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Volume 272, Number 11, Issue of March 14, 1997 pp. 6831-6834
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Cloning and Characterization of a Novel Human Lysyl Hydroxylase Isoform Highly Expressed in Pancreas and Muscle

(Received for publication, December 31, 1996, and in revised form, January 10, 1997)

Minna Valtavaara , Hinni Papponen , Anna-Maria Pirttilä , Kalervo Hiltunen , Heli Helander and Raili Myllylä

From the Biocenter and Department of Biochemistry, University of Oulu, FIN-90570 Oulu, Finland

We report the isolation and characterization of cDNA clones for a novel isoform of lysyl hydroxylase (lysyl hydroxylase 2), a posttranslational enzyme of collagen biosynthesis. The open reading frame predicted a protein of 737 amino acids, including an amino-terminal signal peptide. The amino acid sequence has overall similarity of over 75% to the lysyl hydroxylase (lysyl hydroxylase 1) characterized earlier. This similarity is even higher in the carboxyl-terminal end of the molecules. Lysyl hydroxylase 2 contains nine cysteine residues, which are conserved in lysyl hydroxylase 1. Furthermore, the conserved histidines and aspartate residues required for lysyl hydroxylase activity are present in the sequence. Northern analysis identified a transcript of 4.2 kilobases, which was highly expressed in pancreas and muscle tissues. Expression of cDNA in insect cells using a baculovirus vector yielded proteins with lysyl hydroxylase activity and an antiserum against a synthetic peptide of the deduced amino acid sequence recognized proteins with molecular weights of 88 and 97 kDa in homogenates of the transfected cells.


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