Structure, localization and potential role of a novel molluscan trypsin inhibitor in Lymnaea

Gregg Thomas Nagle, Marijke De Jong-Brink, Sherry D. Painter, Ka Wan Li

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Eggs and egg masses of the freshwater gastropod mollusc Lymnaea provide a microenvironment for developing embryos. Secretions of the exocrine albumen gland of Lymnaea are packaged in the eggs of an egg mass before the eggs are laid externally. The perivitelline fluid that directly surrounds individual oocytes is the main source of nutrition for developing embryos. During early stages of development, the perivitelline fluid is initially internalized by pinocytosis and degraded by lysosomes; in later stages, the embryo ingests the fluid. We previously found that the albumen gland produces large amounts of Lymnaea epidermal growth factor. The albumen gland also appears to produce significant amounts of a novel Lymnaea trypsin inhibitor (LTI), a second peptide that was purified and characterized from Lymnaea albumen gland extracts. The primary structure was determined by microsequence analysis, mass spectrometry, and C-terminal sequence analysis, and showed that LTI is a 57-residue glycosylated peptide. Comparison of the LTI sequence with other known serine protease inhibitors indicates that LTI is a member of the bovine pancreatic trypsin inhibitor family. Reverse phase-high performance liquid chromatography, microsequence analysis, mass spectrometry, and immunocytochemistry demonstrated that abundant amounts of intact LTI are packaged in egg masses. The presence of a trypsin inhibitor in the perivitelline fluid compartment of the egg mass may minimize digestion of peptides and proteins in the perivitelline fluid that are important for the development of the embryo, for example, Lymnaea epidermal growth factor.

Original languageEnglish (US)
Pages (from-to)1213-1221
Number of pages9
JournalEuropean Journal of Biochemistry
Volume268
Issue number5
DOIs
StatePublished - Apr 2 2001

Fingerprint

Lymnaea
Trypsin Inhibitors
Fluids
Ovum
Epidermal Growth Factor
Peptides
Mass spectrometry
Eggs
Molluscs
Embryonic Structures
Serine Proteinase Inhibitors
Aprotinin
High performance liquid chromatography
Nutrition
Mass Spectrometry
Exocrine Glands
Pinocytosis
Gastropoda
Mollusca
Lysosomes

Keywords

  • Albumen gland
  • Lymnaea trypsin inhibitor
  • Mollusc
  • Protein structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

Structure, localization and potential role of a novel molluscan trypsin inhibitor in Lymnaea. / Nagle, Gregg Thomas; De Jong-Brink, Marijke; Painter, Sherry D.; Li, Ka Wan.

In: European Journal of Biochemistry, Vol. 268, No. 5, 02.04.2001, p. 1213-1221.

Research output: Contribution to journalArticle

Nagle, Gregg Thomas ; De Jong-Brink, Marijke ; Painter, Sherry D. ; Li, Ka Wan. / Structure, localization and potential role of a novel molluscan trypsin inhibitor in Lymnaea. In: European Journal of Biochemistry. 2001 ; Vol. 268, No. 5. pp. 1213-1221.
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