Lipocortin I (p35) is abundant in a restricted number of differentiated cell types in adult organs
作者： Roy A. Fava , James McKanna , Stanley Cohen
关键词:
摘要: Lipocortin-l (p35) is a unique calcium- and phospholipid-binding protein of the lipocortin/calpactin family. Although several possibilities have been suggested, functions for individual proteins this family are not yet known with certainty. As an initial step in identification biological function(s) p35, we used immunohistochemical methods to define precisely many cellular phenotypes that contain p35 vivo. In all organs where found, observed striking distribution p35-positive cells. Typically it highly enriched limited range differentiated cell types while apparently totally absent from most others. Our specific vivo will now set limitations on likely thereby permit more logical approach determination its true function.
sci-hub.se 参考文章(46)
K. Weber, N. Johnsson, U. Plessmann, P. N. Van, H. D. Söling, C. Ampe, J. Vandekerckhove, The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins. The EMBO Journal. ,vol. 6, pp. 1599- 1604 ,(1987) , 10.1002/J.1460-2075.1987.TB02406.X
C E Creutz, W J Zaks, H C Hamman, S Crane, W H Martin, K L Gould, K M Oddie, S J Parsons, Identification of chromaffin granule-binding proteins. Relationship of the chromobindins to calelectrin, synhibin, and the tyrosine kinase substrates p35 and p36. Journal of Biological Chemistry. ,vol. 262, pp. 1860- 1868 ,(1987) , 10.1016/S0021-9258(19)75719-6
T D Giugni, L C James, H T Haigler, Epidermal growth factor stimulates tyrosine phosphorylation of specific proteins in permeabilized human fibroblasts. Journal of Biological Chemistry. ,vol. 260, pp. 15081- 15090 ,(1985) , 10.1016/S0021-9258(18)95705-4
B K De, K S Misono, T J Lukas, B Mroczkowski, S Cohen, A calcium-dependent 35-kilodalton substrate for epidermal growth factor receptor/kinase isolated from normal tissue. Journal of Biological Chemistry. ,vol. 261, pp. 13784- 13792 ,(1986) , 10.1016/S0021-9258(18)67088-7
C V Rao, N Ramani, N Chegini, B K Stadig, F R Carman, P G Woost, G S Schultz, C L Cook, Topography of human placental receptors for epidermal growth factor. Journal of Biological Chemistry. ,vol. 260, pp. 1705- 1710 ,(1985) , 10.1016/S0021-9258(18)89651-X
Y Ando, S Imamura, Y M Hong, M K Owada, T Kakunaga, R Kannagi, Enhancement of calcium sensitivity of lipocortin I in phospholipid binding induced by limited proteolysis and phosphorylation at the amino terminus as analyzed by phospholipid affinity column chromatography. Journal of Biological Chemistry. ,vol. 264, pp. 6948- 6955 ,(1989) , 10.1016/S0021-9258(18)83523-2
R B Pepinsky, R Tizard, R J Mattaliano, L K Sinclair, G T Miller, J L Browning, E P Chow, C Burne, K S Huang, D Pratt, Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. Journal of Biological Chemistry. ,vol. 263, pp. 10799- 10811 ,(1988) , 10.1016/S0021-9258(18)38041-4
T Falbel, R J Mattaliano, J L Browning, B P Wallner, J E Smart, A Ribolini, R B Pepinsky, E P Chow, L K Sinclair, J L Garwin, Purification and partial sequence analysis of a 37-kDa protein that inhibits phospholipase A2 activity from rat peritoneal exudates. Journal of Biological Chemistry. ,vol. 261, pp. 4239- 4246 ,(1986) , 10.1016/S0021-9258(17)35653-3
M L Michener, W B Dawson, C E Creutz, Phosphorylation of a chromaffin granule-binding protein in stimulated chromaffin cells. Journal of Biological Chemistry. ,vol. 261, pp. 6548- 6555 ,(1986) , 10.1016/S0021-9258(19)84597-0
H T Haigler, D D Schlaepfer, W H Burgess, Characterization of lipocortin I and an immunologically unrelated 33-kDa protein as epidermal growth factor receptor/kinase substrates and phospholipase A2 inhibitors. Journal of Biological Chemistry. ,vol. 262, pp. 6921- 6930 ,(1987) , 10.1016/S0021-9258(18)48332-9