Blood group A glycosphingolipid accumulation in the hair of patients with α-N-acetylgalactosaminidase deficiency

Kimura, Akihiko; Kanekura, Takuro; Saito, Yasunori; Sagawa, Kazunori; Nosaka, Mizuho; Kanzaki, Tamotsu; Tsuji, Tsutomu

doi:10.1016/j.lfs.2004.09.027

Cited by 8 publications

(4 citation statements)

References 23 publications

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“…It was reported that the hair contains glycolipids and glycoceramides . We previously indicated the presence of sterol glucoside‐type glycolipids, like ester steryl glucoside, with various fatty acids and glucosides including N‐acetyl glucoside in human hair .…”

Section: Discussionmentioning

confidence: 98%

A highly resistant structure between cuticle and cortex of human hair

Takahashi

Yoshida

2016

Intern J of Cosmetic Sci

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Section: Discussionmentioning

confidence: 98%

A highly resistant structure between cuticle and cortex of human hair

Takahashi

Yoshida

2016

Intern J of Cosmetic Sci

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“…Because type O blood is the universal donor blood type, the α-NAGAL and α-GAL enzymes have been used to seroconvert types A, B, and AB blood into type O blood 16. Individuals with defects in their α-NAGAL or α-GAL proteins abnormally process blood group A or B antigens 17,18…”

Section: Introductionmentioning

confidence: 99%

The 1.9 Å Structure of Human α-N-Acetylgalactosaminidase: The Molecular Basis of Schindler and Kanzaki Diseases

Clark

Garman

2009

Journal of Molecular Biology

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Abstractα-N-acetylgalactosaminidase (α-NAGAL, E.C. 3.2.1.49) is a lysosomal exoglycosidase that cleaves terminal α-N-acetylgalactosamine residues from glycopeptides and glycolipids. In humans, a deficiency of α-NAGAL activity results in the lysosomal storage disorders Schindler and Kanzaki diseases. To better understand the molecular defects in the diseases, we determined the crystal structure of human α-NAGAL after expressing wild type and glycosylation-deficient glycoproteins in recombinant insect cell expression systems. We measured the enzymatic parameters of our purified wild type and mutant enzymes, establishing their enzymatic equivalence. To investigate the binding specificity and catalytic mechanism of the human α-NAGAL enzyme, we determined three crystallographic complexes with different catalytic products bound in the active site of the enzyme. To better understand how individual defects in the α-NAGAL glycoprotein lead to Schindler disease, we have analyzed the effect of disease-causing mutations on the three-dimensional structure.

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“…A member of the nucleotide sugar transporter SLC35 family, SLC35E1, was found to be presented in colostrum milk (Crisà et al, 2016). The gene MED28 is expressed in the mammary gland during lactation and is related to breast cancer (Cohen-Zinder et al, 2005;Huang et al, 2012), whereas NAGA was reported to be involved in lipid metabolism (Kimura et al, 2005). Adipocytes play a vital role in lipid-related energy homeostasis and adipocytes differentiation regulator is encoded by a gene found in the region associated with TSP, MIR30D (Bartz et al, 2015).…”

Section: Candidate Genes For Tspmentioning

confidence: 99%