New Class of Blue Animal Pigments Based on Frizzled and Kringle Protein Domains*

The nature of coloration in many marine animals remains poorly investigated. Here we studied the blue pigment of a scyfoid jellyfish Rhizostoma pulmo and determined it to be a soluble extracellular 30-kDa chromoprotein with a complex absorption spectrum peaking at 420, 588, and 624 nm. Furthermore, we cloned the corresponding cDNA and confirmed its identity by immunoblotting and mass spectrometry experiments. The chromoprotein, named rpulFKz1, consists of two domains, a Frizzled cysteine-rich domain and a Kringle domain, inserted into one another. Generally, Frizzleds are members of a basic Wnt signal transduction pathway investigated intensely with regard to development and cancerogenesis. Kringles are autonomous structural domains found throughout the blood clotting and fibrinolytic proteins. Neither Frizzled and Kringle domains association with any type of coloration nor Kringle intrusion into Frizzled sequence was ever observed. Thus, rpulFKz1 represents a new class of animal pigments, whose chromogenic group remains undetermined. The striking homology between a chromoprotein and members of the signal transduction pathway provides a novel node in the evolution track of growth factor-mediated morphogenesis compounds.

[1]  C. Jomary,et al.  Secreted Frizzled-related proteins: searching for relationships and patterns. , 2002, BioEssays : news and reviews in molecular, cellular and developmental biology.

[2]  Y. Minami,et al.  Expression and Function of the Ror‐Family Receptor Tyrosine Kinases During Development: Lessons from Genetic Analyses of Nematodes, Mice, and Humans , 2003, Journal of receptor and signal transduction research.

[3]  David Strutt,et al.  Frizzled signalling and cell polarisation in Drosophila and vertebrates , 2003, Development.

[4]  O. Britanova,et al.  Amplification of cDNA ends based on template-switching effect and step-out PCR. , 1999, Nucleic acids research.

[5]  J. Nathans,et al.  Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains , 2001, Nature.

[6]  E. Lederer Biochemistry of the natural pigments. , 1948, Annual review of biochemistry.

[7]  A. Tulinsky,et al.  Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. , 1998, Biochemistry.

[8]  R. Blanquet,et al.  An unusual blue mesogleal protein from the mangrove jellyfish Cassiopea xamachana , 1987 .

[9]  K. Constantine,et al.  Ligand interactions with the kringle 5 domain of plasminogen. A study by 1H NMR spectroscopy. , 1990, The Journal of biological chemistry.

[10]  S. Pizzo,et al.  The Voltage-dependent Anion Channel Is a Receptor for Plasminogen Kringle 5 on Human Endothelial Cells* , 2003, Journal of Biological Chemistry.

[11]  Konstantin A Lukyanov,et al.  Family of the green fluorescent protein: journey to the end of the rainbow. , 2002, BioEssays : news and reviews in molecular, cellular and developmental biology.

[12]  N. Chayen,et al.  The molecular basis of the coloration mechanism in lobster shell: β-Crustacyanin at 3.2-Å resolution , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[13]  J. Massagué TGF-beta signal transduction. , 1998, Annual review of biochemistry.

[14]  E. Angles-cano,et al.  Apolipoprotein(a): Structure-Function Relationship at the Lysine-Binding Site and Plasminogen Activator Cleavage Site , 2002, Biological chemistry.