Amerikanische Gesellschaft für Hirudotherapie

Chromacin-like peptide in leeches

Basic science / biochemistry published in Neuro Endocrinol Lett (2003)

Zuletzt aktualisiert: June 18, 2026Geprüft von: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Preclinical (animal)Genomik & ProteomikSpeichel-PharmakologieSalzet M et al. · Neuro endocrinology letters, 2003

Abstract

We demonstrate the presence in leech hemolymph of high levels of a peptide recognized by antiserum directed against bovine chromacin. The purification of the chromacin-like peptide was carried out by an acidic extraction, followed by solid phase and high pressure gel permeation chromatography and reversed-phase HPLC purification. Its sequence (GDFELPSIADPQATFESQRGPSAQQVDK) was established by a combination of techniques, including automated Edman degradation, MALDI-TOF measurement and DOT immunobinding assays with anti-chromogranin A. Mass spectrometry measurement revealed a m/z 3177Da, revealing the fact that the molecule is phosphorylated. ELISA titrations performed at each step of the purification revealed a major increase in the level of the peptide (ca. 125 nmol/microl of coelomic fluid) 15 min after LPS exposure. The increase in chromacin-like peptide levels is both time and concentration dependent. The level of this peptide decreased significantly 4 hours after LPS exposure. This report is the first discovery of a chromogranin derived like peptide in invertebrates.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Publication typeJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.
Indexed MeSH termsAmino Acid SequenceAnimalsDose-Response Relationship, DrugEnzyme-Linked Immunosorbent AssayHemolymphLeechesLipopolysaccharidesMolecular Sequence DataPeptidesRadioimmunoassaySpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Zusammenfassung

First discovery of a chromogranin-derived chromacin-like peptide (GDFELPSIADPQATFESQRGPSAQQVDK) in leech hemolymph. Phosphorylated 3177Da molecule whose levels increased markedly after LPS exposure.

Warum dies für die Hirudotherapie relevant ist

This study identified a chromacin-like peptide in leech hemolymph, establishing its amino acid sequence and molecular weight through chromatographic purification, Edman degradation, MALDI-TOF, and immunoassays. The peptide is phosphorylated (m/z 3177 Da) and recognized by anti-chromogranin A and anti-bovine chromacin antisera. ELISA measurements showed that levels of the peptide rose markedly (approximately 125 nmol/microl of coelomic fluid) 15 minutes after lipopolysaccharide (LPS) exposure, with the increase being time- and concentration-dependent and declining significantly by 4 hours. The authors report this as the first discovery of a chromogranin-derived-like peptide in invertebrates. This relevance is indirect for ASH, as it characterizes a component of leech hemolymph and its LPS-responsive dynamics; the abstract does not assign a functional role (e.g., antimicrobial) to the peptide, and no therapeutic or clinical data are provided.

Zitation

Chromacin-like peptide in leeches.

Salzet M et al. · Neuro endocrinology letters, 2003

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