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Laminin alpha 5 chain is required for intestinal smooth muscle development

Bolcato-Bellemin, AL; Lefebvre, O; Arnold, C; Sorokin, Lydia LU ; Miner, JH; Kedinger, M and Simon-Assmann, P (2003) In Developmental Biology 260(2). p.376-390
Abstract
Laminins (comprised of alpha, beta, and gamma chains) are heterotrimeric glycoproteins integral to all basement membranes. The function of the lammin alpha5 chain in the developing intestine was defined by analysing laminin alpha5(-/-) mutants and by grafting experiments. We show that lammin alpha5 plays a major role in smooth muscle organisation and differentiation, as excessive folding of intestinal loops and delay in the expression of specific markers are observed in laminin alpha5(-/-) mice. In the subepithelial basement membrane, loss of alpha5 expression was paralleled by ectopic or accelerated deposition of laminin alpha2 and alpha4 chains; this may explain why no obvious defects were observed in the villous form and enterocytic... (More)
Laminins (comprised of alpha, beta, and gamma chains) are heterotrimeric glycoproteins integral to all basement membranes. The function of the lammin alpha5 chain in the developing intestine was defined by analysing laminin alpha5(-/-) mutants and by grafting experiments. We show that lammin alpha5 plays a major role in smooth muscle organisation and differentiation, as excessive folding of intestinal loops and delay in the expression of specific markers are observed in laminin alpha5(-/-) mice. In the subepithelial basement membrane, loss of alpha5 expression was paralleled by ectopic or accelerated deposition of laminin alpha2 and alpha4 chains; this may explain why no obvious defects were observed in the villous form and enterocytic differentiation. This compensation process is attributable to mesenchyme-derived molecules as assessed by chick/mouse alpha5(-/-) grafted associations. Lack of the laminin alpha5 chain was accompanied by a decrease in epithelial alpha3beta1 integrin receptor expression adjacent to the epithelia] basement membrane and of Lutheran blood group glycoprotein in the smooth muscle cells, indicating that these receptors are likely mediating interactions with laminin alpha5-containing molecules. Taken together, the data indicate that the laminin alpha5 chain is essential for normal development of the intestinal smooth muscle and point to possible mesenchyme-derived compensation to promote normal intestinal morphogenesis when laminin alpha5 is absent. (C) 2003 Elsevier Science (USA). All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
mesenchyme, differentiation, developing intestine, integrins, laminins, basement membrane, laminin alpha 5 mutant mouse, muscle, hybrid, intestines, graft
in
Developmental Biology
volume
260
issue
2
pages
376 - 390
publisher
Elsevier
external identifiers
  • pmid:12921739
  • wos:000184946000008
  • scopus:0043063847
ISSN
1095-564X
DOI
10.1016/S0012-1606(03)00254-9
language
English
LU publication?
yes
id
7726d1b2-d3ae-42ea-9f49-be8e681806b2 (old id 303558)
date added to LUP
2007-08-24 12:47:36
date last changed
2018-09-23 03:27:07
@article{7726d1b2-d3ae-42ea-9f49-be8e681806b2,
  abstract     = {Laminins (comprised of alpha, beta, and gamma chains) are heterotrimeric glycoproteins integral to all basement membranes. The function of the lammin alpha5 chain in the developing intestine was defined by analysing laminin alpha5(-/-) mutants and by grafting experiments. We show that lammin alpha5 plays a major role in smooth muscle organisation and differentiation, as excessive folding of intestinal loops and delay in the expression of specific markers are observed in laminin alpha5(-/-) mice. In the subepithelial basement membrane, loss of alpha5 expression was paralleled by ectopic or accelerated deposition of laminin alpha2 and alpha4 chains; this may explain why no obvious defects were observed in the villous form and enterocytic differentiation. This compensation process is attributable to mesenchyme-derived molecules as assessed by chick/mouse alpha5(-/-) grafted associations. Lack of the laminin alpha5 chain was accompanied by a decrease in epithelial alpha3beta1 integrin receptor expression adjacent to the epithelia] basement membrane and of Lutheran blood group glycoprotein in the smooth muscle cells, indicating that these receptors are likely mediating interactions with laminin alpha5-containing molecules. Taken together, the data indicate that the laminin alpha5 chain is essential for normal development of the intestinal smooth muscle and point to possible mesenchyme-derived compensation to promote normal intestinal morphogenesis when laminin alpha5 is absent. (C) 2003 Elsevier Science (USA). All rights reserved.},
  author       = {Bolcato-Bellemin, AL and Lefebvre, O and Arnold, C and Sorokin, Lydia and Miner, JH and Kedinger, M and Simon-Assmann, P},
  issn         = {1095-564X},
  keyword      = {mesenchyme,differentiation,developing intestine,integrins,laminins,basement membrane,laminin alpha 5 mutant mouse,muscle,hybrid,intestines,graft},
  language     = {eng},
  number       = {2},
  pages        = {376--390},
  publisher    = {Elsevier},
  series       = {Developmental Biology},
  title        = {Laminin alpha 5 chain is required for intestinal smooth muscle development},
  url          = {http://dx.doi.org/10.1016/S0012-1606(03)00254-9},
  volume       = {260},
  year         = {2003},
}