The effect of experimental diabetes on the molecular characteristics of soluble rat-tail tendon collagen

Golub, Lorne M.; Greenwald, Robert A.; Zebrowski, E.J.; Ramamurthy, N.

doi:10.1016/0005-2795(78)90477-4

Cited by 69 publications

(42 citation statements)

References 27 publications

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“…Since these mice had more than twice as high a percentage of fat as was observed in fed normal mice but were fed only two-thirds of the amount consumed by normals (Table 1), the effect of adiposity was clearly separated from that of food intake. Collagen aging was important to measure, because it is accelerated in human diabetes, as well as in an experimentally induced rat diabetes and in ob/ob mice (22)(23)(24), and its rate is known to be retarded by food restriction (25)(26)(27). In the experiments reported here, we confirmed that the rate of collagen aging is greatly accelerated by genetic obesity and retarded by food restriction.…”

Section: Discussionsupporting

confidence: 77%

Effects of food restriction on aging: separation of food intake and adiposity.

Harrison¹,

Archer²,

Astle³

1984

Proc. Natl. Acad. Sci. U.S.A.

178

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Restricted feeding of rodents increases longevity, but its mechanism of action is not understood. We studied the effects of life-long food restriction in genetically obese and normal mice of the same inbred strain in order to distinguish whether the reduction in food intake or the reduction in adiposity (percentage of fatty tissue) was the critical component in retarding the aging process. This was possible because foodrestricted obese (ob/ob) mice maintained a high degree of adiposity. In addition to determining longevities, changes with age were measured in collagen, immune responses, and -renal function. Genetically obese female mice highly congenic with the C57BL/6J inbred strain had substantially reduced longevities and increased rates of aging in tail tendon collagen and thymus-dependent immune responses, but not in urine-concentrating abilities. When their weight was held in a normal range by feeding restricted amounts, longevities were extended almost 50%, although these food-restricted ob/ob mice still had high levels of adiposity, with fat composing about half of their body weights. Their maximum longevities exceeded those of normal C57BL/6J mice and were similar to longevities of equally food-restricted normal mice that were much leaner. Food restricted ob/ob mice had greatly retarded rates of collagen aging, but the rapid losses with age in splenic immune responses were not mitigated. Thus, the extension of life-span by food restriction was inversely related to food consumption and corresponded to the aging rate of collagen. These results suggest that aging is a combination of independent processes; they show that reduced food consumption, not reduced adiposity, is the important component in extending longevity of genetically obese mice.By far the most effective method of increasing longevities in mammals is food restriction (1, 2). Substantial increases have been reported in life-spans of mice and rats whose food intake was restricted by a variety of methods (3-6), and this increase has been attributed to reduced adiposity. These studies have been thought to be relevant to human beings, because there was a continuous, direct relationship between obesity and mortality over a wide range of body weights reported in a very large study by The Society of Actuaries (7). Recently this relationship has been challenged. In surveying relevant longitudinal studies of human beings, Andres found that the lowest mortality rates were shown not by lean people but by individuals 20-30% heavier than their conventionally defined "desirable weights" (8). These conflicting findings may result from the fact that food intake is restricted in the rodent experiments, while the data on human beings, derived from height-to-weight ratios, is a rough estimate of adiposity. Two studies have suggested that adiposity is not correlated with longevity in rats (9, 10); however, the undefined genotypes in one study (9) and the small number examined for this correlation in the other (10) prevented their conclusions from being d...

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Section: Discussionsupporting

confidence: 77%

Effects of food restriction on aging: separation of food intake and adiposity.

Harrison¹,

Archer²,

Astle³

1984

Proc. Natl. Acad. Sci. U.S.A.

178

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“…Golub et al (28) have also reported that the acid-soluble collagen from streptozotocin-diabetic rats contains higher than normal amounts of ß-component and hence exhibits increased cross-linking. The increased intensity of the ß-component observed here in diabetic rats suggests that collagen chains are capable of enhanced intramolecular cross-linking since the ß-component is a dimer of α-chains.…”

Section: Discussionmentioning

confidence: 99%

“…Golub et al (28) have suggested that increased degradation of newly synthesized collagen during streptozotocin-induced diabetes might contribute to collagen deposition in the early stages. Diabetic rats treated with the plant extract and glibenclamide showed a significant decrease in total collagen content when compared to untreated diabetic rats.…”

Section: Discussionmentioning

confidence: 99%

Effect of an aqueous extract of Phaseolus vulgaris on the properties of tail tendon collagen of rats with streptozotocin-induced diabetes

Pari

Subramanian

2003

Braz J Med Biol Res

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Changes in the structural and functional properties of collagen caused by advanced glycation might be of importance for the etiology of late complications in diabetes. The present study was undertaken to investigate the influence of oral administration of aqueous pod extract (200 mg/kg body weight) of Phaseolus vulgaris, an indigenous plant used in Ayurvedic Medicine in India, on collagen content and characteristics in the tail tendon of streptozotocin-diabetic rats. In diabetic rats, collagen content (117.01 ± 6.84 mg/100 mg tissue) as well as its degree of cross-linking was increased, as shown by increased extent of glycation (21.70 ± 0.90 µg glucose/mg collagen), collagen-linked fluorescence (52.8 ± 3.0 AU/µmol hydroxyproline), shrinkage temperature (71.50 ± 2.50ºC) and decreased acid (1.878 ± 0.062 mg hydroxyproline/100 mg tissue) and pepsin solubility (1.77 ± 0.080 mg hydroxyproline/100 mg tissue). The α/ß ratio of acid-(1.69) and pepsin-soluble (2.00) collagen was significantly decreased in streptozotocin-diabetic rats. Administration of P. vulgaris for 45 days to streptozotocin-diabetic rats significantly reduced the accumulation and cross-linking of collagen. The effect of P. vulgaris was compared with that of glibenclamide, a reference drug administered to streptozotocin-diabetic rats at the dose of 600 µg/kg body weight for 45 days by gavage. The effects of P. vulgaris (collagen content, 64.18 ± 1.97; extent of glycation, 12.00 ± 0.53; collagen-linked fluorescence, 33.6 ± 1.9; shrinkage temperature, 57.0 ± 1.0; extent of cross-linking -acidsoluble collagen, 2.572 ± 0.080, and pepsin-soluble collagen, 2.28 ± 0.112) were comparable with those of glibenclamide (collagen content, 71.5 ± 2.04; extent of glycation, 13.00 ± 0.60; collagen-linked fluorescence, 38.9 ± 2.0; shrinkage temperature, 59.0 ± 1.5; extent of cross-linking -acid-soluble collagen, 2.463 ± 0.078, and pepsinsoluble collagen, 2.17 ± 0.104). In conclusion, administration of P. vulgaris pods had a positive influence on the content of collagen and its properties in streptozotocin-diabetic rats.

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“…This disagrees with our rest&s which give evidence for an ordered glucose fixation which differs from in vitro to in vivo glycosylated collagen. Such an orientated glycosylation could be related to the observed dissimilarities in the physico~hemi~a~ properties of these two types of glycosylated collagen [7,9]. For example, the directed fixation of glucose on sites of in vitro glycosylated collagen normaIly implied in cross-linkage may be proposed as an explanation for the previously observed alterations of fibrillogenesis parameters and for the absence of fiber stabilization via cross-linking of in vitro glycosylated collagen [9].…”

Section: Discussionmentioning

confidence: 92%

“…In vitro glycosylation slows the rate of fibril formation and subsequently reduces stabilization via cross-linking [9]. However, this effect cannot be observed with collagen isolated from diabetic rats [7] but both in vitro and in vivo glycosylated collagens exhibit increased potency of inducing platelet aggregation [lO,ll]. These findings led us to determine the Published by Ekevier Science Publishers B. V. distribution of non-enzymatically bound glucose in the CNBr peptides of in vitro and in vivo glycosylated type I collagen.…”

Section: Introductionmentioning

confidence: 98%

Distribution of non‐enzymatically bound glucose in in vivo and in vitro glycosylated type I collagen molecules

1984

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Non‐enzymatic glycosylation of collagen occurs both in vivo during diabetes and in vitro after incubation with glucose. Glycosylated collagen exhibits altered physicochemical and biological properties which could explain some of the complications of diabetes. To provide a mechanistic explanation of this modification the localization of bound glucose was investigated using NaB[3H]H4 reduction and CNBr cleavage. Glucose fixation is distributed mainly on the α1CB6 peptide after in vitro glycosylation whereas this distribution occurs less specifically during diabetes. It is concluded that fibrillogenesis alteration of in vitro glycosylated collagen is related to glucose fixation on free ϵNH2 sites normally implied in intermolecular interactions.

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The effect of experimental diabetes on the molecular characteristics of soluble rat-tail tendon collagen

Cited by 69 publications

References 27 publications

Effects of food restriction on aging: separation of food intake and adiposity.

Effects of food restriction on aging: separation of food intake and adiposity.

Effect of an aqueous extract of Phaseolus vulgaris on the properties of tail tendon collagen of rats with streptozotocin-induced diabetes

Distribution of non‐enzymatically bound glucose in in vivo and in vitro glycosylated type I collagen molecules

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