Role for laminin-alpha 5 chain LG4 module in epithelial branching morphogenesis
(2003) In Developmental Biology 263(1). p.153-164- Abstract
- Laminin-alpha5 chain was localized in all epithelial basement membranes (BMs) of mouse submandibular gland (SMG) from the onset of branching morphogenesis and became restricted to BMs of epithelial ducts in the adult. To investigate whether the laminin-alpha5 chain plays a role in branching morphogenesis, a set of cell-adhesive peptides from the C-terminal globular domains (LG1-5) was tested for their effects in SMG organ cultures. One peptide, LVLFLNHGH (A5G77f), which represents a sequence located in the connecting loop between strands E and F of LG4. perturbed branching morphogenesis and resulted in irregularities in the contours of epithelial structures, with formation of deep clefts. The data suggest a role for the laminin-alpha5 LG4... (More)
- Laminin-alpha5 chain was localized in all epithelial basement membranes (BMs) of mouse submandibular gland (SMG) from the onset of branching morphogenesis and became restricted to BMs of epithelial ducts in the adult. To investigate whether the laminin-alpha5 chain plays a role in branching morphogenesis, a set of cell-adhesive peptides from the C-terminal globular domains (LG1-5) was tested for their effects in SMG organ cultures. One peptide, LVLFLNHGH (A5G77f), which represents a sequence located in the connecting loop between strands E and F of LG4. perturbed branching morphogenesis and resulted in irregularities in the contours of epithelial structures, with formation of deep clefts. The data suggest a role for the laminin-alpha5 LG4 module in the development of the duct system, rather than in the bifurcation of epithelial clusters. The epithelial BM of A5G77f-peptide-treated explants was continuous, which was in contrast to our previous finding of impaired epithelial BM assembly in explants treated with the larninin-alpha1 LG4 module peptide, or with a monoclonal antibody against this domain. A5G77f also perturbed in vitro development of lung and kidney. These results suggest a crucial role for the LG4 module of larninin-alpha5 in epithelial morphogenesis that is distinct from that of the laminin-alpha1 LG4. (C) 2003 Elsevier Inc. All rights reserved. (Less)
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https://lup.lub.lu.se/record/297287
- author
- Kadoya, Y ; Mochizuki, M ; Nomizu, M ; Sorokin, Lydia LU and Yamashina, S
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- peptide, submandibular gland, organ culture, laminin-alpha 5, laminin-alpha chain, immunohistochemistry, basement membrane, branching morphogenesis
- in
- Developmental Biology
- volume
- 263
- issue
- 1
- pages
- 153 - 164
- publisher
- Elsevier
- external identifiers
-
- wos:000186245100012
- pmid:14568553
- scopus:0142042869
- ISSN
- 1095-564X
- DOI
- 10.1016/S0012-1606(03)00446-9
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Pathology, (Lund) (013030000)
- id
- c2309550-ab9f-4be9-82d6-5134569c8116 (old id 297287)
- date added to LUP
- 2016-04-01 12:15:56
- date last changed
- 2022-01-27 01:12:01
@article{c2309550-ab9f-4be9-82d6-5134569c8116,
abstract = {{Laminin-alpha5 chain was localized in all epithelial basement membranes (BMs) of mouse submandibular gland (SMG) from the onset of branching morphogenesis and became restricted to BMs of epithelial ducts in the adult. To investigate whether the laminin-alpha5 chain plays a role in branching morphogenesis, a set of cell-adhesive peptides from the C-terminal globular domains (LG1-5) was tested for their effects in SMG organ cultures. One peptide, LVLFLNHGH (A5G77f), which represents a sequence located in the connecting loop between strands E and F of LG4. perturbed branching morphogenesis and resulted in irregularities in the contours of epithelial structures, with formation of deep clefts. The data suggest a role for the laminin-alpha5 LG4 module in the development of the duct system, rather than in the bifurcation of epithelial clusters. The epithelial BM of A5G77f-peptide-treated explants was continuous, which was in contrast to our previous finding of impaired epithelial BM assembly in explants treated with the larninin-alpha1 LG4 module peptide, or with a monoclonal antibody against this domain. A5G77f also perturbed in vitro development of lung and kidney. These results suggest a crucial role for the LG4 module of larninin-alpha5 in epithelial morphogenesis that is distinct from that of the laminin-alpha1 LG4. (C) 2003 Elsevier Inc. All rights reserved.}},
author = {{Kadoya, Y and Mochizuki, M and Nomizu, M and Sorokin, Lydia and Yamashina, S}},
issn = {{1095-564X}},
keywords = {{peptide; submandibular gland; organ culture; laminin-alpha 5; laminin-alpha chain; immunohistochemistry; basement membrane; branching morphogenesis}},
language = {{eng}},
number = {{1}},
pages = {{153--164}},
publisher = {{Elsevier}},
series = {{Developmental Biology}},
title = {{Role for laminin-alpha 5 chain LG4 module in epithelial branching morphogenesis}},
url = {{http://dx.doi.org/10.1016/S0012-1606(03)00446-9}},
doi = {{10.1016/S0012-1606(03)00446-9}},
volume = {{263}},
year = {{2003}},
}