Matrix and mineral in the sea urchin larval skeleton. Wilt, F., H. Journal of structural biology, 126(3):216-26, 6, 1999. ![Matrix and mineral in the sea urchin larval skeleton. [pdf]](https://bibbase.org/img/filetypes/pdf.svg "pdf")
Paper ![Matrix and mineral in the sea urchin larval skeleton. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Website abstract bibtex The endoskeletal spicules of sea urchin larvae are composed of calcite, a surrounding extracellular matrix, and small amounts of occluded matrix proteins. The spicules are formed by primary mesenchyme cells (PMCs) in the blastocoel of the embryo, where they adopt stereotypical locations, thereby specifying where spicules will form. PMCs also fuse to form cytoplasmic cords connecting the cell bodies, and it is within the cords that spicules arise. The mineral phase contains 5% Mg as well as Ca, and about 0.1% of the mass is protein. The matrix and mineral form concentric plies, and the composite has different physical properties than those of pure calcite. The calcite diffracts as a single crystal and is composed of well-ordered, but not perfectly ordered, microdomains. There is evidence for adsorption of matrix proteins to specific crystal faces at domain boundaries, which may help regulate crystal growth and texture. Immature spicules contain considerable precipitated amorphous CaCO3, and PMCs also have vesicles that contain amorphous CaCO3. This suggests the hypothesis that the cellular precursor to the spicules is actually amorphous CaCO3 stabilized in the cell by protein. The spicule s enveloped by the PMC cord, but is topologically exterior to the cell. The PMC plasmalemma is tightly applied to the developing spicules, except perhaps at the elongating tip. The characteristics, localization, and possible function of the four identified matrix proteins are discussed. SM50, SM37, and PM27 all primarily enclose the mineral, though small amounts are occluded. SM30 is found in cellular vesicles and is probably the principal occluded protein of the spicule.
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title = {Matrix and mineral in the sea urchin larval skeleton.},
type = {article},
year = {1999},
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keywords = {Animals,Calcium Carbonate,Calcium Carbonate: chemistry,Calcium Carbonate: metabolism,Extracellular Matrix,Extracellular Matrix Proteins,Extracellular Matrix Proteins: metabolism,Extracellular Matrix: metabolism,Larva,Larva: metabolism,Minerals,Minerals: chemistry,Minerals: metabolism,Sea Urchins,Sea Urchins: embryology,Sea Urchins: growth & development,Sea Urchins: metabolism},
pages = {216-26},
volume = {126},
websites = {http://www.ncbi.nlm.nih.gov/pubmed/10475684},
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abstract = {The endoskeletal spicules of sea urchin larvae are composed of calcite, a surrounding extracellular matrix, and small amounts of occluded matrix proteins. The spicules are formed by primary mesenchyme cells (PMCs) in the blastocoel of the embryo, where they adopt stereotypical locations, thereby specifying where spicules will form. PMCs also fuse to form cytoplasmic cords connecting the cell bodies, and it is within the cords that spicules arise. The mineral phase contains 5% Mg as well as Ca, and about 0.1% of the mass is protein. The matrix and mineral form concentric plies, and the composite has different physical properties than those of pure calcite. The calcite diffracts as a single crystal and is composed of well-ordered, but not perfectly ordered, microdomains. There is evidence for adsorption of matrix proteins to specific crystal faces at domain boundaries, which may help regulate crystal growth and texture. Immature spicules contain considerable precipitated amorphous CaCO3, and PMCs also have vesicles that contain amorphous CaCO3. This suggests the hypothesis that the cellular precursor to the spicules is actually amorphous CaCO3 stabilized in the cell by protein. The spicule s enveloped by the PMC cord, but is topologically exterior to the cell. The PMC plasmalemma is tightly applied to the developing spicules, except perhaps at the elongating tip. The characteristics, localization, and possible function of the four identified matrix proteins are discussed. SM50, SM37, and PM27 all primarily enclose the mineral, though small amounts are occluded. SM30 is found in cellular vesicles and is probably the principal occluded protein of the spicule.},
bibtype = {article},
author = {Wilt, F H},
journal = {Journal of structural biology},
number = {3}
}
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