Tài liệu Báo cáo khoa học: Molecular and cellular specificity of post-translational aminoacyl

Molecular and cellular specificity of post-translational

aminoacyl isomerization in the crustacean hyperglycaemic

hormone family

Ce´line Ollivaux1,2,3, Dominique Gallois4

, Mohamed Amiche4

, Maryse Boscame´ric4

and Daniel Soyez4

1 Universite´ Pierre et Marie Curie – Paris 06, UMR 7150 Mer et Sante´, E´ quipe Physiologie Compare´e des Erythrocytes, Station Biologique

de Roscoff, France

2 Centre National de la Recherche Scientifique, UMR 7150, Station Biologique de Roscoff, France

3 Universite´ Europe´enne de Bretagne, UEB, Rennes, France

4 Equipe Biogene` se des Signaux Peptidiques, ER3, Universite´ Paris, France

Introduction

Modification of the chirality of a single aminoacyl resi￾due within a peptide chain is a subtle and intriguing

mechanism that remains poorly known to date, and

which leads to structural and functional diversification

of eukaryotic bioactive peptides. Subsequent to the

study by Montecucchi et al. [1] describing the presence

of a d-alanyl residue at the second position of dermor￾phin, a powerful opioid peptide isolated from skin

secretions of the tree frog Phyllomedusa sauvagei, such

a phenomenon has been reported in vertebrates, in

different opioid peptides [2], in antibacterial and

haemolytic peptides from frog skin [3], as well as in

venom from the mammal Platypus [4] (Table 1).

In invertebrates, d-amino acid containing peptides

(DAACPs) were isolated from the nervous system of

molluscs and crustaceans [5], and from venom of a

Keywords

aminoacyl isomerization; confocal laser

scanning microscopy; crustacean

hyperglycaemic hormone; MALDI-TOF MS;

vitellogenesis inhibiting hormone

Correspondence

C. Ollivaux, Universite´ Pierre et Marie Curie

– Paris 06, UMR 7150 Mer et Sante´, E´ quipe

Physiologie Compare´e des Erythrocytes,

Station Biologique de Roscoff, 29682

Roscoff, Cedex, France

Fax: +33 1 44 27 23 61

Tel.: +33 1 44 27 22 62

E-mail: [email protected]

(Received 29 March 2009, revised 23 June

2009, accepted 26 June 2009)

doi:10.1111/j.1742-4658.2009.07180.x

d-aminoacyl residues have been detected in various animal peptides from

several taxa, especially vertebrates and arthropods. This unusual polymor￾phism was shown to occur in isoforms of the crustacean hyperglycaemic

hormone (CHH) of the American lobster because a d-phenylalanyl residue

was found in position 3 of the sequence (CHH and d-Phe3 CHH). In the

present study, we report the detailed strategy used to characterize, in the

lobster neuroendocrine system, isomers of another member of the CHH

family, vitellogenesis inhibiting hormone (VIH). We have demonstrated

that the fourth residue is either an l- or a d- tryptophanyl residue (VIH

and d-Trp4 VIH). Furthermore, use of antisera specifically recognizing the

epimers of CHH and VIH reveals that aminoacyl isomerization occurs in

specialized cells of the X organ–sinus gland neurosecretory system and that

the d-forms of the two neuropeptides are not only present in the same

cells, but, importantly, also are co-packaged within the same secretory

vesicles.

Abbreviations

CHH, crustacean hyperglycaemic hormone; DAACP, D-amino acid containing peptide; gp, guinea pig; PTM, post-translational modification;

r, rat; rb, rabbit; VIH, vitellogenesis inhibiting hormone; XO, X organ.

4790 FEBS Journal 276 (2009) 4790–4802 ª 2009 The Authors Journal compilation ª 2009 FEBS