Mutations in the laminin α2–chain gene (LAMA2) cause merosin–deficient congenital muscular dystrophy

Nature Genetics

Volumn 11, Issue 2, 1995, Pages 216-218

  Helbling Leclerc, Anne ^a   Zhang, Xu ^b   Topaloglu, Haluk ^c   Cruaud, Corinne ^d   Tesson, Frédérique ^a   Weissenbach, Jean ^d   Tomé, Fernando M S ^a   Schwartz, Ketty ^a   Fardeau, Michel ^a   Tryggvason, Karl ^b   Guicheney, Pascale ^a  

^a PITIÉ SALPÊTRIÈRE HOSPITAL   (France)

^b UNIVERSITY OF OULU   (Finland)

^c HACETTEPE UNIVERSITY   (Turkey)

^d GÉNÉTHON   (France)

Author keywords

[No Author keywords available]

Indexed keywords

LAMININ;

ARTICLE; AUTOSOMAL RECESSIVE DISORDER; CHROMOSOMAL LOCALIZATION; CHROMOSOME 6Q; CLINICAL ARTICLE; CONSANGUINEOUS MARRIAGE; GENE MUTATION; GENETIC LINKAGE; HUMAN; MUSCLE BIOPSY; MUSCLE HYPOTONIA; MUSCLE WEAKNESS; MUSCULAR DYSTROPHY; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SINGLE STRAND CONFORMATION POLYMORPHISM;

ADULT; AMINO ACID SEQUENCE; BASE SEQUENCE; CASE REPORT; CHILD; CHROMOSOME MAPPING; CHROMOSOMES, HUMAN, PAIR 6; CONSANGUINITY; DNA PRIMERS; EXONS; FEMALE; HOMOZYGOTE; HUMAN; INTRONS; LAMININ; LINKAGE (GENETICS); MALE; MOLECULAR SEQUENCE DATA; MUSCULAR DYSTROPHIES; SUPPORT, NON-U.S. GOV'T;

EID: 0028980027     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1095-216     Document Type: Article

References (17)

1. Banker, B.Q. in Myology (eds Engel, A.G. & Franzini-Amstrong, C.) 1275-1289 (McGraw-Hill Book Company, New York, 1994).
2. Tomé, F.M.S. et al. Congenital muscular dystrophy with merosin deficiency. C. R. Acad. Sci. Paris 317, 351-357 (1994).
3. Burgeson, R.E. et al. A new nomenclature for the laminins. Matrix Biol. 14, 209-211 (1994).
4. Hillaire, D. et al. Localization of merosin-negative congenital muscular dystrophy to chromosome 6q2 by homozygosity mapping. Hum. molec. Genet. 3, 1657-1661 (1994).
5. Vuolteenaho, R. et al. Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues. J. Cell Biol. 124, 381-394 (1994).
6. Chelly, J., Concordet, J.P., Kaplan, J.C. & Kahn, A. Illegitimate transcription: transcription of any gene in any cell type. Proc. natn. Acad. Sci. U.S.A. 86, 2617-2621 (1989).
7. Gee, S.H. et al. Laminin-binding protein 120 from brain is closely related to dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin domain of laminin. J. biol. Chem. 268, 14972-14980 (1993).
8. Sunada, Y., Bernier, S.M., Kosak, C.A., Yamada, Y. & Campbell, K.P. Deficiency of merosin in dystrophic dy mice and genetic linkage of the laminin M chain gene to the dy locus. J. biol. Chem. 269, 13759-13732 (1994).
9. Ervasti, J.M. & Campbell, K.P. Membrane organization of the dystrophin-glycoprotein complex. Cell 66, 1121-1131 (1991).
10. Campbell, K.P. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 80, 675-679 (1995).
11. Xu, H., Wu, X-R., Werner, U.M. & Engvall, E. Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama 2) gene. Nature Genet. 8, 297-302 (1995).
12. Arahata, K. et al. Laminin in animal models for muscular dystrophy. Defect of laminin M in skeletal and cardiac muscles and peripheral nerve of the homozygous dystrophic dy/dy mice. Proc. Japan Acad. 69, 259-264 (1993).
13. Dubowitz, V. 22nd ENMC sponsored workshop on congenital muscular dystrophy held in Baarn, The Netherlands, 14-16 May 1993. Neuromusc. Disord. 4, 75-81 (1994).
14. Leivo, I. & Engvall, E. Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development. Proc. natn. Acad. Sci. U.S.A. 85, 1544-1548 (1988).
15. Engvall, E., Earwicker, D., Haaparanta, T., Ruoslahti, E. & Sanes, J.R. Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits. Cell Regul. 1, 731-740 (1990).
16. Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J. & Rutter, W.J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease.Biochemistry 18, 5294-5299 (1979).
17. Don, R.H., Cox, P.T., Wainwright, B.J., Baker, K. & Mattick, J.S. "Touchdown" PCR to circumvent spurious priming during gene amplification. Nucl. Acids Res. 19, 4008 (1991).