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Titolo:
Ultrastructural localization of proteins involved in sea urchin biomineralization
Autore:
Ameye, L; Hermann, R; Killian, C; Wilt, F; Dubois, P;
Indirizzi:
Free Univ Brussels, Biol Marine Lab, B-1050 Brussels, Belgium Free Univ Brussels Brussels Belgium B-1050 Lab, B-1050 Brussels, Belgium ETH Zurich, Lab Electron Microscopy 1, Inst Biochem, Zurich, Switzerland ETH Zurich Zurich Switzerland copy 1, Inst Biochem, Zurich, Switzerland Univ Calif Berkeley, Dept Med Cell Biol, Berkeley, CA 94720 USA Univ CalifBerkeley Berkeley CA USA 94720 ll Biol, Berkeley, CA 94720 USA
Titolo Testata:
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY
fascicolo: 9, volume: 47, anno: 1999,
pagine: 1189 - 1200
SICI:
0022-1554(199909)47:9<1189:ULOPII>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPICULE MATRIX PROTEIN; CELL-SURFACE PROTEIN; STRONGYLOCENTROTUS-PURPURATUS; ORGANIC MATRIX; FREEZE SUBSTITUTION; SKELETON FORMATION; LARVAL SPICULE; EXPRESSION; EMBRYO; GENE;
Keywords:
biomineralization; sea urchin; immunocytolabeling; organic matrix; tooth; skeleton; high-pressure freezing; freeze-substitution;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Ameye, L Free Univ Brussels, Biol Marine Lab, CP 160-15,50 Av FD Roosevelt, B-1050 Brussels, Belgium Free Univ Brussels CP 160-15,50 Av FD Roosevelt Brussels Belgium B-1050
Citazione:
L. Ameye et al., "Ultrastructural localization of proteins involved in sea urchin biomineralization", J HIST CYTO, 47(9), 1999, pp. 1189-1200

Abstract

Three skeletal tissues of the adult echinoid Paracentrotus lividus (the pedicellaria primordium, the test, and the tooth) were immunolabeled with three sera raised against the total mineralization organic matrix and two specific matrix proteins (SM30 and SM50) from the embryo of the echinoid Strongylocentrotus purpuratus. Two conventional chemical fixation protocols and two high-pressure freezing/freeze-substitution protocols were tested. One conventional protocol is recommended for its good preservation of the ultrastructure, and one high-pressure freezing/freeze-substitution protocol is recommended for its good retention of antigenicity. Immunolabeling was obtained in the three adult tissues. It was confined to the active skeleton-forming cells and to the structured organic matrix. The results indicate that thematrix proteins follow the classical routes of secretory protein assembly and export and suggest that SM30 and SM50 are a part of the tridimensional network formed by the organic matrix before the onset of mineralization. They show that the genetic program of part of skeletogenesis is conserved among different calcification models and developmental stages.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 11:54:58