Reaction of gold with collagenin vivo

Adam, M.; Bartl, P.; Deyl, Z.; Rosmus, Jan

doi:10.1007/bf02135400

Cited by 23 publications

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“…We found 10 dark bands in one period after treatment cither i n vivo or in vitro, while Adam et al [3,4] have recorded three or four bands in one period.…”

Section: Discussionmentioning

confidence: 43%

Investigations on the Reaction of Metals with Collagen in vivo

Adam

Kühn

1968

European Journal of Biochemistry

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After dosing rats with gold thiosulphate a hardening of the collagen can be observed that is attributed to cross-linkage of the fibrils by the gold ion. Initially no reaction takes place between gold thiosulphate and collagen in vitro. Only after the central gold ion is set free by oxidative destruction of the thiosulphate groups can it enter into a coordination complex with the side-chain groups, forming new intermolecular bonds. I n vivo the gold complex is apparently first taken up into the fibril bv virtue of electrostatic forces. In a second slower reaction tlhe thiosulphate groups are disp1ac"ed by the side The gold thiosulphate complex has been used in the therapy of rheumatoid arthritis for 40 years with beneficial effect, as a number of controlled studies has shown [i], but the mechanism of action of gold salts has yet to be elucidated. Although gold compounds may modify the course of inflammation by reacting with various enzymes, which are thus inhibited [2], we assume that a stabilization of the collagen fibrils causing reduced reactivity of the collagen (less swelling, reduced solubility, and an increased resistance to enzyme systems) could also have an important effect on the pathological processes in connective tissue.In Gold thiosulphate was obtained as sanocrysin (Na,[Au(S,O,),]) made by Ferrosan (Denmark). The tail tendons were prepared from Wistar or SpragueDawley male rats. The acid-soluble collagen was extracted from calf skin or rat skin using 0.6 M citrate buffer a t pH 3.7.chain groups resulting in the cross-linkage. Experiments on Acid-Soluble CollagenThe long-spacing segments were prepared by dialysing a 0. The segments were stained with phosphotungstic acid and uranyl acetate for electron microscopic invest,igation. I n the case of the segments prepared using gold thiosulphate cross-striation patterns visible under the electron microscope were obtained after oxidation with 0.150/, (v/v) H,O, for 16 hours at 4". Experiments on Collagen from Rat Tail TendonsThe treatment of collagen from rat tail tendons was carried out in vivo by administration of 2.0 mg gold thiosulphate per 1OOg body weight intramuscularly once a week for 11 weeks.In vitro, the tail tendons of untreated rats were soaked in 1 mM gold thiosulphate in water for 5 hours, or in 0.15O/, €I,O,, or in both solutions successively at 4" and then washed with water.The shrinkage temperature ( T s ) was measured using a polarizing microscope as described by Borasky and Nutting [6] with the fibre submerged in Britton-Robinson phosphate buffer [7] at pH 7.0, I = 0.0125. The temperature was increased a t 3" per minute.Swelling (in Britton-Robinson phosphate buffer, pH 2.3, I = 0.0125) was measured in Dogadkin's apparatus [8] as a function of the decrease in the liquid volume.

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“…We found 10 dark bands in one period after treatment cither i n vivo or in vitro, while Adam et al [3,4] have recorded three or four bands in one period.…”

Section: Discussionmentioning

confidence: 43%

Investigations on the Reaction of Metals with Collagen in vivo

Adam

Kühn

1968

European Journal of Biochemistry

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“…On the other hand it was shown that gold administred intravitally causes an increase of the cross-links concentration of the collagen molecule (Adam et al, 1964(Adam et al, , 1965. The purpose of our experiments described in this paper was to show changes of the hydrothermal stability of the collagen structure after simultaneous intravital treatment with lathyrogens and univalent gold.…”

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confidence: 97%

Modification of Lathyrogenic Factor by Univalent Gold

Adam¹,

Deyl²,

Rosmus³

1966

Pharmacology

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“…It has been previously shown that heavy metals, mainly in the chelate form, react with collagen in vivo (Adam et al,, 1964(Adam et al,, , 1968aRyback, 1968;Eberl, 1971). The evidence for this interaction was obtained by electron microscopy and, particularly in the case of gold, also by direct analytical estimation (Adam & Kdm, 1968;Deyl et al, 1970).…”

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confidence: 99%

INVESTIGATION ON THE REACTION OF MOLYBDENUM WITH COLLAGEN IN VIVO

Bíbr

Deyl

Lener

et al. 1977

International Journal of Peptide and Protein Research

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Male Wistar rats were treated with Mo in a single dose or over a period of 84 days. The course of molybdenum excretion after a single dose was expressed mathematically. It was shown that various tissues produced different excretion curves and a high retention was observed only in skin. In long‐term treatment it was possible to ascribe this retention to direct binding of molybdenum to collagen. In contrast to some other heavy metals molybdenum causes a decrease of collagen stability. The mechanism of this effect is discussed.

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Reaction of gold with collagenin vivo

Cited by 23 publications

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Investigations on the Reaction of Metals with Collagen in vivo

Investigations on the Reaction of Metals with Collagen in vivo

Modification of Lathyrogenic Factor by Univalent Gold

INVESTIGATION ON THE REACTION OF MOLYBDENUM WITH COLLAGEN IN VIVO

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