Development expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency

Developmental Brain Research

Volumn 96, Issue 1-2, 1996, Pages 62-75

  Blackshear, Perry J ^a   Lai, Wi S ^a   Tuttle, Jane S ^a   Stumpo, Deborah J ^a   Kennington, Elizabeth ^a   Nairn, Angus C ^b   Sulik, Kathleen K ^c  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

^c UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

neural tube defect; neurulation

Indexed keywords

PROTEIN KINASE C; BETA GALACTOSIDASE; HYBRID PROTEIN; ISOENZYME; MARCKS PROTEIN; MEMBRANE PROTEIN; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE; NERVE PROTEIN; PROTEIN; SIGNAL PEPTIDE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BRAIN DEVELOPMENT; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENZYME DEFICIENCY; EXENCEPHALY; IMMUNOHISTOCHEMISTRY; MOUSE; MUTANT; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; TRANSGENIC MOUSE; ANIMAL; C57BL MOUSE; GENE EXPRESSION REGULATION; GENETICS; NEURAL TUBE DEFECT; PHOSPHORYLATION; PHYSIOLOGY; PRENATAL DEVELOPMENT;

ANIMALIA; MUS MUSCULUS;

ANIMALS; BETA-GALACTOSIDASE; EMBRYONIC AND FETAL DEVELOPMENT; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; IMMUNOHISTOCHEMISTRY; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; ISOENZYMES; MEMBRANE PROTEINS; MICE; MICE, INBRED C57BL; MICE, TRANSGENIC; NERVE TISSUE PROTEINS; NEURAL TUBE DEFECTS; PHOSPHORYLATION; PROTEIN KINASE C; PROTEINS; RECOMBINANT FUSION PROTEINS;

EID: 0030599409     PISSN: 01653806     EISSN: None     Source Type: Journal    
DOI: 10.1016/0165-3806(96)00097-1     Document Type: Article

References (32)

1. [1] Aderem, A., The MARCKS brothers: A family of protein kinase C substrates, Cell, 71 (1992) 713-716.
2. [2] Albert, K.A., Walaas, S.I., Wang, J.K.T. and Greengard, P., Widespread occurrence of "87 kDa", a major specific substrate for protein kinase C, Proc. Natl. Acad. Sci. USA, 83 (1986) 2822-2826.
3. [3] Blackshear, P.J., The MARCKS family of cellular protein kinase C substrates, J. Biol. Chem., 268 (1993) 1501-1504.
4. [4] Blackshear, P.J., Verghese, G.M., Johnson, J.D., Haupt, D.M. and Stumpo, D.J., Characteristics of the F52 protein, a MARCKS homologue, J. Biol. Chem., 267 (1992) 13540-13546.
5. [5] Blackshear, P.J., Wen, L., Glynn, B.P. and Witters, L.A., Protein kinase C-stimulated phosphorylation in vitro of a Mr 80,000 protein phosphorylated in response to phorbol esters and growth factors in intact fibroblasts. Distinction from protein kinase C and prominence in brain, J. Biol. Chem., 261 (1986) 1459-1469.
6. [6] Blackshear, P.J., Witters, L.A., Girard, P.R., Kuo, J.F. and Quamo, S.N., Growth factor-stimulated protein phosphorylation in 3T3-L1 cells: Evidence for protein kinase C dependent and independent pathways, J. Biol. Chem., 260 (1985) 13304-13315.
7. [7] Cabell, C.H., Verghese, G.M., Rankl, N.B., Burns, D. and Blackshear, P.J., MARCKS phosphorylation by individual protein kinase C isozymes in insect Sf9 cells, Proc. Assoc. Am. Physicians, 108 (1996) 37-46.
8. [8] Chalepakis, G, Goulding M., Read, A., Strachan T. and Gruss, P., Molecular basis of splotch and Waardenburg Pax-3 mutations, Proc. Natl. Acad. Sci. USA, 91 (1994) 3685-3689.
9. [9] Chomczynki, P. and Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem., 162 (1987) 156-159.
10. [10] Copp, A.J., Neural tube defects, Trends Neurosci., 16 (1993) 381-383.
11. [11] Copp, A.J., Brook, F.A., Estibeiro, J.P., Shum, A.S.W. and Cockcroft. D.L., The embryonic development of mammalian neural tube defects, Prog. Neurobiol., 35 (1990) 363-403.
12. [12] Fujise, A., Mizuno, K., Ueda, Y., Osada, S., Hirai, S., Takayanagi, A., Shimizu, N., Owada, M.K., Nakajima, H. and Ohno, S., Specificity of the high affinity interaction of protein kinase C with a physiological substrate, myristoylated alanine-rich protein kinase C substrate, J. Biol. Chem., 269 (1994) 31642-32648.
13. [13] Goulding, M. and Paquette, A., Pax genes and neural tube defects in the mouse, Ciba Found. Symp., 181 (1994) 103-117.
14. [14] Harlan, D.M., Graff, J.M., Stumpo, D.J., Eddy, R.L. Jr., Shows, T.B., Boyle, J.M. and Blackshear, P.J., The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS), J. Biol. Chem., 266 (1991) 14399-14405.
15. [15] Herget, T., Oehrlein, S.A., Pappin, D.J.C., Rozengurt, E. and Parker, P.J., The myristoylated alanine-rich C kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase C, Eur. J. Biochem., 233 (1995) 448-457.
16. [16] Hogan, B., Constantini, F. and Lacy, E., Manipulating the Mouse Embryo. A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1986.
17. [17] Homanics, G.E., Maeda, N., Traber, M.G., Kayden, H.J., Dehart, D.B. and Sulik, K.K., Exencephaly and hydrocephaly in mice with targeted modification of the apolipoprotein B (Apob) gene. Teratology, 51 (1995) 1-10.
18. [18] Kapron-Bras, C.M. and Trasler, D.G., Interaction between the splotch mutation and retinoic acid in mouse neural tube defects in vitro, Teratology, 38 (1988) 165-173.
19. [19] Kotch, L.E. and Sulik, K.K., Experimental fetal alcohol syndrome: Proposed pathogenic basis for a variety of associated facial and brain anomalies. Am. J. Med. Genet., 44, (1992) 168-176.
20. [20] LaMantia, A.-S., Colbert, M.C. and Linney, E.B., Retinoic acid induction and regional differentiation prefigure olfactory pathway formation in the mammalian forebrain. Neuron, 10 (1993) 1035-1048.
21. [21] Lemire, R.J., Neural tube defects, J. Am. Med. Assoc., 259 (1988) 558-562.
22. [22] Moase, C.E. and Trasler, D.G., Splotch locus mouse mutants: models for neural tube defects and Waardenburg syndrome Type I in humans, J. Med. Genet., 29 (1992) 145-151.
23. r 87,000 protein kinase C substrate from rat brain, J. Biol. Chem., 262 (1987) 16686-16691.
24. [24] Sah, V.P., Attardi, L.D., Mulligan, G.J., Williams, B. O., Bronson, R.T. and Jacks, T., A subset of p53-deficient embryos exhibit exencephaly. Nature Genet., 10 (1995) 175-180.
25. [25] Sanger, F., Nicklen, S. and Coulson, A.R., DNA sequencing with chain-terminating inhibitors, Proc. Natl. Acad. Sci. USA, 74 (1977) 5463-5467.
26. [26] Spach, D.H., Nemenoff, R.A. and Blackshear, P.J., Protein phosphorylation and protein kinase activities in BC3H-1 myocytes. Differences between the effects of insulin and phorbol esters, J. Biol. Chem., 261 (1986) 12570-12573.
27. [27] Stumpo, D.J., Bock, C.B., Tuttle, J.S. and Blackshear, P.J., MARCKS deficiency in mice leads to abnormal brain development and perinatal death, Proc. Natl. Acad. Sci. USA, 92 (1995) 944-948.
28. [28] Stumpo, D.J., Graff, J.M., Albert, K.A., Greengard, P. and Blackshear, P.J., Molecular cloning, characterization and expression of a cDNA encoding the "80-87 kDa" myristoylated alanine-rich C kinase substrate (MARCKS), a major cellular substrate for protein kinase C, Proc. Natl. Acad. Sci. USA, 86 (1989) 4012-4016.
29. [29] Stumpo, D.J., Haupt, D.M. and Blackshear, P.J., Protein kinase C isozyme distribution and down-regulation in relation to insulin-stimulated c-fos induction, J. Biol. Chem., 269 (1994) 21184-21190.
30. [30] Sulik, K.K. and Sadler, T.W., Postulated mechanisms underlying the development of neural tube defects. Insights from in vitro and in vivo studies, Ann. NY Acad. Sci., 678 (1993) 8-21.
31. [31] Szallasi, Z., Smith, C.B., Pettit, G.R. and Blumberg, P. M., Differential regulation of protein kinase C isozymes by myostatin 1 and phorbol 12-myristate 13-acetate in NIH-3T3 fibroblasts. J. Biol. Chem., 269 (1994) 2118-2124.
32. [32] Wetsel, W.C., Khan, W.A., Merchenthaler, I., Rivera, H., Halpern, A.E., Phung, H.M., Negro-Vilar, A. and Hannun, Y.A., Tissue and cellular distribution of the extended family of protein kinase C. isoenzymes, J. Cell. Biol., 117 (1992) 121-133.