2012
DOI: 10.1186/1756-0500-5-385
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Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos

Abstract: BackgroundThe 7S globulins are plant seed storage proteins that have been associated with the development of a number of human diseases, including peanut allergy. Immune reactivity to the wheat seed storage protein globulin-3 (Glo-3) has been associated with the development of the autoimmune disease type 1 diabetes in diabetes-prone rats and mice, as well as in a subset of human patients.FindingsThe present study characterized native wheat Glo-3 in salt-soluble wheat seed protein extracts. Glo-3-like peptides … Show more

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Cited by 11 publications
(8 citation statements)
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“…Analysis of sequence coverage indicated that these spots were produced by cleavage of the N-termini of these proteins. These results are consistent with previous investigations indicating that globulin-3 family proteins can be processed at internal cleavage sites to yield polypeptides with a large range of molecular weights and pI values (Singh et al 2001;Dupont et al 2011;Koziol et al 2012). Interestingly, the spots corresponding to full-length globulin were downaccumulated under e[CO 2 ], whereas those corresponding to endo-proteolytic events accumulated or appeared in samples grown under these conditions.…”
Section: Changes In Seed Proteome Profilessupporting
confidence: 92%
“…Analysis of sequence coverage indicated that these spots were produced by cleavage of the N-termini of these proteins. These results are consistent with previous investigations indicating that globulin-3 family proteins can be processed at internal cleavage sites to yield polypeptides with a large range of molecular weights and pI values (Singh et al 2001;Dupont et al 2011;Koziol et al 2012). Interestingly, the spots corresponding to full-length globulin were downaccumulated under e[CO 2 ], whereas those corresponding to endo-proteolytic events accumulated or appeared in samples grown under these conditions.…”
Section: Changes In Seed Proteome Profilessupporting
confidence: 92%
“…All the 15 significantly changed globulins in JB Asano were increased while most of which in Tobak was decreased by split N application. The increases in globulins abundance may reduce the nutritional quality of wheat flour since globulin-3 has been associated with the incidence of diabetes (Koziol et al, 2012). Moreover, wheat globulins are also likely to be glycosylated which may result in improved emulsifying capacity and emulsion stability (Altenbach et al, 2009).…”
Section: Discussionmentioning
confidence: 99%
“…In wheat, globulin-3 was cleaved post-translationally in embryos. Five major polypeptide spots of globulin-3 were identified by MS and N-terminal sequencing, and each spot displayed different Mr and pI, these post-translational processing events that lead to the maturation of the globulin family of proteins observed seed protein fraction that could be associated with type 1 diabetes or celiac disease following endoproteolytic processing ( Koziol et al, 2012 ). In barley, globulin contains 637 amino acids with one signal peptide detected by the SignalP v4.0 program, the peptide starts at position 1 and ends at position 27.…”
Section: Discussionmentioning
confidence: 99%