Structural characterization of a Lymnaea putative endoprotease related to human furin

FEBS Letters

Knock, Susan L.³  Nagle, Gregg T.²  Smit, August B.¹  Spijker, Sabine¹  Kurosky, Alexander³  Geraerts, Wijnand P.M.¹ 

[1] Graduate School Neurosciences Amsterdam, Research Institute Neurosciences Vrije Universiteit, Faculty of Biology, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands;Marine Biomedical Institute, Department of Anatomy and Neuroscience, The University of Texas Medical Branch, Galveston, TX, USA;Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, TX, USA

关键词: Furin-related endoprotease;    cDNA cloning;    Polymerase chain reaction;    Central nervous system;    Mollusc;    Lymnaeastagnalis;   

DOI  :  10.1016/0014-5793(94)80600-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A number of peptides have been identified in the central nervous system of the freshwater snail, Lymnaea stagnalis, that function as hormones and neurotransmitters/neuromodulators. These peptides are typically proteolytically processed from larger prohormones mostly at sites composed of single or multiple basic amino acid residues. Previously we demonstrated a diversity of putative prohormone convertases that may be involved in prohormone processing in the Lymnaea brain. In the present report, we have characterized a cDNA clone encoding a putative endoprotease of 837 amino acids. The primary structure of the endoprotease (Lfur2) was comparable to that of human furin and contained a putative catalytic domain, a Cys-rich domain, and a transmembrane region. The catalytic domain of Lfur2 demonstrated about 70% residue identity when compared with human furin, PACE4 and Drosophila Dfur1 and dKLIP-1. The Lfur2 gene was expressed in the central nervous system as well as various peripheral tissues of Lymnaea.

【 授权许可】

Unknown