Up-regulation of multiple serine proteinases during earthworm tail regeneration

S. J. Cho, P. Y. Cho, M. S. Lee, Y. Na, JooHun Lee, K. S. Koh, J. K. Choo, S. C. Park

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Previous studies have shown that spatiotemporal regulation of extracellular matrix (ECM) by proteinases is implicated in the initial step of regeneration. In amphibian regeneration, the up-regulation of proteinases such as metalloproteinases (MMPs) and cathepsin D, and proteinase-related proteins such as proteinase tissue inhibitors and activators has been demonstrated. Since the earthworm could provide a unique and valuable model to investigate the mechanism of regeneration, we studied the developmental change in proteinase expression during earthworm tail regeneration. Zymographic analysis revealed that proteinase activities began to increase within 1 h after amputation and reached a maximum at 7 days post-amputation. This peak in activity was approximately 22-fold greater than the unamputated controls. Thereafter, the proteinase activities tended to decrease followed by another peak at 30 days before returning to control levels. At least four types of proteinase were distinguishable at 7 and 30 days post-amputation, with molecular weights of 25, 28, 38, and 44 kDa, respectively. All proteinase activities were strongly inhibited by addition of phenylmethylsulfonyl fluoride (PMSF) and aprotinin, specific inhibitors for serine proteinase. Pepstatin A, E-64, iodoacetamide and a metal ion-free medium were not effective inhibitors, indicating that proteinases expressed during earthworm tail regeneration would be serine proteinases. In addition, we were able to detect two types of plasminogen activator (PA) with molecular weights of 40 and 47 kDa, respectively. PA activities were predominantly expressed at 1, 5, and 25 days post-amputation, which preceded two peaks of serine proteinase activities appearing at approximately 7 and 30 days after amputation, respectively. This fact supports the view that serine proteinases expressed in respond to tail amputation may be plasmin-like proteinases activated by PA.

Original languageEnglish
Pages (from-to)103-108
Number of pages6
JournalInvertebrate Reproduction and Development
Volume40
Issue number2-3
DOIs
Publication statusPublished - 2001 Jan 1

Fingerprint

Oligochaeta
Serine Proteases
serine proteinases
earthworms
Tail
Regeneration
Peptide Hydrolases
tail
Up-Regulation
proteinases
amputation
Amputation
plasminogen activator
Plasminogen Activators
Molecular Weight
molecular weight
cathepsin D
Phenylmethylsulfonyl Fluoride
plasmin
Iodoacetamide

All Science Journal Classification (ASJC) codes

  • Animal Science and Zoology
  • Developmental Biology

Cite this

Cho, S. J. ; Cho, P. Y. ; Lee, M. S. ; Na, Y. ; Lee, JooHun ; Koh, K. S. ; Choo, J. K. ; Park, S. C. / Up-regulation of multiple serine proteinases during earthworm tail regeneration. In: Invertebrate Reproduction and Development. 2001 ; Vol. 40, No. 2-3. pp. 103-108.
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Up-regulation of multiple serine proteinases during earthworm tail regeneration. / Cho, S. J.; Cho, P. Y.; Lee, M. S.; Na, Y.; Lee, JooHun; Koh, K. S.; Choo, J. K.; Park, S. C.

In: Invertebrate Reproduction and Development, Vol. 40, No. 2-3, 01.01.2001, p. 103-108.

Research output: Contribution to journalArticle

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