title: Modifications in integrin expression and extracellular matrix composition in children with biliary atresia.
abstract: BACKGROUND
  The aetiology of biliary atresia (BA) is still unresolved. The study's aim was to investigate the distribution of extracellular matrix proteins and cellular adhesion molecules in children with BA compared to other cholestatic liver disease (CLD) and normal liver architecture (NLA).
  
  
  METHODS
  Liver biopsies were obtained from children with BA (n=13), CLD (n=6) and NLA (n=8).
  
  
  METHODS
  We systematically analysed ultra thin frozen sections from the liver hilum stained with 25 monoclonal antibodies for cellular characterisation, extracellular matrix proteins and adhesion molecules.
  
  
  RESULTS
  2 changes were specifically found in BA: laminin beta1 was reduced in children with BA vs. NLA and CLD. Conversely, integrin alpha 3 was increased in BA vs. NLA and CLD (p<0.05). Furthermore, we detected changes in a similar pattern for both BA and CLD vs. NLA: in BA and CLD perlecan was increased. On the contrary, integrin beta1 and entactin were decreased vs. NLA (p<0.05).
  
  
  CONCLUSIONS
  Extracellular matrix proteins and adhesion molecules mediate cellular polarity and integrity, development of tubular structures, and proliferation. Therefore, our findings can be important for the understanding of the genesis of BA.
  
  
  CONCLUSIONS
  The composition of extracellular matrix proteins and adhesion molecules in children with BA differs from NLA and other CLD in distribution of laminin beta1 and integrin alpha 3, which may have implications for genetic, immunologic and environmental associations in BA.
authors.affiliation: Paediatric Gastroenterology, Hepatology and Nutrition, Alder Hey Children's NHS Foundation Trust, Liverpool, United Kingdom.
authors.forename: T
authors.initials: T
authors.lastname: Whitby
authors.affiliation: Paediatric Gastroenterology, Hepatology and Liver Transplant, University Hospital Essen, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Schroeder
authors.affiliation: Paediatric Gastroenterology, Hepatology and Liver Transplant, University Hospital Essen, Germany.
authors.forename: H S
authors.initials: HS
authors.lastname: Kim
authors.affiliation: Paediatric Surgery, Medical School Hannover, Germany.
authors.forename: C
authors.initials: C
authors.lastname: Petersen
authors.affiliation: Institute of Pathology, University Hospital Jena, Germany.
authors.forename: O
authors.initials: O
authors.lastname: Dirsch
authors.affiliation: Liver Unit, Children's Hospital and University Hospital Birmingham, United Kingdom.
authors.forename: U
authors.initials: U
authors.lastname: Baumann
authors.affiliation: Paediatric Gastroenterology, Hepatology and Nutrition, Alder Hey Children's NHS Foundation Trust, Liverpool, United Kingdom.
authors.forename: M K H
authors.initials: MK
authors.lastname: Auth
mesh_terms: D001653:Bile Ducts, Intrahepatic / Q000473:pathology; D001656:Biliary Atresia / Q000473:pathology*; D001706:Biopsy; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002648:Child; D002675:Child, Preschool; D002780:Cholestasis, Intrahepatic / Q000473:pathology; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005260:Female; D006801:Humans; D007223:Infant; D039422:Integrin alpha3 / Q000378:metabolism; D019012:Integrin beta1 / Q000378:metabolism; D016023:Integrins / Q000378:metabolism*; D007797:Laminin / Q000378:metabolism; D008099:Liver / Q000473:pathology*; D008297:Male; D008562:Membrane Glycoproteins / Q000378:metabolism; D012016:Reference Values
chemical_list: D015815:Cell Adhesion Molecules; D016326:Extracellular Matrix Proteins; D039422:Integrin alpha3; D019012:Integrin beta1; D016023:Integrins; C478221:LAMB1 protein, human; D007797:Laminin; D008562:Membrane Glycoproteins; C029967:nidogen