Movement of Ca2+-ATPase molecules within the sarcoplasmic/endoplasmic reticulum in skeletal muscle. J. Cell Sci. 109: 2529-2537.
  18. Ishii, T., F. Hata, M.V. Lemas, D.M. Fambrough and K. Takeyasu. 1997. Carboxy-terminal regions of the SERCA- and Na+/K+-ATPases control their K+-selectivity. Biochemistry 36: 442-451.
  19. Colonna, T., M. Kostich, M. Hamrick, B. Hwang, J.D. Rawn and D. M. Fambrough 1997. Subunit Interactions in the Sodium Pump. Ann. N.Y. Acad. Sci. 834: 498-513.
  20. Colonna, T. L. Huynh, and D. M. Fambrough. 1997. Subunit interactions in the Na,K-ATPase explored with the yeast two-hybrid system. J. Biol. Chem. 272: 12366-12372
  21. Feng, Y., L. Huynh, K. Takeyasu, and D. M. Fambrough. 1997. The Drosophila Na, K-ATPase a-subunit gene: gene structure, promoter function, and analysis of a cold-sensitive recessive lethal mutation. Genes and Function 1: 91-116.
  22. Zhou, X. and D. M. Fambrough. 1999. Expression of the avian Na,K-ATPase subunits in Dictyostelium discoideum. J. Membrane Biol 167: 19-24.
  23. Wilson, P.D., Devuyst, O., Gatti, L., Falkenstein, D., Robinson, S. and D. M. Fambrough. 2000. Apical plasma membrane mispolarization of NaK-ATPase in polycystic kidneydisease epithelia is associated with aberrant expressionof the beta-2 isoform. Am. J. Pathol. 156: 1-16.
  24. Fambrough, D., Huynh, H.L. and Hwang, B. 2000. The Na,K-ATPase alpha-beta subunit assembly site. In Na/K-ATPase and Related ATPases. 9th International Conference on Na/K Pump and Related Pumps (K. Taniguchi and S. Kaya, eds.) Elsevier, Amsterdam, pp 103-106.
  25. Okamura, H., Yasuhara, J.C., Fambrough, D.M., and Takeyasu, K. 2003. P-type ATPases in Caenorhabditis and Drosophila: Implications for evolution of the P-type ATPase subunit families with special reference to the Na,K-ATPase and H,K-ATPase subgroup. J. Memb. Biol. 191 (in press for Jan issue)

Lysosome-Associated Membrane Proteins

  1. Mathews, P. M., J. B. Martinie, and D. M. Fambrough. 1992. The pathway and targeting signal for delivery of the integral membrane glycoprotein LEP100 to lysosomes. J. Cell Biol., 118: 1027-1040.
  2. Hatem, C.L., Gough, N.R. and Fambrough, D.M. 1995. Multiple mRNAs encode the avian lysosomal membrane protein LAMP-2, resulting in alternative transmembrane and cytoplasmic domains. J. Cell Sci. 108, 2093-2100.
  3. Gough, N.R., C. L. Hatem, and D.M. Fambrough. 1995. The family of LAMP-2 proteins arise by alternative splicing from a single gene. Characterization of the avian LAMP-2 gene and identification of mammalian homologs of LAMP-2b and LAMP-2c. DNA and Cell Biology. 14: 863-867.
  4. Gough, N.R. and D.M. Fambrough. 1997. The different cytoplasmic domains of avian LAMP-2a,b and c confer different cellular distributions to chimeric LAMP-1/LAMP-2 proteins. J. Cell Biol. 137: 1161-1169.
  5. Gough, N.R., M.E. Zweifel, O. Martinez-Augustin, R.C. Aguilar, J.S. Bonifacino and D.M. Fambrough. 1999. Utilization of the indirect lysosome targeting pathway by lysosome-associated membrane proteins (LAMPs) is influenced largely by the C-terminal residue of their GYXX[hydrophobe] targeting signals. J. Cell Sci.: 4257-4269.
  6. Kostich, M., Fire, A. and Fambrough, D.M. 2000. Identification and molecular-genetic characterization of a LAMP/CD68-like protein from Caenorhabditis elegans. J. Cell Biol. 113: 2595-2606.

Major Earlier Publications

HISTONES:

  1. Fambrough, D. M. and J. Bonner. 1966. On similarity of plant and animal histones. Biochemistry 5: 2563-2570.
  2. Fambrough, D. M. and J. Bonner. 1968. Sequence homology and role of cysteine in plant and animal arginine-rich histones. J. Biol. Chem. 243: 4434-4439.
  3. DeLange, R. J., D. M. Fambrough, E. Smith and J. Bonner. 1968. Calf and pea histone IV. I. Amino acid compositions and the identical COOH-terminal 19-residue sequence. J. Biol. Chem. 243: 5906-5913.
  4. Bonner, J., M. E. Dahmus, D. M. Fambrough, R. C. Huang, K. Marushige and D. Y. Tuan. 1968. The biology of isolated chromatin. Science 159: 47-53.
  5. DeLange, R., J., D. M. Fambrough, E. Smith and J. Bonner. 1969. Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine. J. Biol. Chem. 244: 319-334.
  6. DeLange, R. J., D. M. Fambrough, E. Smith and J. Bonner. 1969. Calf and pea histone IV. III. Complete amino acid sequence of pea seedling histone IV; comparison with the homologous calf thymus histone. J. Biol. Chem. 244: 5669- 5679.

ACETYLCHOLINE RECEPTORS AND NEUROMUSCULAR JUNCTIONS:

  1. Fambrough, D. M. 1970. Acetylcholine sensitivity of muscle fiber membranes: mechanism of regulation by motoneurons. 1970. Science 168: 372-373.
  2. Fambrough, D. M. and J. E. Rash. 1971. Development of acetylcholine sensitivity during myogenesis. Devel. Biol. 26: 55-68.
  3. Fambrough, D. M. and H. C. Hartzell. 1972. Acetylcholine receptors: number and distribution at neuromuscular junctions in rat diaphragm. Science 176: 189-191.
  4. Hartzell, H. C. and D. M. Fambrough. 1972. Acetylcholine receptors: distribution and extrajunctional density in rat diaphragm after denervation correlated with acetylcholine sensitivity. J. Gen. Physiol. 60: 248-262.
  5. Hartzell, H. C. and D. M. Fambrough. 1972. Acetylcholine receptors production and incorporation into membranes of developing muscle fibers. Devel. Biol. 30: 153-165.
  6. Fambrough, D. M., D. B. Drachman and S. Satyamurti. 1973. Neuromuscular junction in myasthenia gravis: decreased acetylcholine receptors. Science 182: 293-295.
  7. Devreotes, P. N. and D. M. Fambrough. 1975. Acetylcholine receptor turnover in membranes of developing muscle fibers. J. Cell Biol. 65: 335-358.
  8. Ritchie, A. K. and D. M. Fambrough. 1975. Ionic properties of the acetylcholine receptor in cultured rat myotubes. J. Gen. Physiol. 65: 751-767.
  9. Ritchie, A. K. and D. M. Fambrough. 1975. Electrophysiological properties of the membrane and acetylcholine receptor in developing rat and chick myotubes. J. Gen. Physiol. 66: 327-355.
  10. Devreotes, P. N. and D. M. Fambrough. 1976. Synthesis of acetylcholine receptors by cultured chick myotubes and denervated mouse extensor digitorum longus muscles. Proc. Natl. Acad. Sci. U.S.A. 73: 161-164.
  11. Devreotes, P. N. and D. M. Fambrough. 1976. Turnover of acetylcholine receptors in skeletal muscle. Cold Spring Harbor Symp. Quant. Biol. 40: 237-251.
  12. Devreotes, P. N., J. M. Gardner and D. M. Fambrough. 1977. Kinetics of biosynthesis of acetylcholine receptor and subsequent incorporation into plasma membrane of cultured chick skeletal muscle. Cell. 10: 365-373.
  13. Fambrough, D. M. and P. N. Devreotes. 1978. Newly synthesized acetylcholine receptors are located in the Golgi apparatus. J. Cell Biol. 76: 237-244.
  14. Carbonetto, S. T., D. M. Fambrough and K. J. Muller. 1978. Nonequivalence of a- bungarotoxin receptors and acetyolcholine receptors in chick sympathetic neurons. Proc. Natl. Acad. Sci. U.S.A. 75: 1016-1020.
  15. Gardner, J. M. and D. M. Fambrough. 1979. Acetylcholine receptor degradation measured by density labeling: effect of cholinergic ligands and evidence against recycling. Cell 16: 661-674.
  16. Linden, D. C. and D. M. Fambrough. 1979. Biosynthesis and degradation of acetylcholine receptors in rat skeletal muscle. Effects of electrical stimulation. Neuroscience 4: 527-538.
  17. Carbonetto, S. T. and D. M. Fambrough. 1979. Synthesis, insertion into the plasma membrane and turnover of a-bungarotoxin receptors in chick sympathetic neurons. J. Cell Biol. 81: 555-569.
  18. Fambrough, D. M. 1979. Control of acetylcholine receptors in skeletal muscle. Physiol. Rev. 59: 165-227.
  19. Pumplin, D. W. and D. M. Fambrough. 1982. Turnover of acetylcholine receptors in skeletal muscle. Ann. Rev. Physiol. 44: 319-335.
  20. Anderson, M. J. and D. M. Fambrough. 1983. Aggregates of acetylcholine receptors are associated with plaques of a basal lamina heparan sulfate proteoglycan on the surface of skeletal muscle fibers. J. Cell Biol. 97: 1396-1411.

ACETYLCHOLINESTERASE

  1. Rotundo, R. L. and D. M. Fambrough. 1979. Molecular forms of chicken embryo acetylcholinesterase in vitro and in vivo: isolation and characterization. J. Biol. Chem. 254: 4790-4799.
  2. Rotundo, R. L. and D. M. Fambrough. 1980. Synthesis, transport and fate of acetylcholinesterase in cultured chick embryo muscle cells. Cell 22: 583-594.
  3. Rotundo, R. L. and D. M. Fambrough. 1980. Secretion of acetylcholinesterase; relation to acetylcholine receptor metabolism. Cell 22: 595-602.
  4. Fambrough, D. M., A. G. Engel and T. L. Rosenberry. 1982. Acetylcholinesterase of human erythrocytes and neuromuscular junctions: homologies revealed by monoclonal antibodies. Proc. Natl. Acad. Sci. U.S.A. 79: 1078-1082.
  5. Hedreen, J. C., G. R. Uhl, S. J. Bacon, D. M. Fambrough and D. L. Price. 1984. Acetylcholinesterase immunoreactive axonal network in monkey visual cortex. J. Comp. Neurol. 226: 246 254.
  6. Rotundo, R. L. and D. M. Fambrough. 1986. Function and molecular structure of acetylcholinesterase. In Myology (A. G. Engel and B. Q. Banker, eds.) McGraw Hill Book Co., New York. pp. 791-810.

EXTRACELLULAR MATRIX

  1. Chiquet, M. and D. M. Fambrough. 1983. Cellular origin of extracellular matrix components during muscle morphogenesis revealed by monoclonal antibodies. In Limb Development and Regeneration, Alan R. Liss, New York, pp. 359-368.
  2. Gardner, J. M. and D. M. Fambrough. 1983. Fibronectin expression during myogenesis. J. Cell Biol. 96: 474-485.
  3. Chiquet, M. and D. M. Fambrough. 1984. Chick myotendinous antigen: I. A monoclonal antibody as a marker for tendon and muscle morphogenesis. J. Cell Biol. 98: 1926-1936.

(Note: Myotendinous antigen was later renamed "tenescin" by Matthias Chiquet and Ruth Ehrismann-Chiquet)

  1. Chiquet, M. and D. M. Fambrough. 1984. Chick myotendinous antigen: II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits. J. Cell Biol. 98: 1937-1946.
  2. Bayne, E. K., M. J. Anderson and D. M. Fambrough. 1984. Extracellular matrix organization in developing muscle: Correlation with acetylcholine receptor aggregates. J. Cell Biol. 99: 1486-1501.

MISCELLANEOUS MEMBRANE STUDIES

  1. Rash, J. E. and D. M. Fambrough. 1973. Ultrastructural and electrophysiological correlates of cell coupling and cytoplasmic fusion during myogenesis in vitro. Devel. Biol. 30: 166-186.
  2. Edidin, M. and D. Fambrough. 1973. Fluidity of the surface of cultured muscle fibers: rapid lateral diffusion of marked surface antigens. J. Cell Biol. 57: 27-37.
  3. Powell, J. A. and D. M. Fambrough. 1973. Electrical properties of normal and dysgenic mouse skeletal muscle in culture. J. Cell. Physiol. 82: 21-38.
  4. Kehry, M., S. Ewald, R. Douglas, C. Sibley, W. Raschke, D. Fambrough, and L. Hood. 1980. The immunoglobulin chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments. Cell 21: 393-406.
  5. Wakshull, E., E. K. Bayne, M. Chiquet and D. M. Fambrough. 1983. Characterization of a plasma membrane glycoprotein common to myoblasts, skeletal muscle satellite cells and glia. Devel. Biol. 100: 464-477.
  6. Hille, B. and D. M. Fambrough (Editors). 1987. "Proteins of Excitable Membranes," 331 pp., Wiley-Interscience, New York.

LYSOSOME-ASSOCIATED MEMBRANE PROTEINS

  1. Lippincott-Schwartz, J. and D. M. Fambrough. 1986. Lysosomal membrane dynamics: Structure and inter-organellar movement of a lysosomal membrane glycoprotein. J. Cell Biol. 102: 1593-1605.
  2. Lippincott-Schwartz, J. and D. M. Fambrough. 1987. Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: Kinetic and morphological analysis. Cell, 49: 669-677.
  3. Mathews, P. and D. M. Fambrough. 1988. Structure-behavior correlates for the shuttling membrane glycoprotein LEP100. J. Gen. Physiol. 92: 18a.
  4. Fambrough, D. M., K. Takeyasu, J. Lippincott-Schwartz, and N. R. Siegel. 1988. Structure of LEP100, a glycoprotein that shuttles between lysosomes and the plasma membrane, deduced from the nucleotide sequence of the encoding cDNA. J. Cell Biol. 106: 61-67.
  5. Zot, A. S. and D. M. Fambrough. 1990. Structure of a gene for a lysosomal membrane glycoprotein (LEP100): housekeeping gene with unexpected exon organization. J. Biol. Chem. 265: 20988-20995.
  6. Nabi, I. R., A. Le Bivic, D. Fambrough, and E. Rodriguez-Boulan. 1991. An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes. J. Cell Biol., 115: 1573-1584.

P-TYPE ATPases

  1. Fambrough, D. M. and E. K. Bayne. 1983. Multiple forms of (Na+ + K+)-ATPase in the chicken: selective detection of the major nerve, skeletal muscle, and kidney form by a monoclonal antibody. J. Biol. Chem. 258: 3926-3935.
  2. Pumplin, D. W. and D. M. Fambrough. 1983. (Na+ + K+)-ATPase correlated with a major group of intramembranous particles in freeze fracture replicas of cultured chick myotubes. J. Cell Biol. 97: 1214-1225.
  3. Fambrough, D. M. 1983. Studies on the (Na+ + K+)-ATPase of skeletal muscle and nerve. Cold Spring Harbor Symp. Quant. Biol. 48: 297-304.
  4. Tamkun, M. M. and D. M. Fambrough. 1986. The (Na+ + K+)-ATPase of chick sensory neurons: Studies on biosynthesis and intracellular transport. J. Biol. Chem. 261: 1009-1019.
  5. Wolitzky, B. A. and D. M. Fambrough. 1986. Regulation of the (Na+ + K+)-ATPase in cultured chick skeletal muscle: Modulation of expression by demand for ion transport. J. Biol. Chem. 261: 9990-9999.
  6. Fambrough, D. M., B. A. Wolitzky, M. M. Tamkun and K. Takeyasu. 1987. Regulation of the sodium pump in excitable cells. Kidney International 32: S97-S112.
  7. Takeyasu, K., M. M. Tamkun, N. R. Siegel and D. M. Fambrough. 1987. Expression of hybrid (Na+ + K+)-ATPase molecules after transfection of mouse Ltk- cells with DNA encoding the b-subunit of an avian brain sodium pump. J. Biol. Chem. 262: 10733-10740.
  8. Kaprielian, Z. and D. M. Fambrough. 1987. Expression of fast and slow isoforms of the Ca2+-ATPase in developing chick skeletal muscle. Devel. Biol. 124: 490 503.
  9. Takeyasu, K., M. M. Tamkun, K. Renaud, and D. M. Fambrough. 1988. Ouabain- sensitive (Na+ + K+)-ATPase activity expressed in mouse Ltk- cells by transfection with DNA encoding the alpha-subunit of an avian sodium pump. J. Biol. Chem. 263: 4347-4354.
  10. Fambrough, D. M. 1988. The sodium pump becomes a family. Trends in Neuroscience 11: 325-328.
  11. Takeyasu, K., K. J. Renaud, J. P. Taormino, B. A. Wolitzky, A. Barnstein, M. M. Tamkun, and D. M. Fambrough. 1989. Differential subunit and isoform expression are involved in regulation of the sodium pump in skeletal muscle. Curr. Topics in Memb. Transport 34: 143-165.
  12. Lebovitz, R. M., K. Takeyasu, and D. M. Fambrough. 1989. Molecular characterization and expression of the (Na+ + K+)-ATPase a-subunit in Drosophila melanogaster. EMBO J. 8: 193-202.
  13. Karin, N. J., Z. Kaprielian, and D. M. Fambrough. 1989. Expression of avian Ca2+- ATPase cDNA in cultured mouse myogenic cells. Mol. Cell. Biol. 9: 1978-1986. Kaprielian, Z., A. M. Campbell, and D. M. Fambrough. 1989. Identification of a Ca2+- ATPase in cerebellar Purkinje cells. Mol. Brain Res. 6: 55-60.
  14. Taormino, J. P. and D. M. Fambrough. 1990. Pre-translational regulation of the (Na+ + K+)-ATPase in response to demand for ion transport in cultured chicken skeletal muscle. J. Biol. Chem. 265: 4116-4123.
  15. Takeyasu, K., V. Lemas and D. M. Fambrough. 1990. Stability of (Na+ + K+)-ATPase alpha-subunit isoforms in evolution. Amer. J. Physiol. 259: C619-630.
  16. Kaprielian, Z., E. Bandman, and D. M. Fambrough. 1991. Expression of Ca2+-ATPase isoforms in denervated, regenerating, and dystrophic chicken skeletal muscle. Devel. Biol., 144: 199-211.
  17. Campbell, A. M., P. D. Kessler, Y. Sagara, G. Inesi, and D. M. Fambrough. 1991. Nucleotide sequences of avian cardiac and brain SR/ER Ca2+-ATPases and functional comparisons with fast twitch Ca2+-ATPase: calcium affinities and inhibitor effects. J. Biol. Chem. 266: 16050-16055.
  18. Renaud, K. J., E. M. Inman and D. M. Fambrough. 1991. Cytoplasmic and transmembrane domain deletions of Na,K-ATPase b-subunit: effects on subunit assembly and intra- cellular transport. J. Biol. Chem., 266: 20491-20497.
  19. Luckie, D. B., V. Lemas, K. L. Boyd, D. M. Fambrough, and K. Takeyasu. 1992. Molecular dissection of functional domains of the E1E2-ATPase using sodium and calcium pump chimeric molecules. Biophysical J. 62: 220-227.
  20. Lemas, M. V., K. Takeyasu and D. M. Fambrough. 1992. The carboxyl terminal 161 amino acids of the Na,K-ATPase a-subunit are sufficient for assembly to the b-subunit. J. Biol. Chem., 267: 20987-20991.
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