Experimental Lathyrism: Apparent Antithesis of Aging in Connective Tissue

Bickley, Harmon C.

doi:10.1111/j.1532-5415.1964.tb05021.x

Cited by 12 publications

(3 citation statements)

References 62 publications

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“…A definite increase was demonstrated in the lathyritic aorta and became most marked at 21 days (table 1 and fig. DISCUSSION The basic mechanism responsible for the development of dissecting aneurysm in angiolathyrism is still a matter of dispute.25, 26 Biochemical investigation of the lathyritic aorta, has been conducted only by Grant et a1.~3 and girtschafter and Bentley. DISCUSSION The basic mechanism responsible for the development of dissecting aneurysm in angiolathyrism is still a matter of dispute.25, 26 Biochemical investigation of the lathyritic aorta, has been conducted only by Grant et a1.~3 and girtschafter and Bentley.…”

Section: Methodsmentioning

confidence: 99%

Angiolathyrism

Hosoda

Iri

1967

Angiology

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The term &dquo;angiolathyrism&dquo; has been used to characterize the dissecting aneurysm' and other vascular lesions produced by administration of sweet pea seeds or lathyrogenic chemicals .2, 3 The nature of the lathyritic aneurysm still remains in doubt. Many workers have recognized an increase in acid mucopolysaccharides in the lathyritic aortic media, 4-13 while others have demonstrated an increase in soluble collagen. 14, 15 Chemical changes of elastin are not well documented, although some morphological alterations have been observed with light and electron&dquo;, 16-19 microscopy. Grant et a1.13 have reported no quantitative difference in elastin content between the lathyritic and control rat aorta after a 25-day, 50 per cent Lathyrus odoratus diet.We have observed that dissecting aneurysms first occur after approximately 20 days on a lathyrogenic diet, and we believe that the structural and biochemical changes of the aorta during this period may play a role in the development of the dissecting aneurysm in angiolathyrism. MATERIALS AND METHODSTwenty-one-day-old weanling male rats of the Sprague-Dawley strain were fed ad libitum with powdered commercial rat meal (CE-2 rat meal, Central Laboratory for Experimental Animal, Tokyo) containing /3-aminopropionitrile fumarate (Abbott Laboratory, lot no. 744-7354) in a concentration of 0.4 per cent. Control rats were fed ad libitum with basal powdered meal.Aortas of 20 rats were collected at days 7, 14 and 21 of the dietary period. Each aorta was excised under ether anesthesia, carefully avoiding the surrounding soft tissue.As the control, 20 rat aortas of 21, 28, 35 and 42 days of age were collected in the same fashion. The aortas were finely minced and disintegrated with acetone in a Universal homogenizer, then maintained for 24 hr. at 38° C in acetone. After three changes of acetone, the samples were dried and ground in a mortar.

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Section: Methodsmentioning

confidence: 99%

Angiolathyrism

Hosoda

Iri

1967

Angiology

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“…This has been demonstrated by an increase in lathyritic tissues of immature neutral salt-soluble collagen Gross and Levene, 1959). On the basis of these observations, it has been suggested that experimental lathyrism is the apparent antithesis of ageing in connective tissue (Bickley, 1964). The purpose of this study was to test this hypothesis, that lathyrism is indeed the antithesis of ageing, and to determine what implications a change in cartilage permeability in experimental lathyrism might have on the pathogenesis of this disease.…”

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Changes in permeability of articular cartilage in experimental lathyrism.

Aleo¹,

Miller²,

Karmilowicz³

1969

Annals of the Rheumatic Diseases

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“…The induction of lathyrism in animals increases the solubility of tissue collagen (Levene & Gross, 1959;Glimcher, Friberg, Orloff & Gross, 1965;Levene, Kranzler & Franco-Browder, 1966;Bickley, 1964;Gross, 1963), including the normally insoluble collagen of bone (Levene & Gross, 1959; and cartilage (Levene et al 1966). The effect of the lathyrogens on the protein-polysaccharide components of connective tissues is, however, less clear.…”

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The solubilization of collagen and protein–polysaccharides from the developing cartilage of lathyrytic chicks

Glimcher

Seyer

Brickley

1969

Biochemical Journal

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1. The solubilization of collagen and protein-polysaccharides from the developing cartilage of normal and lathyritic chicks was studied by using mild extraction procedures. One-third of the protein-polysaccharides could be solubilized in salt solutions at neutral pH from normal cartilage, whereas 95-100% could be extracted from the cartilage of animals that were severely lathyritic. Likewise, whereas in normal animals the collagen of cartilage was essentially insoluble in salt solutions at neutral pH, in lathyritic animals it was almost completely soluble. 2. The increased solubility of the collagen of cartilage from lathyritic animals enabled sufficient material to be collected so that the pure alpha1 chains of the collagen were isolated by repeated reconstitution, precipitation and CM-cellulose column chromatography. The purified alpha1 component was characterized by its relatively high content of hydroxylysine (14 residues/1000 amino acids). 3. About 37% of the collagen from the cartilage of normal chick embryos could be extracted as the gelatin at pH7.4 in lithium chloride solution. This was accompanied by the extraction of approx. 14% of the protein-polysaccharide content. 4. The protein-polysaccharides and the collagen from normal animals could be extracted from the cartilage relatively independently of one another under mild conditions. These same components obtained from lathyritic animals easily separated from one another after solubilization. This provided evidence that the two components are probably not covalently cross-linked. 5. The collagen of cartilage extracted as a gelatin from normal animals contained a high proportion of alpha chains compared with beta dimers, similar to the lathyritic collagen of cartilage and other tissues, and similar to the gelatin extracted from normal chick bone.

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Experimental Lathyrism: Apparent Antithesis of Aging in Connective Tissue

Cited by 12 publications

References 62 publications

Angiolathyrism

Angiolathyrism

Changes in permeability of articular cartilage in experimental lathyrism.

The solubilization of collagen and protein–polysaccharides from the developing cartilage of lathyrytic chicks

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