Experimental Lathyrism

Tanzer, Marvin L.

doi:10.1016/b978-1-4831-6753-4.50009-0

Cited by 59 publications

(17 citation statements)

References 129 publications

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“…Immature collagen is relatively weak, in spite of a normal microscopic appearance, and acquires tensile strength by the formation of intermolecular and intramolecular cross-linkages. This involves the enzy'matic synthesis of aldehy'des at the site of lysyl and hvdroxylysy'l residues, which are then used to form chemical bonds of various ty-pes between adjacent tropocollagen molecules or between the a chains of an individual molecule (19,20). Several agents, including SC, interfere with the synthesis or the utilization of these aldehydes and thereby' inhibit the biosynthesis of cross-linkages (12.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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show abstract

“…Other suggested defects include a deficiency of the enzyme galactosyl hydroxylysyl glucosyltransferase [79] or the presence of anti bodies to the basement membrane collagens [80], but it is not clear whether any of these defects play a role in the pathogenesis of the disease. of homocysteine is therefore similar to that of ß-aminopropionitrile and penicillamine [84,85], Menkes' Kinky-Hair Syndrome. The main manifestations of the disease are the neuro logical and skeletal abnormalities, but the patients also have characteristically kinky hair and suffer from weakness of the great vessels [86], The molecular defect, which is still unknown, leads to a defective uptake of copper from the intestine [87,88].…”

Section: Epidermolysis Bullosamentioning

confidence: 72%

Molecular Defects in Inborn Disorders of Collagen Metabolism

Kirsch¹,

Ihme²,

Müller³

et al. 1982

Enzyme

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Disturbances of collagen metabolism may result in the manifestation of clinical symptoms. The collagen disorders best characterized are genetically inherited and are known to vary at the clinical and molecular levels. Defective posttranslational modifications of collagen chains due to mutant enzymes have been found in patients with the Ehlers-Danlos syndrome and cutis laxa. Altered selection of collagen types and defective primary structure of the molecules themselves are prominent features in osteogenesis imperfecta. In other pathological conditions, such as Marfan syndrome, no clear molecular defect has been identified as yet.

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“…BAPN and 4-deoxypyridoxine prevent cross-link formation by inhibiting lysyl oxi dase, thereby preventing the formation of allysyl and hydroxyallysyl residues [13]. The concentration of BAPN used in the present study was high enough to totally inhibit lysyl oxidase [11,14]. BAPN and elevated glu cose both increased the solubility of newly synthesized collagen.…”

Section: Discussionmentioning

confidence: 97%

Increased Solubility of Newly Synthesized Collagen in Retinal Capillary Pericyte Cultures by Nonenzymatic Glycosylation

Shen

Robertson

et al. 1984

Ophthalmic Res

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The effect of increasing glucose concentration on the solubility of newly synthesized collagen was studied in bovine retinal capillary pericyte (BRCP) cultures. Synchronized pericytes were labeled with [³H]-proline in media containing either 5, 10, 20 or 40 mM glucose, or 5 mM glucose and 100 μg/ml β-aminopropionitrile fumarate (BAPN). The relative rate of collagen synthesis in the medium (soluble collagen) was significantly increased, and the rate in the cell layer (insoluble collagen) was decreased, by an elevated glucose concentration. The increase in collagen solubility with 20 and 40 mM glucose (over normal, 5 mM glucose) was 14 and 42%, respectively, of that obtained with BAPN. BAPN and 4-deoxypyridoxine inhibited BRCP lysyl oxidase activity, but elevated glucose concentrations did not. Increased nonenzymatic glycosylation of newly synthesized collagen was demonstrated in BRCP cultures co-labeled with L-[¹⁴C]-glucose and L-[³H]-proline. The increase in collagen solubility with elevated glucose concentrations therefore appears to be the result of the inhibition of lysyl-derived cross-link formation because of an increased nonenzymatic glycosylation of the ε-amino groups of lysyl residues of newly synthesized collagen in culture.

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Experimental Lathyrism

Cited by 59 publications

References 129 publications

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

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

Molecular Defects in Inborn Disorders of Collagen Metabolism

Increased Solubility of Newly Synthesized Collagen in Retinal Capillary Pericyte Cultures by Nonenzymatic Glycosylation

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