@article{fdi:010052975,
  title = {{P}roteomic analysis of the organic matrix of the abalone {H}aliotis asinina calcified shell},
  author = {{M}arie, {B}. and {M}arie, {A}. and {J}ackson, {D}. {J}. and {D}ubost, {L}. and {D}egnan, {B}. {M}. and {M}ilet, {C}. and {M}arin, {F}r{\'e}d{\'e}ric},
  editor = {},
  language = {{ENG}},
  abstract = {{B}ackground: {T}he formation of the molluscan shell is regulated to a large extent by a matrix of extracellular macromolecules that are secreted by the shell forming tissue, the mantle. {T}his so called "calcifying matrix" is a complex mixture of proteins and glycoproteins that is assembled and occluded within the mineral phase during the calcification process. {W}hile the importance of the calcifying matrix to shell formation has long been appreciated, most of its protein components remain uncharacterised. {R}esults: {R}ecent expressed sequence tag ({EST}) investigations of the mantle tissue from the tropical abalone ({H}aliotis asinina) provide an opportunity to further characterise the proteins in the shell by a proteomic approach. {I}n this study, we have identified a total of 14 proteins from distinct calcified layers of the shell. {O}nly two of these proteins have been previously characterised from abalone shells. {A}mong the novel proteins are several glutamine-and methionine-rich motifs and hydrophobic glycine-, alanine-and acidic aspartate-rich domains. {I}n addition, two of the new proteins contained {K}unitz-like and {WAP} (whey acidic protein) protease inhibitor domains. {C}onclusion: {T}his is one of the first comprehensive proteomic study of a molluscan shell, and should provide a platform for further characterization of matrix protein functions and interactions.},
  keywords = {},
  booktitle = {},
  journal = {{P}roteome {S}cience},
  volume = {8},
  numero = {},
  pages = {54},
  ISSN = {1477-5956},
  year = {2010},
  DOI = {10.1186/1477-5956-8-54},
  URL = {https://www.documentation.ird.fr/hor/fdi:010052975},
}