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Author Baumann, Tommy ♦ Kämpfer, Urs ♦ Schürch, Stefan ♦ Schaller, Johann ♦ Largiadèr, Carlo ♦ Nentwig, Wolfgang ♦ Kuhn Nentwig, Lucia
Source SpringerLink
Content type Text
Publisher SP Birkhäuser Verlag Basel
File Format PDF
Copyright Year ©2010
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Life sciences; biology
Subject Keyword Ctenidin ♦ Cupiennius salei ♦ Glycine-rich peptides ♦ Antimicrobial ♦ Tissue expression ♦ Biochemistry ♦ Life Sciences ♦ Biomedicine general ♦ Cell Biology
Abstract Three novel glycine-rich peptides, named ctenidin 1–3, with activity against the Gram-negative bacterium E. coli, were isolated and characterized from hemocytes of the spider Cupiennius salei. Ctenidins have a high glycine content (>70%), similarly to other glycine-rich peptides, the acanthoscurrins, from another spider, Acanthoscurria gomesiana. A combination of mass spectrometry, Edman degradation, and cDNA cloning revealed the presence of three isoforms of ctenidin, at least two of them originating from simple, intronless genes. The full-length sequences of the ctenidins consist of a 19 amino acid residues signal peptide followed by the mature peptides of 109, 119, or 120 amino acid residues. The mature peptides are post-translationally modified by the cleavage of one or two C-terminal cationic amino acid residue(s) and amidation of the newly created mature C-terminus. Tissue expression analysis revealed that ctenidins are constitutively expressed in hemocytes and to a small extent also in the subesophageal nerve mass.
ISSN 1420682X
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2010-04-06
Publisher Place Basel
e-ISSN 14209071
Journal Cellular and Molecular Life Sciences
Volume Number 67
Issue Number 16
Page Count 12
Starting Page 2787
Ending Page 2798


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Source: SpringerLink