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Updated: Aug 1, 2026

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts
Published on: August 27, 2012
Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases
I A Kramerova1, N Kawaguchi, L I Fessler
1MCD Biology Department and Molecular Biology Institute, University of California at Los Angeles, CA 90095, USA.
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.
Insights
Papilin, an extracellular matrix glycoprotein, plays a crucial role in embryonic development by influencing cell arrangements and modulating metalloproteinases. Its inhibition leads to developmental defects and embryonic lethality in model organisms.
Area of Science:
- Developmental Biology
- Extracellular Matrix Biology
- Molecular Genetics
Background:
- Papilin is an extracellular matrix glycoprotein identified in Drosophila, Caenorhabditis, and mammals.
- Its conserved domain structure suggests functional links with metalloproteinases.
- Papilin is found in various matrix structures during development, including basement membranes and hemocyte-associated matrices.
Purpose of the Study:
- To elucidate the function of papilin in embryonic development.
- To investigate the molecular interactions and mechanisms of papilin.
- To determine the role of papilin in cell rearrangement and organogenesis.
Main Methods:
- cDNA sequencing to identify papilin homologues.
- In vitro biochemical assays to study enzyme inhibition.
- Genetic manipulation (inhibition and ectopic expression) in Drosophila and Caenorhabditis.
- Analysis of developmental defects and embryonic lethality.
Main Results:
- Papilin's cDNA sequence revealed conserved domains, including a 'papilin cassette' shared with ADAMTS metalloproteinases.
- Papilin non-competitively inhibits procollagen N-proteinase in vitro.
- Inhibition of papilin synthesis resulted in defective cell arrangements and embryonic lethality.
- Ectopic papilin expression caused lethal abnormalities in multiple organ systems.
Conclusions:
- Papilin is essential for normal embryonic development, particularly for cell rearrangements.
- Papilin likely modulates the activity of metalloproteinases during organogenesis.
- Papilin's functions are conserved across different species, highlighting its fundamental biological importance.
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