Isolation and Characterization of the Novel Lipophilic Protein, Pb CP-12.7, from the Shell of the Pink Shrimp, Pandalus borealis

Suzuki, Kouichi; Okamori, Mariko; Katsuzaki, Hirotaka; Komiya, Takashi; Imai, Kunio

doi:10.1271/bbb.65.1038

Cited by 5 publications

(3 citation statements)

References 8 publications

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“…[11][12][13][21][22][23][24] Although the latter have the chitin-binding ability, the domain structures responsible for chitin binding are unclear.…”

Section: )mentioning

confidence: 99%

Structural and Functional Analyses of a Strong Chitin-Binding Protein-1 (SCBP-1) from the Exoskeleton of the Crayfish <i>Procambarus clarkii</i>

Suzuki

Sugisaka-Nobayashi

Kogure

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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The organic matrices in the exoskeleton of the crayfish Procambarus clarkii are classified into three groups depending on solubility; acid soluble, acid insoluble-SDS/dithiothreitol (DTT) soluble, and acid insoluble-SDS/DTT insoluble fractions. In our previous studies, Casp-1 and -2 were identified in the acid soluble fraction, and CAP-1 and -2 were identified in the acid insoluble-SDS/DTT soluble fraction. In this study, acid insoluble-SDS/DTT insoluble materials were digested with proteases and the resulting peptides were purified and sequenced. Based on the sequences, a cDNA encoding this protein was cloned. The whole primary sequence of the matrix protein named strong chitinbinding protein-1 (SCBP-1), was deduced. SCBP-1 consisted of 155 amino acid residues and had a Rebers-Riddiford consensus sequence for chitin binding. A recombinant protein of SCBP-N corresponding to the N-terminal part of SCBP-1 showed no chitin-binding ability, while SCBP-C corresponding to the C-terminal part of SCBP-1, showed weak affinity to chitin. These results suggest that the primary sequence of SCBP-1 does not have strong chitin-binding ability. Therefore, SCBP-1 probably binds covalently to chitin through a particular residue contained in the peptide part that was not obtained by protease digestion.

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“…[11][12][13][21][22][23][24] Although the latter have the chitin-binding ability, the domain structures responsible for chitin binding are unclear.…”

Section: )mentioning

confidence: 99%

Structural and Functional Analyses of a Strong Chitin-Binding Protein-1 (SCBP-1) from the Exoskeleton of the Crayfish <i>Procambarus clarkii</i>

Suzuki

Sugisaka-Nobayashi

Kogure

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…Finally, repetitive sequences similar to those found in molluscs are also common in skeletal matrix proteins in disparate metazoans. RLCD-containing proteins such as collagens, silks, and silk-like proteins are commonly observed in metazoan skeletal matrices, including in the echinoderms [ 143 , 144 ], vertebrates [ 145 , 146 ], arthropods [ 147 ] and brachiopods [ 126 , 137 , 138 ]. Different repeats have been hypothesized to have different roles but most appear to be involved in binding chitin or other macromolecules or in imparting flexibility or fracture resistance to the skeleton [ 108 ].…”

Section: Introductionmentioning

confidence: 99%

Sea shell diversity and rapidly evolving secretomes: insights into the evolution of biomineralization

et al. 2016

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An external skeleton is an essential part of the body plan of many animals and is thought to be one of the key factors that enabled the great expansion in animal diversity and disparity during the Cambrian explosion. Molluscs are considered ideal to study the evolution of biomineralization because of their diversity of highly complex, robust and patterned shells. The molluscan shell forms externally at the interface of animal and environment, and involves controlled deposition of calcium carbonate within a framework of macromolecules that are secreted from the dorsal mantle epithelium. Despite its deep conservation within Mollusca, the mantle is capable of producing an incredible diversity of shell patterns, and macro- and micro-architectures. Here we review recent developments within the field of molluscan biomineralization, focusing on the genes expressed in the mantle that encode secreted proteins. The so-called mantle secretome appears to regulate shell deposition and patterning and in some cases becomes part of the shell matrix. Recent transcriptomic and proteomic studies have revealed marked differences in the mantle secretomes of even closely-related molluscs; these typically exceed expected differences based on characteristics of the external shell. All mantle secretomes surveyed to date include novel genes encoding lineage-restricted proteins and unique combinations of co-opted ancient genes. A surprisingly large proportion of both ancient and novel secreted proteins containing simple repetitive motifs or domains that are often modular in construction. These repetitive low complexity domains (RLCDs) appear to further promote the evolvability of the mantle secretome, resulting in domain shuffling, expansion and loss. RLCD families further evolve via slippage and other mechanisms associated with repetitive sequences. As analogous types of secreted proteins are expressed in biomineralizing tissues in other animals, insights into the evolution of the genes underlying molluscan shell formation may be applied more broadly to understanding the evolution of metazoan biomineralization.

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“…The protein components are different depending on the shrimp species. A novel lipophilic protein abundantly containing hydrophobic amino acids was isolated from the shells of Pandalus borealis [34] . Pan et al [29] , [35] isolated red color-related proteins from the shells of Litopenaeus vannamei and Procambarus clarkia , with the monomer molecular mass of 75 and 24 kDa, respectively.…”

Section: Resultsmentioning

confidence: 99%

Positive effects and mechanism of ultrasound on chitin preparation from shrimp shells by co-fermentation

Zhang

Duan

2022

Ultrasonics Sonochemistry

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Isolation and Characterization of the Novel Lipophilic Protein, Pb CP-12.7, from the Shell of the Pink Shrimp, Pandalus borealis

Cited by 5 publications

References 8 publications

Structural and Functional Analyses of a Strong Chitin-Binding Protein-1 (SCBP-1) from the Exoskeleton of the Crayfish <i>Procambarus clarkii</i>

Structural and Functional Analyses of a Strong Chitin-Binding Protein-1 (SCBP-1) from the Exoskeleton of the Crayfish <i>Procambarus clarkii</i>

Sea shell diversity and rapidly evolving secretomes: insights into the evolution of biomineralization

Positive effects and mechanism of ultrasound on chitin preparation from shrimp shells by co-fermentation

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