Dental changes in experimental lathyrism

1. C14-labeled ß-aminopropionitrile distributed throughout the egg contents within 10 minutes postinjection. By ion exchange chromatography and electrophoretic analysis three major components of the extractable dialyzable radioactive material could be demonstrated, representing at least 80 per cent of the total. The acidic and basic components were identified as ß-aminopropionitrile and cyanoacetic acid, while the fraction isoelectric at pH 5.3, consisting of two components, remained unidentified. 2. Less than 1 molecule of ßAPN per 100 molecules of protein was present in the highly purified extractable lathyritic bone collagen indicating that binding of the lathyrogen is not a factor in collagen extractability. 3. The proximity of ßAPN to collagen in bone is not essential to its extractability. 4. The effect of incubation temperature of the embryo on collagen extractability suggests the involvement of a metabolic process in this phenomenon.

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Influence of Injury and Adaptation of the Periodontal Ligament to Pathologic Changes During Experimental Lathyrism

Journal of Periodontology ◽

10.1902/jop.1959.30.3.253 ◽

1959 ◽

Vol 30 (3) ◽

pp. 253-264 ◽

Cited By ~ 9

Author(s):

Alvin F. Gardner

Keyword(s):

Periodontal Ligament ◽

Experimental Lathyrism

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Experimental Lathyrism

International Review of Connective Tissue Research ◽

10.1016/b978-1-4831-6753-4.50009-0 ◽

1965 ◽

pp. 91-112 ◽

Cited By ~ 40

Author(s):

Marvin L. Tanzer

Keyword(s):

Experimental Lathyrism

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Chemical Contraction and Relaxation of Collagen Fibres in Rats with Experimental Lathyrism

Pharmacology ◽

10.1159/000135328 ◽

1963 ◽

Vol 9 (1) ◽

pp. 41-45

Author(s):

Zdena Trnavská ◽

Karel Trnavský

Keyword(s):

Collagen Fibres ◽

Contraction And Relaxation ◽

Experimental Lathyrism

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RADIOAUTOGRAPHIC STUDY OF S35O4 UPTAKE BY EPIPHYSEAL CARTILAGE IN EXPERIMENTAL LATHYRISM

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y62-067 ◽

1962 ◽

Vol 40 (1) ◽

pp. 565-570 ◽

Cited By ~ 1

Author(s):

Yurika K. Shintani ◽

H. E. Taylor

Keyword(s):

Normal Diet ◽

Cartilage Matrix ◽

Epiphyseal Cartilage ◽

Acid Mucopolysaccharides ◽

The Matrix ◽

Endochondral Growth ◽

Experimental Lathyrism

Disturbances in the uptake of radiosulphate were observed in radioautographs of the epiphysis of rats made lathyritic by giving either beta-aminopropionitrile or semicarbazide. There was a decreased uptake of sulphate which became more marked as the lesions advanced and an increased uptake was noted as the lesions regressed when the rats were returned to a normal diet. In normal rats, the radio-sulphate shifted to the zone of calcifying cartilage by the 4th day postinjection and, by the 7th day, it was concentrated over the ossifying trabeculae. In lathyrism this shift was delayed and the radiosulphate image was still concentrated in the cartilage matrix at days 4 and 7 postinjection. It is believed these findings reflect a disturbance in the matrix acid mucopolysaccharides and an interference with endochondral growth in lathyrism.

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A SEX-LINKED DEFECT IN THE CROSS-LINKING OF COLLAGEN AND ELASTIN ASSOCIATED WITH THE MOTTLED LOCUS IN MICE

Journal of Experimental Medicine ◽

10.1084/jem.139.1.180 ◽

1974 ◽

Vol 139 (1) ◽

pp. 180-192 ◽

Cited By ~ 57

Author(s):

David W. Rowe ◽

Ermona B. McGoodwin ◽

George R. Martin ◽

Michael D. Sussman ◽

Douglas Grahn ◽

...

Keyword(s):

Coat Color ◽

Cross Linking ◽

Genetic Abnormality ◽

Cross Link ◽

Skin Collagen ◽

The Cross ◽

Tissue Abnormalities ◽

Link Formation ◽

Experimental Lathyrism

A genetic abnormality in collagen and elastin cross-linking resembling experimental lathyrism has been identified in mice. The defect is an X-linked trait, attributed to the mottled locus which also influences coat color. The affected mice have aneurysms of the aorta and its branches, weak skin, and bone deformities in a spectrum of severity varying with the alleles at the mottled locus. A defect in the cross-linking of collagen was demonstrated in the skin of the affected animals by a marked increase in collagen extractability and a reduced proportion of cross-linked components in the extracted collagen. A decrease in lysine-derived aldehyde levels was found in both skin collagen and aortic elastin similar to that found in lathyritic tissue. Furthermore the in vitro formation of lysine-derived aldehyde was reduced. Thus the cause of the connective tissue abnormalities in these mice appears to be a defect in cross-link formation due to an impairment in aldehyde formation.

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