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Expression and biological role of laminin-1.

Ekblom, Peter LU ; Lonai, Peter and Talts, Jan LU (2003) In Matrix Biology 22(1). p.35-47
Abstract
Of the approximately 15 laminin trimers described in mammals, laminin-1 expression seems to be largely limited to epithelial basement membranes. It appears early during epithelial morphogenesis in most tissues of the embryo, and remains present as a major epithelial laminin in some adult tissues. Previous organ culture studies with embryonic tissues have suggested that laminin-1 is important for epithelial development. Recent data using genetically manipulated embryonic stem (ES) cells grown as embryoid bodies provide strong support for the view of a specific role of laminin-1 in epithelial morphogenesis. One common consequence of genetic ablation of FGF signaling, beta1-integrin or laminin gamma1 chain expression in ES cells is the... (More)
Of the approximately 15 laminin trimers described in mammals, laminin-1 expression seems to be largely limited to epithelial basement membranes. It appears early during epithelial morphogenesis in most tissues of the embryo, and remains present as a major epithelial laminin in some adult tissues. Previous organ culture studies with embryonic tissues have suggested that laminin-1 is important for epithelial development. Recent data using genetically manipulated embryonic stem (ES) cells grown as embryoid bodies provide strong support for the view of a specific role of laminin-1 in epithelial morphogenesis. One common consequence of genetic ablation of FGF signaling, beta1-integrin or laminin gamma1 chain expression in ES cells is the absence of laminin-1, which correlates with failure of BM assembly and epiblast differentiation. Partial but distinct rescue of epiblast differentiation has been achieved in all three mutants by exogenously added laminin-1. Laminin-1 contains several biologically active modules, but several are found in beta1 or gamma1 chains shared by at least 11 laminins. However, the carboxytermini of the alpha chains contain five laminin globular (LG) modules, distinct for each alpha chain. There is increasing evidence for a particular role of alpha1LG4 binding to its receptors for epithelial tubulogenesis. The biological roles of this and other domains of laminin-1 are currently being explored by genetic means. The pathways controlling laminin-1 synthesis have remained largely unknown, but recent advances raise the possibility that laminin-1 and collagen IV synthesis can be regulated by pro-survival kinases of the protein kinase B/Akt family. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Carboxytermini, Epithelial, Collagen, Tubulogenesis, Kinases
in
Matrix Biology
volume
22
issue
1
pages
35 - 47
publisher
Elsevier
external identifiers
  • wos:000182967400004
  • pmid:12714040
  • scopus:0345381943
ISSN
1569-1802
DOI
10.1016/S0945-053X(03)00015-5
language
English
LU publication?
yes
id
d222c50f-d4ea-4c1d-8524-6e7921a489a1 (old id 113135)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12714040&dopt=Abstract
date added to LUP
2007-07-11 14:47:01
date last changed
2018-01-07 09:24:29
@article{d222c50f-d4ea-4c1d-8524-6e7921a489a1,
  abstract     = {Of the approximately 15 laminin trimers described in mammals, laminin-1 expression seems to be largely limited to epithelial basement membranes. It appears early during epithelial morphogenesis in most tissues of the embryo, and remains present as a major epithelial laminin in some adult tissues. Previous organ culture studies with embryonic tissues have suggested that laminin-1 is important for epithelial development. Recent data using genetically manipulated embryonic stem (ES) cells grown as embryoid bodies provide strong support for the view of a specific role of laminin-1 in epithelial morphogenesis. One common consequence of genetic ablation of FGF signaling, beta1-integrin or laminin gamma1 chain expression in ES cells is the absence of laminin-1, which correlates with failure of BM assembly and epiblast differentiation. Partial but distinct rescue of epiblast differentiation has been achieved in all three mutants by exogenously added laminin-1. Laminin-1 contains several biologically active modules, but several are found in beta1 or gamma1 chains shared by at least 11 laminins. However, the carboxytermini of the alpha chains contain five laminin globular (LG) modules, distinct for each alpha chain. There is increasing evidence for a particular role of alpha1LG4 binding to its receptors for epithelial tubulogenesis. The biological roles of this and other domains of laminin-1 are currently being explored by genetic means. The pathways controlling laminin-1 synthesis have remained largely unknown, but recent advances raise the possibility that laminin-1 and collagen IV synthesis can be regulated by pro-survival kinases of the protein kinase B/Akt family.},
  author       = {Ekblom, Peter and Lonai, Peter and Talts, Jan},
  issn         = {1569-1802},
  keyword      = {Carboxytermini,Epithelial,Collagen,Tubulogenesis,Kinases},
  language     = {eng},
  number       = {1},
  pages        = {35--47},
  publisher    = {Elsevier},
  series       = {Matrix Biology},
  title        = {Expression and biological role of laminin-1.},
  url          = {http://dx.doi.org/10.1016/S0945-053X(03)00015-5},
  volume       = {22},
  year         = {2003},
}