Covalent modification of chitin with silk-derivatives acts as an amphiphilic self-organizing template in nacre biomineralisation

Weiss, Ingrid M.; Kaufmann, Stefan; Heiland, Birgit; Tanaka, Motomu

doi:10.1016/j.jsb.2009.04.005

Cited by 31 publications

(19 citation statements)

References 56 publications

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“…This suggests that chitin serves not only as a mechanically favourable thinlayer material and shock-absorber in the final composite. To a certain extent, it may fulfil an additional role as a surface-active component while it is synthesized [159]. As a consequence, the materials properties could change as a function of density and alignment of chitin in the bulk.…”

Section: Coordination With Other Shell Constituentsmentioning

confidence: 99%

“…As outlined in Fig. 17 with respect to mollusc chitin synthases, biophysical cell cortex models, and suitable living systems such as the larval shell should help to identify additional key principles of controlled biomineralization [159,186,190,191]. , The forming shell edge shows the gradual structuring of the prisms (upper arrow).…”

Section: Experimental Tools For Studying Mollusc Chitin Synthasesmentioning

confidence: 99%

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Species-specific shells: Chitin synthases and cell mechanics in molluscs

Weiss¹

2012

Zeitschrift Für Kristallographie - Crystalline Materials

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Abstract. The size, morphology and species-specific texture of mollusc shell biominerals is one of the unresolved questions in nature. In search of molecular control principles, chitin has been identified by Weiner and Traub (FEBS Lett. 1980, 111 : 311-316) as one of the organic compounds with a defined co-organization with mineral phases. Chitin fibers can be aligned with certain mineralogical axes of crystalline calcium carbonate in a speciesspecific manner. These original observations motivated the functional characterization of chitin forming enzymes in molluscs. The full-length cDNA cloning of mollusc chitin synthases identified unique myosin domains as part of the biological control system. The potential impact of molecular motors and other conserved domains of these complex transmembrane enzymes on the evolution of shell biomineralization is investigated and discussed in this article. Chitin in organisms Chitin in extracellular matrices of cellsIn the end of the 19th century, there was a hot debate regarding the chemical nature of chitin. It lasted until acetylated glucosamine was found in alkaline melts of the carapace of diverse arthropods in contrast to tunicate cellulose [1], and "mycosin" of fungi in contrast to "fungal cellulose" (reviewed by [2]). Today, fungi are well accepted as one of the most prominent groups of eukaryotic organisms which contain chitin as part of their extracellular matrix [3]. Since chitin is usually associated with proteins, complex carbohydrates and sometimes mineral phases, it remains a challenge until today to characterize the diversity of cell walls and integuments in both, uni-and multicellular organisms [4][5][6][7][8][9]. One of the best examples for naturally pure chitin are cell wall appendices of diatoms [10,11], and some enzymes involved in their formation have recently been identified [12,13]. As originally determined by fiber diffraction studies [14-17], three major modifications of chitin are distinguished: a-, b-, and g-chitin [18,19], which differ from each other by the arrangement and molar fractions of differently oriented poly-N-acetylated linear b(1!4) glucosamine (i.e. chitobiose homopolymer, Fig. 1) backbones. They assemble into fiber crystals which are stabilized by H-bonds in either two or three dimensions [4,20,21]. Squids such as the European Squid Loligo vulgaris or the Humboldt squid Dosidicus gigas, which are members of the molluscan class Cephalopoda, perform the biosynthesis of different chitin polymorphs in a tissuespecific manner. The chitinous organs are associated with different sets of proteins [22]. The N-acetyl-glucosamine (GlcNAc) chains are assembled into fibrils and hierarchical structures in order to accomodate specific functions such as mechanical stiffness and strength [23,24]. This is important for the functional design, e.g. of insect exoskeletons and additional functions such as structural colours and adhesive micro-pillar appendages [25,26].A major achievement is the abundant information regarding primary structures of enzyme...

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Section: Coordination With Other Shell Constituentsmentioning

confidence: 99%

Section: Experimental Tools For Studying Mollusc Chitin Synthasesmentioning

confidence: 99%

Species-specific shells: Chitin synthases and cell mechanics in molluscs

Weiss¹

2012

Zeitschrift Für Kristallographie - Crystalline Materials

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“…Covalent modification of chitin with silk-derivatives can create an amphiphilic interface that acts as a self-organizing template to form the periodic matrix texture during nacre biomineralization (Weiss et al, 2002(Weiss et al, , 2009). Suzuki et al (2009) showed that chitin could recruit an acidic matrix protein, Pif, which regulates nacre formation in the pearl oyster Pinctada fucata.…”

Section: Introductionmentioning

confidence: 99%

Characterization and functional analysis of a chitin synthase gene (HcCS1) identified from the freshwater pearlmussel Hyriopsis cumingii

Lin

et al. 2015

Genet. Mol. Res.

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ABSTRACT. The triangle sail mussel, Hyriopsis cumingii, is the most important freshwater pearl mussel in China. However, the mechanisms underlying its chitin-mediated shell and nacre formation remain largely unknown. Here, we characterized a chitin synthase (CS) gene (HcCS1) in H. cumingii, and analyzed its possible physiological function. The complete ORF sequence of HcCS1 contained 6903 bp, encoding a 2300-amino acid protein (theoretical molecular mass = 264 kDa; isoelectric point = 6.22), and no putative signal peptide was predicted. A myosin motor head domain, a CS domain, and 12 transmembrane domains were found. The predicted spatial structures of the myosin head and CS domains were similar to the electron microscopic structure of the heavy meromyosin subfragment 19264-19274 (2015) of chicken smooth muscle myosin and the crystal structure of bacterial cellulose synthase, respectively. This structural similarity indicates that the functions of these two domains might be conserved. Quantitative reverse transcription PCR results showed that HcCS1 was present in all detected tissues, with the highest expression levels detected in the mantle. The HcCS1 transcripts in the mantle were upregulated following shell damage from 12 to 24 h post-damage, and they peaked (approximately 1.5-fold increase) at 12 h after shell damage. These findings suggest that HcCS1 was involved in shell regeneration, and that it might participate in shell and nacre formation in this species via chitin synthesis. HcCS1 might also dynamically regulate chitin deposition during the process of shell and nacre formation with the help of its conserved myosin head domain.

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“…Chitin/chitosan have been identified as versatile biopolymers for a broad range of biological functions, including shell regeneration in mollusks, crustaceans, and insects (Suzuki et al, 2009;Proespraiwong et al, 2010;Zhang et al, 2011); repair of wounded skin, nerve, cartilage, and bone (Riccardo, 2009), and immunity (Badariotti et al, , 2011. In recent years, studies investigating the functions of chitin/chitosan in bivalves have concentrated mainly on Crassostrea gigas (Badariotti et al, , 2011, Mytilus galloprovincialis (Weiss et al, 2009), and Pinctada fucata (Suzuki et al, 2009). Badariotti et al (2011) have found that chitinase plays significant roles in various biological processes such as development, tissue remodeling, and immunity in C. gigas by regulating chitin.…”

Section: Introductionmentioning

confidence: 99%

“…Badariotti et al (2011) have found that chitinase plays significant roles in various biological processes such as development, tissue remodeling, and immunity in C. gigas by regulating chitin. Weiss et al (2009) have demonstrated the presence of covalently attached, hydrophobic amino acid side chains in the chitin matrix in the bivalve mollusk M. galloprovincialis using a combination of infrared spectroscopy and mass spectrometry. This finding suggests an active role of such chemically modified chito-oligosaccharides in the creation of a defined interface and guidance of periodic matrix textures, which results in the unique material properties of mollusk shells.…”

Section: Introductionmentioning

confidence: 99%

Two chitin metabolic enzyme genes from Hyriopsis cumingii: cloning, characterization, and potential functions

Gl¹,

Xu²,

Zy³

et al. 2012

Genet. Mol. Res.

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ABSTRACT. Chitin, the second most important natural polymer in the world, and its N-deacetylated derivative chitosan are found in a wide variety of organisms. These versatile biopolymers are associated with a broad range of biological functions. This article is the first to report the potential functions of 2 chitin metabolic enzyme genes from Hyriopsis cumingii. A chitinase-3 gene (Chi-3) and a chitin deacetylase gene (Cda) were cloned from H. cumingii and characterized. Semi-quantitative reverse transcription polymerase chain reaction analysis revealed that the Cda gene was expressed in blood, mantle, liver, stomach, kidney, intestine, gill, and foot, whereas Chi-3 was also expressed in those tissues but not in blood. The tissue-specific expression of H. cumingii Chi-3 indicated that other Chi genes may be involved in the H. cumingii immune system. Real-time quantitative polymerase chain reaction analysis showed that the expression of Chi-3 was significantly (P < 0.05) upregulated 12 h after shell damage, suggesting that Chi-3 might hydrolyze superfluous chitin after shell recovery and play a role in shell formation. Conversely, Cda expression did not change significantly (P 4540 G.-L. Wang et al. ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 11 (4): 4539-4551 (2012) > 0.05) to maintain a certain degree of acetylation in chitin/chitosan. This study enriches the basic research on chitin metabolic genes and lays foundations for further research of shell regeneration in mussels.

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Covalent modification of chitin with silk-derivatives acts as an amphiphilic self-organizing template in nacre biomineralisation

Cited by 31 publications

References 56 publications

Species-specific shells: Chitin synthases and cell mechanics in molluscs

Species-specific shells: Chitin synthases and cell mechanics in molluscs

Characterization and functional analysis of a chitin synthase gene (HcCS1) identified from the freshwater pearlmussel Hyriopsis cumingii

Two chitin metabolic enzyme genes from Hyriopsis cumingii: cloning, characterization, and potential functions

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