Papilin, a novel component of basement membranes, in relation to ADAMTS metalloproteases and ECM development

Int J Biochem Cell Biol. 2004 Jun;36(6):1079-84. doi: 10.1016/j.biocel.2003.12.010.

Abstract

Papilins are homologous, secreted extracellular matrix proteins which share a common order of protein domains. They occur widely, from nematodes to man, and can differ in the number of repeats of a given type of domain. Within one species the number of repeats can vary by differential RNA splicing. A distinctly conserved cassette of domains at the amino-end of papilins is homologous with a cassette of protein domains at the carboxyl-end of the ADAMTS subgroup of secreted, matrix-associated metalloproteases. Papilins primarily occur in basement membranes. Papilins interact with several extracellular matrix components and ADAMTS enzymes. Papilins are essential for embryonic development of Drosophila melanogaster and Caenorhabditis elegans.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Basement Membrane / metabolism
  • Basement Membrane / ultrastructure
  • Caenorhabditis elegans / genetics
  • Drosophila / genetics
  • Drosophila / metabolism
  • Drosophila Proteins / analysis
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Extracellular Matrix / physiology
  • Extracellular Matrix Proteins / analysis
  • Extracellular Matrix Proteins / chemistry*
  • Extracellular Matrix Proteins / physiology*
  • Glycoproteins / analysis
  • Glycoproteins / genetics
  • Glycoproteins / metabolism
  • Metalloproteases / chemistry*
  • Metalloproteases / genetics
  • Metalloproteases / metabolism*
  • Mice
  • Protein Binding
  • Protein Structure, Tertiary

Substances

  • Drosophila Proteins
  • Extracellular Matrix Proteins
  • Glycoproteins
  • Ppn protein, Drosophila
  • Metalloproteases