Lathyrism: A Review

Barrow, Mark V.; Simpson, Charles F.; Miller, Edward J.

doi:10.1086/408017

Cited by 154 publications

(49 citation statements)

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“…Lathyrus is predominantly a true diploid with a chromosome number of 2n = 2x = 14 (also reconstructed as the ancestral number), with a few exceptions having 2n = 28 or 42 (Schaefer et al, 2012 clymenum-with an aim at improving grain yield, biomass, resistance to biotic and abiotic stresses, and, most importantly, to reduce the neurotoxin in its seeds. Unfortunately Lathyrus seeds, apart of being protein rich, contain the water soluble non-protein amino acid β-diaminopropionic acid (ODAP), which has been found to be a neurotoxin linked to an irreversible neurological disorder called lathyrism (Barrow et al, 1974). Several low β-diaminopropionic acid (with < 0.1% ODAP) cultivares were developed through intraspecific hybridization in Bangladesh, ICARDA, Ethiopia, Canada and Australia.…”

Section: A Genus Lathyrus Lmentioning

confidence: 99%

Legume Crops Phylogeny and Genetic Diversity for Science and Breeding

Smýkal

Coyne

Ambrose

et al. 2014

Critical Reviews in Plant Sciences

253

189

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Section: A Genus Lathyrus Lmentioning

confidence: 99%

Legume Crops Phylogeny and Genetic Diversity for Science and Breeding

Smýkal

Coyne

Ambrose

et al. 2014

Critical Reviews in Plant Sciences

253

189

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“…the amount of lysine in elastin and collagen (66)(67)(68). When all of the data were taken together it eventually became clear that the lysine in elastin and collagen served as a precursor to the crosslinks; and selected steps in crosslink formation could be inhibited by copper deficiency and lathyrogenic agents.…”

Section: Post-translational Steps In Elastic Fiber Formationmentioning

confidence: 99%

“…Another interesting feature of the relationship between copper and lysyl oxidase is the observation that copper ligand complexes appear to influence the actual synthesis of the enzyme (78). Certain genetic disorders are also characterized in part by low or suboptimal lysyl oxidase activity (5,25,66,68).…”

Section: Post-translational Steps In Elastic Fiber Formationmentioning

confidence: 99%

Elastin metabolism and chemistry: potential roles in lung development and structure.

Rucker¹,

Dubick²

1984

Environ Health Perspect

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Elastic fibers are important for elasticity and extensibility of lung tissue. In the developing lung, elastic fibers appear in greatest numbers during the process or period of alveolarization. A variety of mesenchymal cells in lung appear responsible for elastin synthesis. Elastin is a novel protein both from the standpoint of its processing into elastic fibers and chemical properties. For example, elastin undergoes posttranslational modification before its assembly into fibers. These steps include limited proteolysis, hydroxylation of prolyl residues and the oxidative deamination of lysyl residues prior to their incorporation into the crosslinks that covalently bond together polypeptide chains of elastin. The crosslinking amino acids include lysinonorleucine, merodesmosine and desmosine isomers. A key enzyme that controls this process is lysyl oxidase. Lysyl oxidase is a copper metalloprotein whose activity is responsive to and modulated by environmental insults, nutrition deficiencies and the administration of various pharmacological agents. Regarding chemical properties, elastin is one of the most apolar proteins secreted by mammalian cells. Moreover, elastin is one of the most long-lived proteins secreted into the extracellular matrix. In relationship to its processing into elastic fibers and chemical properties, details related to major aspects of elastin metabolism as well as speculation on its potential as a factor in lung development and disease are discussed.

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“…These arise through the extracellular condensation of lysine or hydroxylysine residues on one polypeptide chain with lysine-or hydroxylysine-derived aldehydes on a different chain to form aldimine or aldol-type conjugates, as in collagen, or desmosine and isodesmosine, as in elastin (12). Semicarbazide (SC)1 is one of several compounds, called lathyrogens, capable of interfering with the cross-linking process.…”

Section: Introductionmentioning

confidence: 99%

“…Semicarbazide (SC)1 is one of several compounds, called lathyrogens, capable of interfering with the cross-linking process. Lathyrogens exert their effect through the inhibition of lysyl oxidase, the enzyme that converts lysine or hydroxylvsine to the respective aldehyde, by reacting with preformed aldehydes and thus blocking cross-linkage formation, by disrupting preexisting aldimine cross-linkages, or though combinations of these (12)(13)(14). The net result is that the affected connective tissue is more friable, particularly in rapidly growing animals.…”

Section: Introductionmentioning

confidence: 99%

Effects of a molecular change in collagen on lung structure and mechanical function.

Stanley¹,

Alper²,

Cunningham³

et al. 1975

J. Clin. Invest.

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A B S T R A C T Semicarbazide, a lathyrogen. was given to growing rats to elucidate the consequences of altering the molecular structure of fibrous proteins within the lung. Static pressure-volume (P-V) measurements during deflation of saline-filled lungs showed normal recoil pressure and compliance values within the physiological range of lung volume. Quasi-static P-V measurements were also normal during slow reinflation, even beyond physiological limits to a recoil pressure of 20 cm H20. However, the lungs of experimental rats ruptured at much lower recoil pressures than controls. Histology was normal in lungs fixed at 20 cm H20. In contrast, lungs showed dilatation of terminal air spaces, rupture of alveolar walls, and an increase in mean linear intercept in experimental compared with control specimens, when fixed at 30 cm H20. Biochemical analyses revealed reduced cross-linking of lung collagen without change in its total content. There were no detectable changes in the quantity or quality of lung elastin. It is concluded that semicarbazide may selectively impair the maturation of lung collagen and that immaturity of lung collagen is associated with a reduction in the tensile strength of lung tissue, without changes in elasticity within physiological volume limits.

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Lathyrism: A Review

Cited by 154 publications

References 0 publications

Legume Crops Phylogeny and Genetic Diversity for Science and Breeding

Legume Crops Phylogeny and Genetic Diversity for Science and Breeding

Elastin metabolism and chemistry: potential roles in lung development and structure.

Effects of a molecular change in collagen on lung structure and mechanical function.

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