CIHIDECAR   12529
CENTRO DE INVESTIGACIONES EN HIDRATOS DE CARBONO
Unidad Ejecutora - UE
artículos
Título:
Chemical and in situ characterization of macromolecular components of the cell walls from the green seaweed Codium fragile
Autor/es:
JOSÉ MANUEL ESTEVEZ; PAULA VIRGINIA FERNÁNDEZ; LUCIANA KASULIN; PAUL DUPREE; MARINA CIANCIA
Revista:
GLYCOBIOLOGY
Editorial:
Oxford University Press
Referencias:
Año: 2009 vol. 19 p. 212 - 228
ISSN:
0959-6658
Resumen:
A comprehensive analysis of the carbohydrate-containing
macromolecules from the coencocytic green seaweed
Codium fragile and their arrangement in the cell wall was
carried out. Cell walls in this seaweed are highly complex
structures composed of 31% (w/w) of linear (1¨4)-À-Dmannans,
9% (w/w) of pyruvylated arabinogalactan sulfates
(pAGS), and low amounts of hydroxyproline richglycoprotein
epitopes (HRGP). In situ chemical imaging
by synchrotron radiation Fourier transform infrared
(SR-FTIR) microspectroscopy and by immunolabeling using
antibodies against specific cell wall carbohydrate epitopes
revealed that À-D-mannans and pAGS are placed in
the middle part of the cell wall, whereas HRGP epitopes
(arabinogalactan proteins (AGPs) and extensins) are located
on the wall boundaries, especially in the utricle apical zone.
pAGS are sulfated at C-2 and/or C-4 of the 3-linked À-Larabinopyranose
units and at C-4 and/or C-6 of the 3-linkedand their arrangement in the cell wall was
carried out. Cell walls in this seaweed are highly complex
structures composed of 31% (w/w) of linear (1¨4)-À-Dmannans,
9% (w/w) of pyruvylated arabinogalactan sulfates
(pAGS), and low amounts of hydroxyproline richglycoprotein
epitopes (HRGP). In situ chemical imaging
by synchrotron radiation Fourier transform infrared
(SR-FTIR) microspectroscopy and by immunolabeling using
antibodies against specific cell wall carbohydrate epitopes
revealed that À-D-mannans and pAGS are placed in
the middle part of the cell wall, whereas HRGP epitopes
(arabinogalactan proteins (AGPs) and extensins) are located
on the wall boundaries, especially in the utricle apical zone.
pAGS are sulfated at C-2 and/or C-4 of the 3-linked À-Larabinopyranose
units and at C-4 and/or C-6 of the 3-linked¨4)-À-Dmannans,
9% (w/w) of pyruvylated arabinogalactan sulfates
(pAGS), and low amounts of hydroxyproline richglycoprotein
epitopes (HRGP). In situ chemical imaging
by synchrotron radiation Fourier transform infrared
(SR-FTIR) microspectroscopy and by immunolabeling using
antibodies against specific cell wall carbohydrate epitopes
revealed that À-D-mannans and pAGS are placed in
the middle part of the cell wall, whereas HRGP epitopes
(arabinogalactan proteins (AGPs) and extensins) are located
on the wall boundaries, especially in the utricle apical zone.
pAGS are sulfated at C-2 and/or C-4 of the 3-linked À-Larabinopyranose
units and at C-4 and/or C-6 of the 3-linkedÀ-D-mannans and pAGS are placed in
the middle part of the cell wall, whereas HRGP epitopes
(arabinogalactan proteins (AGPs) and extensins) are located
on the wall boundaries, especially in the utricle apical zone.
pAGS are sulfated at C-2 and/or C-4 of the 3-linked À-Larabinopyranose
units and at C-4 and/or C-6 of the 3-linkedÀ-Larabinopyranose
units and at C-4 and/or C-6 of the 3-linked
À-D-galactopyranose residues. In addition, high levels of ketals
of pyruvic acid were found mainly at 3,4- of some terminal-D-galactopyranose residues. In addition, high levels of ketals
of pyruvic acid were found mainly at 3,4- of some terminal
À-D-Galp units forming a five-membered ring. Ramification
was found at some C-6 of the 3-linked À-D-Galp-D-Galp units forming a five-membered ring. Ramification
was found at some C-6 of the 3-linked À-D-GalpÀ-D-Galp
units. In agreement with the immunolabeled AGP epitopes,
a nonsulfated branched furanosidic arabinan with 5-linked
¿-L-Araf, 3,5-linked ¿-L-Araf, and terminal ¿-L-Araf units
and a nonsulfated galactan structure composed of 3-(3,6)-
linked À-D-Galp residues, both typical of type-II AG glycans
were found, suggesting that AGP structures are present at
low levels in the cell walls of this seaweed. Based on this
study, it is starting to emerge that Codium has developed
unique cell wall architecture, when compared, not only with
that of vascular plants, but also with other related green
seaweeds and algae.-L-Araf, 3,5-linked ¿-L-Araf, and terminal ¿-L-Araf units
and a nonsulfated galactan structure composed of 3-(3,6)-
linked À-D-Galp residues, both typical of type-II AG glycans
were found, suggesting that AGP structures are present at
low levels in the cell walls of this seaweed. Based on this
study, it is starting to emerge that Codium has developed
unique cell wall architecture, when compared, not only with
that of vascular plants, but also with other related green
seaweeds and algae.À-D-Galp residues, both typical of type-II AG glycans
were found, suggesting that AGP structures are present at
low levels in the cell walls of this seaweed. Based on this
study, it is starting to emerge that Codium has developed
unique cell wall architecture, when compared, not only with
that of vascular plants, but also with other related green
seaweeds and algae.Codium has developed
unique cell wall architecture, when compared, not only with
that of vascular plants, but also with other related green
seaweeds and algae.

