Primary structure and expression of a novel human laminin alpha 4 chain

FEBS Lett. 1995 May 29;365(2-3):183-8. doi: 10.1016/0014-5793(95)00462-i.


The complete primary structure of a novel human laminin alpha 4 chain was derived from cDNA clones. The translation product contains a 24-residue signal peptide preceding the mature alpha 4 chain of 1792 residues. The domain structure is similar to that of the recently described alpha 3 chain [Ryan, Tizard, Van Devanter and Carter (1994) J. Biol. Chem. 269, 22779-22787]. Northern analysis of RNA from human fetal and adult tissues revealed developmental regulation of expression. In adult, strong expression was observed in heart as well as lung, ovary, small and large intestines, placenta and liver, whereas weak or no expression was detected in skeletal muscle, kidney, pancreas, testis, prostate or brain. In contrast, fetal lung and kidney revealed high expression. In situ hybridization analysis of human fetal and newborn tissues showed expression of the laminin in alpha 4 chain in certain mesenchymal cells in tissues such as smooth muscle and dermis.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aging / metabolism
  • Amino Acid Sequence
  • Base Sequence
  • Blotting, Northern
  • Cloning, Molecular
  • Female
  • Fetus
  • Gene Expression
  • Gene Library
  • Humans
  • In Situ Hybridization
  • Infant, Newborn
  • Laminin / biosynthesis*
  • Laminin / chemistry*
  • Lung
  • Macromolecular Substances
  • Male
  • Molecular Sequence Data
  • Organ Specificity
  • Polymerase Chain Reaction
  • Pregnancy
  • Restriction Mapping


  • LAMA4 protein, human
  • Laminin
  • Macromolecular Substances

Associated data

  • GENBANK/S78569