Protein Profiling of the Medicinal Leech Salivary Gland Secretion by Proteomic Analytical Methods

I. P. Baskova^1*, L. L. Zavalova², A. V. Basanova¹, S. A. Moshkovskii³, and V. G. Zgoda³

¹Faculty of Biology, Lomonosov Moscow State University, Moscow 119899, Russia; fax: (7-095) 939-1745; E-mail: Saliva1@yandex.ru

²Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow 119997, Russia; fax: (7-095) 330-6538; E-mail: leech@humgen.siobc.ras.ru

³Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, ul. Pogodinskaya 10, Moscow 119992, Russia; fax: (7-095) 245-0857; E-mail: vic@ibmh.msk.su

^* To whom correspondence should be addressed.

Received December 15, 2003; Revision received February 3, 2004

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Protein diversity of the high molecular weight fraction (molecular mass > 500 daltons) of salivary grand secretion of the medicinal leech Hirudo medicinalis has been demonstrated using methods of proteomic analysis. One-dimensional (1D) electrophoresis revealed the presence of more than 60 bands corresponding to molecular masses ranging from 11 to 483 kD. 2D-electrophoresis revealed more than 100 specific protein spots differing in molecular masses and pI values. SELDI-mass spectrometry analysis using the ProteinChip. System based on chromatography surfaces of strong anion or weak cation exchanger detected 45 individual compounds of molecular masses ranged from 1.964 to 66.5 kD. Comparison of SELDI-MS data with protein databases revealed eight known proteins from the medicinal leech. Other masses detected by proteomic analytical methods may be related to both modifications of known proteins and unknown biologically active components of leech saliva secretion.

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KEY WORDS: medicinal leech, salivary gland secretion, proteomics, 1D-electrophoresis, 2D-electrophoresis, protein chip, SELDI-MS

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