A decrease in serum sialyltransferase levels in Alzheimer's disease

Maguire, Teresa; Gillian, A.M.; O’Mahony, Denis; Coughlan, Christine M.; Breen, Kieran C.

doi:10.1016/0197-4580(94)90149-x

Cited by 51 publications

(42 citation statements)

References 32 publications

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“…Namely, the alterations concerning both biosynthetic and catabolic pathways of nonneural glycosphingolipids (skin fibroblasts, leukocytes, serum) in AD and DS have been observed and published by several groups [7], [9], [17] and [19]. Most recent results on increased β-galactosidase activity in AD skin fibroblasts [19], based on somewhat different experimental approach, nicely confirm the observations and conclusions of other studies dealing with glycosphingolipid metabolism in AD peripheral cells.…”

Section: Commentsupporting

confidence: 77%

“…In available literature there have been only a few data referring to glycosphingolipid metabolism in AD peripheral cells. However, it has to be pointed out that the observations on glycosphingolipid metabolic alterations not only in AD but also in Down's syndrome (DS) peripheral tissues have been previously published by other groups [9] and [17], in addition to the paper by Pitto et al [19].…”

Section: Commentmentioning

confidence: 95%

“…It was a logical step further to analyze glycosphingolipid metabolism in peripheral cells. In 1994 and 1995, Maguire and colleagues showed decreased activity of GSL biosynthetic enzymes (sialyltransferases) in serum [16] and brain tissue [17] in AD and DS as compared with control samples. In our study published in 2002, the activity of several enzymes involved in ganglioside and sulfatide catabolism (β-galactosidase, β-hexosaminidase, β-hexosaminidase A and arylsulfatase A) was analyzed in leukocytes and skin fibroblasts derived from individuals with Alzheimer's disease and Down's syndrome [9].…”

Section: Commentmentioning

confidence: 99%

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Ganglioside catabolism is altered in fibroblasts and leukocytes from Alzheimer's disease patients

Kalanj-Bognar

2006

Neurobiology of Aging

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Section: Commentsupporting

confidence: 77%

Section: Commentmentioning

confidence: 95%

Section: Commentmentioning

confidence: 99%

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Ganglioside catabolism is altered in fibroblasts and leukocytes from Alzheimer's disease patients

Kalanj-Bognar

2006

Neurobiology of Aging

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“…A significant decrease in soluble sialyltransferase (ST) activity in serum was reported in a study comparing 12 AD patients with 12 age-matched controls [7]. Subsequently, it was reported that ST activity was decreased in membrane and soluble fractions from AD and control postmortem brains [8].…”

Section: Ad and Protein Sialylationmentioning

confidence: 99%

“…The roles of these O-glycans are elusive, although it has been proposed that APP processing by a-secretase, b-secretase and c-secretase occurs after O-glycosylation of APP, and that O-glycosylated APP is preferentially secreted [26,29]. Interestingly, a recent report demonstrated a new type of tyrosine O-glycosylation on short (Ab [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] to Ab [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] but not on full-length (Ab 1-38 to Ab 1-42 ) Ab fragments [27]. In a study using CSF from AD patients and nondemented controls, an increase in the short Ab fragments carrying the tyrosine-linked glycan was observed in AD patients.…”

Section: App and Glycosylationmentioning

confidence: 99%

The role of protein glycosylation in Alzheimer disease

2013

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Glycosylation is one of the most common, and the most complex, forms of post-translational modification of proteins. This review serves to highlight the role of protein glycosylation in Alzheimer disease (AD), a topic that has not been thoroughly investigated, although glycosylation defects have been observed in AD patients. The major pathological hallmarks in AD are neurofibrillary tangles and amyloid plaques. Neurofibrillary tangles are composed of phosphorylated tau, and the plaques are composed of amyloid b-peptide (Ab), which is generated from amyloid precursor protein (APP). Defects in glycosylation of APP, tau and other proteins have been reported in AD. Another interesting observation is that the two proteases required for the generation of amyloid b-peptide (Ab), i.e. c-secretase and b-secretase, also have roles in protein glycosylation. For instance, c-secretase and b-secretase affect the extent of complex N-glycosylation and sialylation of APP, respectively. These processes may be important in AD pathogenesis, as proper intracellular sorting, processing and export of APP are affected by how it is glycosylated. Furthermore, lack of one of the key components of c-secretase, presenilin, leads to defective glycosylation of many additional proteins that are related to AD pathogenesis and/or neuronal function, including nicastrin, reelin, butyrylcholinesterase, cholinesterase, neural cell adhesion molecule, v-ATPase, and tyrosine-related kinase B. Improved understanding of the effects of AD on protein glycosylation, and vice versa, may therefore be important for improving the diagnosis and treatment of AD patients.

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Dessert or Poison? The Roles of Glycosylation in Alzheimer's, Parkinson's, Huntington's Disease, and Amyotrophic Lateral Sclerosis

Yang

Zhao

2023

ChemBioChem

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Ministry of Education and Key Laboratory of Neurons and glial cells of the central nervous system (CNS) are modified by glycosylation and rely on glycosylation to achieve normal neural function. Neurodegenerative disease is a common disease of the elderly, affecting their healthy life span and quality of life, and no effective treatment is currently available. Recent research implies that various glycosylation traits are altered during neurodegenerative diseases, suggesting a potential implication of glycosylation in disease pathology. Herein, we summarized the current knowledge about glycosylation associated with Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), and Amyotrophic lateral sclerosis (ALS) pathogenesis, focusing on their promising functional avenues. Moreover, we collected research aimed at highlighting the need for such studies to provide a wealth of disease‐related glycosylation information that will help us better understand the pathophysiological mechanisms and hopefully specific glycosylation information to provide further diagnostic and therapeutic directions for neurodegenerative diseases.

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A decrease in serum sialyltransferase levels in Alzheimer's disease

Cited by 51 publications

References 32 publications

Ganglioside catabolism is altered in fibroblasts and leukocytes from Alzheimer's disease patients

Ganglioside catabolism is altered in fibroblasts and leukocytes from Alzheimer's disease patients

The role of protein glycosylation in Alzheimer disease

Dessert or Poison? The Roles of Glycosylation in Alzheimer's, Parkinson's, Huntington's Disease, and Amyotrophic Lateral Sclerosis

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