Acidic glycosaminoglycans in liver from five patients with mucopolysaccharidosis and mucolipidosis.

Minami, Ryoji; Abo, Katsuyuki; Tsugawa, Satoshi; Oyanagi, Kiyomitsu

doi:10.1620/tjem.134.215

Cited by 4 publications

(3 citation statements)

References 18 publications

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“…However, systematic investigations of the GAGS in various organs, especially the brains from those patients are scanty. We have previously analyzed GAGS accumulated in the livers from patients with Hurler, Hunter and Morquio syndromes (Minami et al 1979(Minami et al , 1981. In this paper, we have extended our studies on brain GAGS and gangliosides from four patients with MPS (Hurler, fetal Hurler, Hunter and Morquio syndromes).…”

mentioning

confidence: 70%

“…In this paper, we have extended our studies on brain GAGS and gangliosides from four patients with MPS (Hurler, fetal Hurler, Hunter and Morquio syndromes). Brain GAGS were isolated by a procedure described previously (Brunngraber et al 1971;Minami et al 1979Minami et al , 1981. The absence of GAGS in water and 0.25 M NaCI fractions was confirmed by electrophoresis.…”

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confidence: 99%

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Acidic glycosaminoglycans and gangliosides in the brains from four patients with genetic mucopolysaccharidosis.

Ikeno

Minami

Tsugawa³

et al. 1982

Tohoku J. Exp. Med.

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confidence: 70%

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confidence: 99%

Acidic glycosaminoglycans and gangliosides in the brains from four patients with genetic mucopolysaccharidosis.

Ikeno

Minami

Tsugawa³

et al. 1982

Tohoku J. Exp. Med.

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“…High local concentration of GAGs may be encountered also within intracellular compartments, i.e. a 30 -40-fold increase of GAG content in liver from patients with mucopolysaccharidoses was noticed (69). At physiological concentrations, GAGs increase the yields and rates of TPP I activation, allow for effective autoactivation at less acidic pH only moderately inhibiting the activity of mature enzyme generated, and at the same time, protect the enzyme against alkaline pH-induced degradation.…”

Section: Figmentioning

confidence: 99%

Glycosaminoglycans Modulate Activation, Activity, and Stability of Tripeptidyl-peptidase I in Vitro and in Vivo

Golabek

Walus

Wisniewski

et al. 2005

Journal of Biological Chemistry

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Tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysosomal exopeptidase that sequentially removes tripeptides from the N termini of polypeptides and shows a minor endoprotease activity. Mutations in TPP I lead to classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disease. TPP I proenzyme is converted in lysosomes into a mature enzyme with the assistance of another protease and is able to autoactivate in acidic pH in vitro via a unimolecular mechanism. Because autoactivation in vitro at the pH values reported for lysosomes generated inactive enzyme, we intended to determine whether physiologically relevant factors can modify this process to also make it plausible in vivo. Here, we report that high ionic strength and glycosaminoglycans (GAGs) increase yields (ionic strength) or yields and rates (GAGs) of activation, enhance degradation of liberated TPP I prosegment fragments, and switch effective autoactivation of TPP I proenzyme toward less acidic pH values (up to pH 6.0). Although ionic strength and GAGs also inhibited TPP I activity in vitro and in living cells, the degree of inhibition (from 20 to 60%) appears to be of rather limited functional significance. Importantly, binding to GAGs improved thermal stability of TPP I and protected the enzyme against alkaline pH-induced denaturation in vitro (t1 ⁄2 of mature enzyme at pH 7.4 increased by ϳ8-fold in the presence of heparin) and in vivo (ϳ2-fold higher loss of TPP I in cells deficient in GAGs than in control cells after bafilomycin A1 treatment). These findings elucidate a potent physiologically relevant mechanism of TPP I regulation by GAGs and suggest that generation of the active enzyme via autoactivation can be accomplished not only in vitro but in vivo as well.

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Heparan sulfate and dermatan sulfate from the liver of a patient with Hurler syndrome: high performance liquid chromatography of their degradation products after incubation with α-l-iduronidase-deficient fibroblasts

Minami

Igarashi

et al. 1984

Clinica Chimica Acta

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Acidic glycosaminoglycans in liver from five patients with mucopolysaccharidosis and mucolipidosis.

Cited by 4 publications

References 18 publications

Acidic glycosaminoglycans and gangliosides in the brains from four patients with genetic mucopolysaccharidosis.

Acidic glycosaminoglycans and gangliosides in the brains from four patients with genetic mucopolysaccharidosis.

Glycosaminoglycans Modulate Activation, Activity, and Stability of Tripeptidyl-peptidase I in Vitro and in Vivo

Heparan sulfate and dermatan sulfate from the liver of a patient with Hurler syndrome: high performance liquid chromatography of their degradation products after incubation with α-l-iduronidase-deficient fibroblasts

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