Document Detail


Functional diversity of laminins.
MedLine Citation:
PMID:  23057746     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Laminins are a large family of conserved, multidomain trimeric basement membrane proteins that contribute to the structure of extracellular matrix and influence the behavior of associated cells, such as adhesion, differentiation, migration, phenotype stability, and resistance to anoikis. In lower organisms such as Hydra there is only one isoform of laminin, but higher organisms have at least 16 trimeric isoforms with varying degrees of cell/tissue specificity. In vitro protein and cell culture studies, gene manipulation in animals, and laminin gene mutations in human diseases have provided insight into the specific functions of some laminins, but the biological roles of many isoforms are still largely unexplored, mainly owing to difficulties in isolating them in pure form from tissues or cells. In this review, we elucidate the evolution of laminins, describe their molecular complexity, and explore the current knowledge of their diversity and functional aspects, including laminin-mediated signaling via membrane receptors, in vitro cell biology, and involvement in various tissues gained from animal model and human disease studies. The potential use of laminins in cell biology research and biotechnology is discussed.
Authors:
Anna Domogatskaya; Sergey Rodin; Karl Tryggvason
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Annual review of cell and developmental biology     Volume:  28     ISSN:  1530-8995     ISO Abbreviation:  Annu. Rev. Cell Dev. Biol.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-10-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9600627     Medline TA:  Annu Rev Cell Dev Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  523-53     Citation Subset:  IM    
Affiliation:
Division of Matrix Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institute, 171 77 Stockholm, Sweden; email: anna.domogatskaya@ki.se , sergey.rodin@ki.se , karl.tryggvason@ki.se.
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