Glycosidases (fucosidases, galactosidases, glucosidases. Hexosaminidases and glucuronidase from some molluscs and vertebrates, and neuraminidase from virus)

Cabezas, JoséA.; Reglero, Ángel; Calvo, Pedro

doi:10.1016/0020-711x(83)90087-3

Cited by 38 publications

(7 citation statements)

References 112 publications

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“…Whatever the source and the origin of membrane α‐ l ‐fucosidase, our finding must be emphasized in the context of the well known occurrence of glycosydases mainly in lysosomes, but also in other subcellular fractions [39]. For integral membrane proteins, but not for serum glycoproteins, a new mechanism termed ‘reprocessing’ or intramolecular heterogeneous turnover has been described [40,41].…”

Section: Discussionmentioning

confidence: 88%

Cell surface human α‐L‐fucosidase

Cordero

Merino

Cadena

et al. 2001

European Journal of Biochemistry

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The acid a-l-fucosidase is usually found as a soluble component of lysosomes where fucoglycoconjugates are degraded. In the present investigation, we have demonstrated the existence of a cell surface protein with enzymatic a-l-fucosidase activity that crossreacts specifically with a rabbit anti-(a-l-fucosidase) Ig. By different approaches, this a-l-fucosidase, which represents 10±20% of the total cellular fucosidase activity, was detected in all the tested human cells (hemopoietic, epithelial, mesenchymal). Two bands of < 43±49 kDa were observed, although theoretical data support the possibility of having the same genetic origin that the known 50 to 55-kDa M r a-l-fucosidase. We speculate about an alternative traffic pathway for the plasma membrane a-l-fucosidase to work on the rapid turnover of glycoproteins.Keywords: a-l-fucosidase; plasma membrane; protein traffic; CD26; glycoprotein turnover.The lysosomal a-l-fucosidase (EC 3.2.1.51) is involved in the hydrolytic degradation of fucose-containing molecules. Mammalian a-l-fucosidases are multimeric forms of glycoproteins of < 53 kDa exhibiting optimal activity between pH values of 4 and 6.5 [1]. There appears to be a considerable degree of structural heterogeneity, both tissue-specific and within the same tissue. This is probably due to a different content in sialic acid residues [2,3], in addition to the two different alleles and genetic polymorphism encoded by the FUCA1 gene [4,5]. The significance of the FUCA2 gene is currently unknown [4±6].The absence or gross deficiency of a-l-fucosidase activity causes accumulation of fucoglycoconjugates, which leads to the genetic neurovisceral storage disease fucosidosis in mammals [7,8]. A new syndrome, previously known as leukocyte adhesion deficiency II, has been recently characterized as a generalized metabolic disease consisting of severe hypofucosylation of glycoconjugates [9]. Moreover, an abnormal intracellular and extracellular distribution of a-l-fucosidase is found, for example, in cystic fibrosis (decreased levels in antiserum and higher levels in skin fibroblasts) or in colon carcinomas (decreased levels in antiserum and in tumor tissue) [10±13]. In general, tissue differentiation and development through cell±cell recognition are modulated by sequential changes of the sugar chains of cell surface glycoproteins. As the expression or deletion of a-fucosyl residues linked at various positions of sugar chains of glycoproteins is one of these alterations, the role of a-l-fucosidase in these processes is of considerable interest.The majority (90±100%) of the a-l-fucosidase activity in almost all mammalian tissues investigated is in the soluble fraction [1], the human brain being the exception [14]. A serum form of a-l-fucosidase, which has attracted interest as a diagnostic marker in many clinical studies [15], has turned out to be similar to the tissue forms [4±6,16,17]. Very recently, a-l-fucosidase from rat testis and epididymal spermatozoa was found by immunocytochemistry to be associated with the outer p...

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Section: Discussionmentioning

confidence: 88%

Cell surface human α‐L‐fucosidase

Cordero

Merino

Cadena

et al. 2001

European Journal of Biochemistry

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“…In this study the authors examined long- and short-splice variants of the gene but as we are examining enzyme activity the results cannot be directly compared. α-L-Fucosidase has been much more extensively studied than L-fucokinase due to its role in fucosidosis (Cabezas et al, 1983) and is considered to have a ubiquitous distribution.…”

Section: Discussionmentioning

confidence: 99%

Enzymatic activity of α-L-fucosidase and L-fucokinase across vertebrate animal species

Honas

Glassman

Wiese

2009

Comparative Biochemistry and Physiology Part B: Biochemistry an

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The oligosaccharide portion of glycoproteins is known to modulate protein structure, function, and turnover. Our laboratory is interested in the metabolism of L-fucose, a normal constituent of eukaryotic glycoproteins. L-Fucose is unique in that it is the only levorotatory sugar utilized in mammalian systems. There is considerable interest in understanding the controls which determine the level of L-fucose attached to proteins, in order to generate stable and active glycoforms of protein for the treatment of disease. As part of a program to determine the controls on protein L-fucosylation, we have systematically determined the tissue distribution of the enzymes L-fucokinase and α-L-fucosidase in species across the vertebrate animal kingdom. In general, the level of α-L-fucosidase is higher than L-fucokinase level. The tissue with highest enzyme activity cannot be generalized, regardless of which enzyme is of interest. Furthermore, there is not a correlation between synthetic and catabolic enzyme activity within a tissue. L-Fucokinase can be detected in all tissues examined. Interestingly, we have also detected β-D-fucosidase activity, present in extraordinary levels in the liver and small intestine of snake. Whether this is due to a specific enzyme or whether it represents a broad specificity of the α-L-fucosidase is currently being investigated.

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“…In Table 1 we summarized only few examples, while in the following paragraphs remarkable work using important marine glycosyl hydrolases, used in synthesis and in hydrolysis, will be reported. Various activities were found in marine organisms such as Charonia lampas, Turbo cornutus [9], and many others [13,14]. Interest in these enzymes from marine origin has also increased for the study of phylogenetic position and feeding habits of various molluscs [15].…”

Section: Marine Ecosystem As a Source Of New Enzymes For Hydrolysis Amentioning

confidence: 99%

Marine glycosyl hydrolases in the hydrolysis and synthesis of oligosaccharides

Giordano

Andreotti

Tramice

et al. 2006

Biotechnology Journal

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The marine ecosystem can be considered a rather unexplored source of biological material (e.g. natural substances with therapeutic activity) and can also be a surprising source of enzymes carrying new and interesting catalytic activities to be applied in biocatalysis. The use of glycosyl hydrolases from marine environments dates back to the end of the 1960s and was mainly focused on the development of sensitive and reliable hydrolytic methods for the analysis of sugar chains. As a result not all the benefits of a particular enzymatic activity have been investigated, especially regarding the transglycosylation potential of these enzymes for the synthesis of glycosidic bonds. In this review, the potential of marine sources will be demonstrated reporting on the few examples found in literature for the synthesis and hydrolysis of biologically relevant oligosaccharides catalyzed by glycosyl hydrolases of marine origin. Particular emphasis is given to the synthesis of glycosidic bonds, which is easy by the use of glycosyl hydrolases. Further aspects considered in this review are applications of these biocatalysts for vegetal waste treatment in recovering useful materials, for structural identification and for preparation of target materials from new purified polysaccharides, for the synthesis or modification of food-related compounds and for glycobiology related studies.

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Glycosidases (fucosidases, galactosidases, glucosidases. Hexosaminidases and glucuronidase from some molluscs and vertebrates, and neuraminidase from virus)

Cited by 38 publications

References 112 publications

Cell surface human α‐L‐fucosidase

Cell surface human α‐L‐fucosidase

Enzymatic activity of α-L-fucosidase and L-fucokinase across vertebrate animal species

Marine glycosyl hydrolases in the hydrolysis and synthesis of oligosaccharides

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