X‐ray diffraction evidence of collagen‐type protein fibers in the Echinodermata, Coelenterata and Porifera

Marks, Mildred H.; Bear, Richard S.; Blake, Charles H.

doi:10.1002/jez.1401110104

Cited by 75 publications

(14 citation statements)

References 21 publications

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“…Collagen, a well-characterized fibrillar (i.e., framework) protein, plays a structural role in mammal SOM (reviewed in ref. 10), and has been investigated in the structural components of several coelenterates (11,12), of which Order Scleractinia (i.e., stony corals) is a member. However, the greatest emphasis for nucleation proteins rests on the highly acidic proteins, such as bone sialoproteins and dentin matrix proteins in teeth in vertebrates (13,14).…”

Section: Thementioning

confidence: 99%

Proteomic analysis of skeletal organic matrix from the stony coral Stylophora pistillata

Drake

Mass

Haramaty

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

198

283

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It has long been recognized that a suite of proteins exists in coral skeletons that is critical for the oriented precipitation of calcium carbonate crystals, yet these proteins remain poorly characterized. Using liquid chromatography-tandem mass spectrometry analysis of proteins extracted from the cell-free skeleton of the hermatypic coral, Stylophora pistillata , combined with a draft genome assembly from the cnidarian host cells of the same species, we identified 36 coral skeletal organic matrix proteins. The proteome of the coral skeleton contains an assemblage of adhesion and structural proteins as well as two highly acidic proteins that may constitute a unique coral skeletal organic matrix protein subfamily. We compared the 36 skeletal organic matrix protein sequences to genome and transcriptome data from three other corals, three additional invertebrates, one vertebrate, and three single-celled organisms. This work represents a unique extensive proteomic analysis of biomineralization-related proteins in corals from which we identify a biomineralization “toolkit,” an organic scaffold upon which aragonite crystals can be deposited in specific orientations to form a phenotypically identifiable structure.

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Section: Thementioning

confidence: 99%

Proteomic analysis of skeletal organic matrix from the stony coral Stylophora pistillata

Drake

Mass

Haramaty

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

198

283

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“…Chitin and collagen are structural polymers known to fulfill important functions in biomineralization (Ehrlich, ) and there is evidence of their occurrence in gorgonian and scleractinian skeletons (Marks et al, ; Goldberg, ; Drake et al, ; Ramos‐Silva et al, ). In a thin foil lift‐out of the skeleton of a 5‐days old settled larva of A. millepora , van de Locht et al () have described with TEM the occurrence of transverse linear boundaries forming pores across acicular bundles, which might relate to the transverse fibrils described here.…”

Section: Discussionmentioning

confidence: 99%

Biomineralization in newly settled recruits of the scleractinian coral Pocillopora damicornis

Gilis

Meibom

Domart‐Coulon

et al. 2014

Journal of Morphology

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Calcium carbonate biomineralization of scleractinian coral recruits is fundamental to the construction of reefs and their survival under stress from global and local environmental change. Establishing a baseline for how normal, healthy coral recruits initiate skeletal formation is, therefore, warranted. Here, we present a thorough, multiscale, microscopic and spectroscopic investigation of skeletal elements deposited by Pocillopora damicornis recruits, from 12 h to 22 days after settlement in aquarium on a flat substrate. Six growth stages are defined, primarily based on appearance and morphology of successively deposited skeletal structures, with the following average formation time-scales: A (<24 h), B (24-36 h), C (36-48 h), D (48-72 h), E (72-96 h), and F (>10 days). Raman and energy dispersive X-ray spectroscopy indicate the presence of calcite among the earliest components of the basal plate, which consist of micrometer-sized, rod-shaped crystals with rhomboidal habit. All later CaCO3 skeletal structures are composed exclusively of aragonite. High-resolution scanning electron microscopy reveals that, externally, all CaCO3 deposits consist of <100 nm granular units. Fusiform, dumbbell-like, and semispherulitic structures, 25-35 µm in longest dimension, occur only during the earliest stages (Stages A-C), with morphologies similar to structures formed abiotically or induced by organics in in vitro carbonate crystallization experiments. All other skeletal structures of the basal plate are composed of vertically extending lamellar bundles of granules. From Stage D, straight fibrils, 40-45 nm in width and presumably of organic composition, form bridges between these aragonitic bundles emerging from the growing front of fusing skeletal structures. Our results show a clear evolution in the coral polyp biomineralization process as the carbonate structures develop toward those characterizing the adult skeleton.

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“…This pattern may be observed with the electron microscope and detected by x-ray diffraction in the collagen fibers of most phyla ranging from sponges to mammals (13,22,34). In several instances, however, collagen which can be identified by x-ray diffraction and amino acid composition appears to be composed of unstrlated fibrils; the best example being that of the earthworm cuticle (44).…”

Section: The Collagen Fibril and Its Building Block Tropocollagenmentioning

confidence: 98%

The Behavior of Collagen Units as a Model in Morphogenesis

Gross

1956

The Journal of Cell Biology

189

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X‐ray diffraction evidence of collagen‐type protein fibers in the Echinodermata, Coelenterata and Porifera

Cited by 75 publications

References 21 publications

Proteomic analysis of skeletal organic matrix from the stony coral Stylophora pistillata

Proteomic analysis of skeletal organic matrix from the stony coral Stylophora pistillata

Biomineralization in newly settled recruits of the scleractinian coral Pocillopora damicornis

The Behavior of Collagen Units as a Model in Morphogenesis

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