Chapter 11
Structure and Function of Matrix Proteins
and Peptides in the Biomineral Formation
in Crustaceans
Hiromichi Nagasawa
Contents
11.1 Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 316
11.2 Molting and Calcification . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 317
11.3 Identification of Matrix Proteins in the Tissues for Temporary Storage
of Calcium Carbonate . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 319
11.4 Identification of Matrix Peptides and Proteins in Exoskeleton . . . . . . . . . . . . . . . . . . . . . . . . 321
11.5 Structure-Activity Relationship of a Cuticle Matrix Peptide . . . . . . . . . . . . . . . . . . . . . . . . . . 323
11.6 Regulation of Amorphous Calcium Carbonate . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 326
11.7 Conclusion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 327
References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 327
Abstract Crustaceans have hard cuticle with layered structure, which is composed
mainly of chitin, proteins, and calcium carbonate. Crustaceans grow by shedding
the old cuticle and replacing it with a new one. Decalcification in the cuticle during
the pre-molt stage and concomitant calcification in the stomach to form gastroliths
observed in some crustacean species are triggered by the molting hormone. Various
proteins and peptides have been identified from calcified cuticle and gastroliths,
and their functions have been examined in terms of calcification and interaction
with chitin. Acidic nature of matrix proteins is important for recruitment of calcium
ions and interaction with calcium carbonate. Examination of the relationship
between amino acid sequence containing acidic amino acid residues and calcification inhibitory activity revealed that the potency did not depend on the sequence but
on the number of acidic amino acid residues. Calcium carbonate in the calcified
H. Nagasawa (*)
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences,
The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo 113-8657, Japan
e-mail: anagahi@mail.ecc.u-tokyo.ac.jp
W.E.G. M€ uller (ed.), Molecular Biomineralization, Progress in Molecular
and Subcellular Biology 52, DOI 10.1007/978-3-642-21230-7_11,
# Springer-Verlag Berlin Heidelberg 2011
315
Structure and Function of Matrix Proteins
and Peptides in the Biomineral Formation
in Crustaceans
Hiromichi Nagasawa
Contents
11.1 Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 316
11.2 Molting and Calcification . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 317
11.3 Identification of Matrix Proteins in the Tissues for Temporary Storage
of Calcium Carbonate . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 319
11.4 Identification of Matrix Peptides and Proteins in Exoskeleton . . . . . . . . . . . . . . . . . . . . . . . . 321
11.5 Structure-Activity Relationship of a Cuticle Matrix Peptide . . . . . . . . . . . . . . . . . . . . . . . . . . 323
11.6 Regulation of Amorphous Calcium Carbonate . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 326
11.7 Conclusion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 327
References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 327
Abstract Crustaceans have hard cuticle with layered structure, which is composed
mainly of chitin, proteins, and calcium carbonate. Crustaceans grow by shedding
the old cuticle and replacing it with a new one. Decalcification in the cuticle during
the pre-molt stage and concomitant calcification in the stomach to form gastroliths
observed in some crustacean species are triggered by the molting hormone. Various
proteins and peptides have been identified from calcified cuticle and gastroliths,
and their functions have been examined in terms of calcification and interaction
with chitin. Acidic nature of matrix proteins is important for recruitment of calcium
ions and interaction with calcium carbonate. Examination of the relationship
between amino acid sequence containing acidic amino acid residues and calcification inhibitory activity revealed that the potency did not depend on the sequence but
on the number of acidic amino acid residues. Calcium carbonate in the calcified
H. Nagasawa (*)
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences,
The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo 113-8657, Japan
e-mail: anagahi@mail.ecc.u-tokyo.ac.jp
W.E.G. M€ uller (ed.), Molecular Biomineralization, Progress in Molecular
and Subcellular Biology 52, DOI 10.1007/978-3-642-21230-7_11,
# Springer-Verlag Berlin Heidelberg 2011
315