Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases

Citations Over TimeTop 17% of 2000 papers

Abstract

Papilin is an extracellular matrix glycoprotein that we have found to be involved in, (1) thin matrix layers during gastrulation, (2) matrix associated with wandering, phagocytic hemocytes, (3) basement membranes and (4) space-filling matrix during Drosophila development. Determination of its cDNA sequence led to the identification of Caenorhabditis and mammalian papilins. A distinctly conserved 'papilin cassette' of domains at the amino-end of papilins is also the carboxyl-end of the ADAMTS subgroup of secreted, matrix-associated metalloproteinases; this cassette contains one thrombospondin type 1 (TSR) domain, a specific cysteine-rich domain and several partial TSR domains. In vitro, papilin non-competitively inhibits procollagen N-proteinase, an ADAMTS metalloproteinase. Inhibiting papilin synthesis in Drosophila or Caenorhabditis causes defective cell arrangements and embryonic death. Ectopic expression of papilin in Drosophila causes lethal abnormalities in muscle, Malpighian tubule and trachea formation. We suggest that papilin influences cell rearrangements and may modulate metalloproteinases during organogenesis.

Related Papers

• → A Review of the ADAMTS Family, Pharmaceutical Targets of the Future(2009)73 cited
• → Characterization of ADAMTS14, a novel member of the ADAMTS metalloproteinase family(2001)31 cited
• A disintegrin and metalloproteinase with thrombospondin motifs-1(ADAMTS-1)の乳癌細胞における遺伝子・蛋白発現及びADAMTS-1抗体の抗腫瘍効果の検討(2009)
• The Research of A Disintegrin-like and Metalloproteinase with Thrombospondin Type 1 Motifs(2010)
• FRS-078 ADAMTS-1, A Disintegrin And Metalloprotease with ThromboSpondin motifs-1, Is a Novel Hypoxic Immediate Gene Expressed by Endothelial Cells(NO and Cardiovascular System (H) : FRS10)(Featured Research Session (English))(2004)