Canine α-<scp>l</scp>-fucosidase in relation to the enzymic defect and storage products in canine fucosidosis

Barker, Christopher; Dell, Anne; Rogers, Mark E.; Alhadeff, Jack A.; Winchester, Bryan

doi:10.1042/bj2540861

Cited by 22 publications

(9 citation statements)

References 33 publications

(33 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Absence or gross deficiency of α--fucosidase activity leads, at least in some mammals (e.g. humans and dogs), to the genetic neurovisceral storage disease fucosidosis [10,11].…”

Section: Introductionmentioning

confidence: 99%

Alteration of the isoform composition of plasma-membrane-associated rat sperm α-l-fucosidase during late epididymal maturation: comparative characterization of the acidic and neutral isoforms

Abascal

Skalaban

Grimm

et al. 1998

Biochemical Journal

View full text Add to dashboard Cite

In a previous study, evidence was provided for the presence of a novel plasma-membrane-associated neutral-pH-optimum alpha-L-fucosidase in rat sperm. In the present study, rat sperm alpha-L-fucosidase was characterized during epididymal maturation. The pH 7 activity optimum of alpha-L-fucosidase and its subunit composition (one or two closely spaced immunoreactive protein bands of about 53+/-2 kDa) did not appear to change during transit through the epididymis. Isoelectric focusing of alpha-L-fucosidase indicated the presence of a major isoform (B) with a pI near 7 in sperm from testis, caput, corpus and the proximal half of the cauda. alpha-L-Fucosidase from sperm from the distal half of the cauda, which contained a significant enrichment of sperm and alpha-L-fucosidase activity, contained isoform B and an additional minor isoform (A) with a pI near 5.2. Isoform B and small amounts of isoform A were present in sperm from the vas deferens. The two fucosidase isoforms present in sperm from the distal cauda were separated by isoelectric focusing and comparatively characterized. They had similar pH-activity curves (with optima near pH 7) and comparable apparent KM values (0.4+/-0.04 mM) for 4-methylumbelliferyl alpha-l-fucopyranoside. Preincubation of the isoforms at different temperatures indicated that isoform A is considerably more thermostable than isoform B. Immunoprecipitation studies using polyclonal antibodies against human liver alpha-L-fucosidase indicated that approx. 90% of the enzymic activity for both isoforms was immunoprecipitable under conditions that immunoprecipitated essentially all the human liver enzyme. Neuraminidase treatment of sperm alpha-L-fucosidase from distal cauda (when compared with the appropriate heat-treated control) led to disappearance of isoform A and a concomitant increase in isoform B. The overall results suggest that isoform A is derived by sialylation of isoform B near the end of epididymal maturation.

show abstract

“…Absence or gross deficiency of α--fucosidase activity leads, at least in some mammals (e.g. humans and dogs), to the genetic neurovisceral storage disease fucosidosis [10,11].…”

Section: Introductionmentioning

confidence: 99%

Alteration of the isoform composition of plasma-membrane-associated rat sperm α-l-fucosidase during late epididymal maturation: comparative characterization of the acidic and neutral isoforms

Abascal

Skalaban

Grimm

et al. 1998

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…The mature enzyme from rat liver has an approximate subunit Mr of 55000 and exists as a tetramer in the native state [2]. A deficiency of this acid hydrolase in humans and dogs results in the lysosomal storage disease fucosidosis [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Isolation and sequence analysis of a cDNA encoding rat liver α-l-fucosidase

Fisher

Aronson

1989

Biochemical Journal

View full text Add to dashboard Cite

cDNA clones for alpha-L-fucosidase were isolated from a rat liver lambda gt11 expression library by using both monospecific polyclonal antibodies against the affinity-purified enzyme and biotinylated rat liver fucosidase cDNA sequences as probes. The largest clone, lambda FC9, contained a 1522 bp full-length cDNA insert (FC9) that encoded the 434-amino acid-residue subunit (Mr 50439) of rat liver alpha-L-fucosidase. A putative signal peptide 28 amino acid residues in length preceded the sequence for the mature protein. In addition, FC9 specified for 11 nucleotide residues of 5' untranslated sequence, 78 nucleotide residues of 3' untranslated sequence and a poly(A) tail. The deduced amino acid sequence from FC9 in conjunction with the experimentally determined N-terminus of the mature enzyme suggested that rat liver fucosidase did not contain a pro-segment. However, there was the possibility of limited N-terminal processing (one to five amino acid residues) having occurred after removal of the predicted signal peptide. Amino acid sequences deduced from FC9 were co-linear with amino acid sequences measured at the N-terminus of purified fucosidase and on two of its CNBr-cleavage peptides. An unusual aspect of rat liver alpha-L-fucosidase protein structure obtained from the FC9 data was its high content of tryptophan (6%). The coding sequence from FC9 showed 82% sequence identity with that from a previously reported incomplete human fucosidase sequence [O'Brien, Willems, Fukushima, de Wet, Darby, DiCioccio, Fowler & Shows, (1987) Enzyme 38, 45-53].

show abstract

“…The absence or gross deficiency of α‐ 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].…”

mentioning

confidence: 99%

Cell surface human α‐L‐fucosidase

Cordero

Merino

Cadena

et al. 2001

European Journal of Biochemistry

View full text Add to dashboard Cite

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...

show abstract

Canine α-l-fucosidase in relation to the enzymic defect and storage products in canine fucosidosis

Cited by 22 publications

References 33 publications

Alteration of the isoform composition of plasma-membrane-associated rat sperm α-l-fucosidase during late epididymal maturation: comparative characterization of the acidic and neutral isoforms

Alteration of the isoform composition of plasma-membrane-associated rat sperm α-l-fucosidase during late epididymal maturation: comparative characterization of the acidic and neutral isoforms

Isolation and sequence analysis of a cDNA encoding rat liver α-l-fucosidase

Cell surface human α‐L‐fucosidase

Contact Info

Product

Resources

About