Immunocytochemical Localization of Wheat Storage Proteins in Endosperm Cells 30 Days After Anthesis

Stenram, Unna; Heneen, Waheeb K.; Skerritt, John H.

doi:10.1093/jxb/42.11.1347

Cited by 12 publications

(4 citation statements)

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“… Loussert et al (2008) showed that antibodies against a range of gluten protein types labelled all protein bodies and densely stained Golgi vesicles. Although these authors failed to show any differences in intensity of labelling using antibodies with different specificities this was reported by Stenram et al (1991) , suggesting that differences occur in the proportions of different protein types in different protein bodies.…”

Section: Discussionmentioning

confidence: 78%

“…The densely stained immunoreactive vesicles often appeared to be enveloped in larger electrolucent vesicles which have also been described previously and proposed to represent completely distended Golgi cisternae ( Kim et al , 1988 ). The same authors also demonstrated that some of the Golgi-associated electron opaque vesicles were labelled by an anti-gliadin antibody while others ( Stenram et al , 1991 ; Loussert et al , 2008 ) showed that they also reacted with antibodies to HMW glutenin subunits and possibly to antibodies to LMW glutenin subunits. It was therefore suggested that they may represent precursors of the protein bodies.…”

Section: Discussionmentioning

confidence: 89%

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Trafficking of storage proteins in developing grain of wheat

Tosi

Parker

Gritsch

et al. 2009

Journal of Experimental Botany

114

126

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The processing properties of the wheat flour are largely determined by the structures and interactions of the grain storage proteins (also called gluten proteins) which form a continuous visco-elastic network in dough. Wheat gluten proteins are classically divided into two groups, the monomeric gliadins and the polymeric glutenins, with the latter being further classified into low molecular weight (LMW) and high molecular weight (HMW) subunits. The synthesis, folding and deposition of the gluten proteins take place within the endomembrane system of the plant cell. However, determination of the precise routes of trafficking and deposition of individual gluten proteins in developing wheat grain has been limited in the past by the difficulty of developing monospecific antibodies. To overcome this limitation, a single gluten protein (a LMW subunit) was expressed in transgenic wheat with a C-terminal epitope tag, allowing the protein to be located in the cells of the developing grain using highly specific antibodies. This approach was also combined with the use of wider specificity antibodies to compare the trafficking and deposition of different gluten protein groups within the same endosperm cells. These studies are in agreement with previous suggestions that two trafficking pathways occur in wheat, with the proteins either being transported via the Golgi apparatus into the vacuole or accumulating directly within the lumen of the ER. They also suggest that the same individual protein could be trafficked by either pathway, possibly depending on the stage of development, and that segregation of gluten proteins both between and within protein bodies may occur.

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Section: Discussionmentioning

confidence: 78%

Section: Discussionmentioning

confidence: 89%

Trafficking of storage proteins in developing grain of wheat

Tosi

Parker

Gritsch

et al. 2009

Journal of Experimental Botany

114

126

View full text Add to dashboard Cite

show abstract

“…In wheat, labelling with prolamin antibodies was observed more often on densely stained vesicles attached at the periphery of the medial and trans-cisternae (Loussert et al, 2008;Stenram et al, 1991), or on free vesicles facing the trans-Golgi stacks ( Fig. 1A and B) which may constitute the trans-Golgi network (Tosi et al, 2009).…”

Section: The Golgi-dependent Pathwaymentioning

confidence: 97%

Trafficking and deposition of prolamins in wheat

Tosi

2012

Journal of Cereal Science

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“…TEM with immunocytochemical detection is a novel approach for examining the structure of gluten and the distribution of the individual components of gluten in dough. Previous researchers have used immunocytochemical microscopy to study the transport and deposition of endosperm storage proteins (Krishnan et al 1990, Stenram et al 1991 and to locate storage proteins in wheat endosperm and bread (Parker et al 1990). Immunocytochemical localization TEM was used to study the distribution of gluten proteins in dough and changes in the distribution of gluten proteins during dough mixing.…”

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confidence: 99%

Immunocytochemical Localization of Gluten Proteins Uncovers Structural Organization of Glutenin Macropolymer

Lindsay

Skerritt

2000

Cereal Chem

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The content and composition of the disulfide‐bonded glutenin macropolymer has been shown to influence dough properties, although its structural organization is poorly characterized. The structure of the glutenin macropolymer in dough was studied using an immunolocalization transmission electron microscopy (TEM) technique by localizing gliadins, low molecular weight glutenin subunits (LMW‐GS), and high molecular weight glutenin subunits (HMW‐GS) in sections of dough using antibody probes selective for each of the three classes of gluten polypeptides. Distinct differences in the distribution patterns of gliadins, LMW‐GS, and HMW‐GS were observed, which suggests that proteins have different roles in the structural organization of the gluten matrix. On the basis of the observed distribution of the proteins in dough, it is speculated that gliadins, which are randomly distributed as individual particles, fill space within the glutenin macropolymer; LMW‐GS, which are present as clusters, are speculated to form aggregated branch structures; and HMW‐GS, which are present as chains, are speculated to form a network from which the LMW‐GS branches are formed. Changes in the distribution of gliadins, LMW‐GS, and HMW‐GS in dough during mixing were also noted. Such an arrangement supports previous biochemical evidence which has established that gliadins, LMW‐GS, and HMW‐GS have specific roles in the structural organization of the glutenin macropolymer in doughs.

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Immunocytochemical Localization of Wheat Storage Proteins in Endosperm Cells 30 Days After Anthesis

Cited by 12 publications

References 0 publications

Trafficking of storage proteins in developing grain of wheat

Trafficking of storage proteins in developing grain of wheat

Trafficking and deposition of prolamins in wheat

Immunocytochemical Localization of Gluten Proteins Uncovers Structural Organization of Glutenin Macropolymer

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