Changes in glycosylation of rat liver arylsulfatase B in relation to age

Przybyło, Małgorzata; Lityń́ska, Anna

doi:10.1016/s0047-6374(99)00109-8

Cited by 3 publications

(4 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, all glycans in GP10 are core fucosylated and this group did not decrease with age. Some previous lectin studies also indicated that there is an age-dependent decrease of fucosylation of individual proteins in both humans and animals . One study of the effects of aging on the monosaccharide composition of the cell surface in the unexposed normal human epidermis also reported a decrease in fucose .…”

Section: Discussionmentioning

confidence: 92%

“…Some previous lectin studies also indicated that there is an age-dependent decrease of fucosylation of individual proteins in both humans 34 and animals. 35 One study of the effects of aging on the monosaccharide composition of the cell surface in the unexposed normal human epidermis also reported a decrease in fucose. 36 Taken together, these data suggest that at least some types of protein fucosylation are strongly age-dependent.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Variability, Heritability and Environmental Determinants of Human Plasma N-Glycome

et al. 2008

View full text Add to dashboard Cite

Plasma glycans were analyzed in 1008 individuals to evaluate variability and heritability, as well as the main environmental determinants that affect glycan structures. By combining HPLC analysis of fluorescently labeled glycans with sialidase digestion, glycans were separated into 33 chromatographic peaks and quantified. A high level of variability was observed with the median ratio of minimal to maximal values of 6.17 and significant age-and gender-specific differences. Heritability estimates for individual glycans varied widely, ranging from very low to very high. Glycome-wide environmental determinants were also detected with statistically significant effects of different variables including diet, smoking and cholesterol levels.

show abstract

Section: Discussionmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Variability, Heritability and Environmental Determinants of Human Plasma N-Glycome

et al. 2008

View full text Add to dashboard Cite

show abstract

“…The arylsulfatase B, which is significantly important for glycosaminoglycan (dermatan and chondroityn-4 sulfates) turnover was extracted from six Wistar rats. The carbohydrate structures from each rat aged 18 days of gestation as well as 1 week, one month, one and a half, three and eighteen months were examined [101]. As a result, the sialylation has been found to increase whereas fucosylation decreases with the aging.…”

Section: Potassium Channelsmentioning

confidence: 99%

“…As a result, the sialylation has been found to increase whereas fucosylation decreases with the aging. An especially large increase has been observed in (α2-6) Neu5Ac and (α2-3) Neu5Ac between rats 3 and 18 months of age showing a change in sialylation during aging [101]. In order to investigate the alterations in sodium channels, the channels from 15 day rat embryo forebrains and postnatal states were compared.…”

Section: Potassium Channelsmentioning

confidence: 99%

Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function

Baycin-Hizal

Gottschalk

Jacobson

et al. 2014

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Voltage-gated ion channels are transmembrane proteins that regulate electrical excitability in cells and are essential components of the electrically active tissues of nerves, muscle and the heart. Potassium channels are one of the largest subfamilies of voltage sensitive channels and are among the most-studied of the voltage-gated ion channels. Voltage-gated channels can be glycosylated and changes in the glycosylation pattern can affect ion channel function, leading to neurological and neuromuscular disorders and congenital disorders of glycosylation (CDG). Alterations in glycosylation can also be acquired and appear to play a role in development and aging. Recent studies have focused on the impact of glycosylation and sialylation on ion channels, particularly for voltage-gated potassium and sodium channels. The terminal step of sialylation often affects channel activation and inactivation kinetics. The presence of sialic acids on O or N-glycans can alter the gating mechanism and cause conformational changes in the voltage-sensing domains due to sialic acid's negative charges. This manuscript will provide an overview of sialic acids, potassium and sodium channel function, and the impact of sialylation on channel activation and deactivation.

show abstract

Rat submandibular gland during the maturation process: changes in enzyme activities, protein and lectin-binding profiles.

Przybyło¹,

Lityń́ska²,

Hoja-Łukowicz³

et al. 2004

Physiol Res

View full text Add to dashboard Cite

The total protein glycosylation profile and specific activity of lysosomal enzymes were investigated in rat submandibular glands isolated from very young (1-month), young (1.5-months) and adult rats (3-months) rats. The specific activity of lysosomal hydrolases (i.e. acid phosphatase, arylsulfatases A and B, beta-N-acetyl-D-glucosaminidase, beta-galactosidase and beta-glucuronidase) decreased in parallel to increasing age of the animals. Furthermore, the thermal stability of acid phosphatase and beta-N-acetyl-D-glucosaminidase was influenced by the age of rats. Age-related changes in protein profile regarding the intensity of particular bands as well as the appearance of certain proteins limited to special age groups were also demonstrated as revealed by Coomassie and lectin staining. Moreover, the marked age-related increase in structures Man (alpha1-2, alpha1-3, alpha1-6) Man, Fuc (alpha1-6) GlcNAc as well as Gal (beta1-3) GlcNAc was observed, whereas staining with terminal NeuAc and GlcNAc showed an inverse correlation. The reaction with (beta1-6) branched N-glycans and Gal (beta1-3) Gal structures was limited to 1-month-old rats. No significant changes in a specific reaction with NeuAc (alpha2-3) Gal were observed. We speculate that the observed differences with respect to protein and glycosylation profiles between 1-month-old rats and older ones could be caused by a modification of the diet composition as well as by the functional and morphological maturation of the rat submandibular gland.

show abstract

Changes in glycosylation of rat liver arylsulfatase B in relation to age

Cited by 3 publications

References 46 publications

Variability, Heritability and Environmental Determinants of Human Plasma N-Glycome

Variability, Heritability and Environmental Determinants of Human Plasma N-Glycome

Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function

Rat submandibular gland during the maturation process: changes in enzyme activities, protein and lectin-binding profiles.

Contact Info

Product

Resources

About