Expression of cDNA encoding the human “protective protein≓ associated with lysosomal β-galactosidase and neuraminidase: Homology to yeast proteases

Galjart, Niels; Gillemans, Nynke; Harris, Alan; Horst, Gijsbertus T. J. van der; Verheijen, Frans W.; Galjaard, H.; d’Azzo, Alessandra

doi:10.1016/s0092-8674(88)90999-3

Cited by 220 publications

(177 citation statements)

References 35 publications

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“…AAR87281) are each 41% identical to the human retinoid-inducible SCP (Chen et al, 2001) but only 21% to 25% identical to any other plant SCPL proteins outside of Clade VI. Clade III stands apart from the other clades in that it contains exclusively animal SCPL proteins, including the human SCP lysosomal protective protein also known as cathepsin A (Galjart et al, 1988;Fig. 1C).…”

Section: Animal and Fungal Scpl Proteins Help To Define Four Additionmentioning

confidence: 99%

“…Proteins that contain this catalytic triad and are otherwise homologous to SCPs have been found in a variety of organisms (Doi et al, 1980;Kim and Hayashi, 1983;Breddam, 1986;Baulcombe et al, 1987;Galjart et al, 1988;Bradley, 1992;Degan et al, 1994;Endrizzi et al, 1994;Wajant et al, 1994;Jones et al, 1996;Li and Steffens, 2000). Many of these serine carboxypeptidase-like (SCPL) proteins have been annotated as peptidases based only on this shared sequence similarity; however, studies have shown that some of them function not as peptidases, but as acyltransferases and lyases (Wajant et al, 1994;Lehfeldt et al, 2000;Li and Steffens, 2000;Shirley et al, 2001).…”

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An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

2005

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The Arabidopsis (Arabidopsis thaliana) genome encodes a family of 51 proteins that are homologous to known serine carboxypeptidases. Based on their sequences, these serine carboxypeptidase-like (SCPL) proteins can be divided into several major clades. The first group consists of 21 proteins which, despite the function implied by their annotation, includes two that have been shown to function as acyltransferases in plant secondary metabolism: sinapoylglucose:malate sinapoyltransferase and sinapoylglucose:choline sinapoyltransferase. A second group comprises 25 SCPL proteins whose biochemical functions have not been clearly defined. Genes encoding representatives from both of these clades can be found in many plants, but have not yet been identified in other phyla. In contrast, the remaining SCPL proteins include five members that are similar to serine carboxypeptidases from a variety of organisms, including fungi and animals. Reverse transcription PCR results suggest that some SCPL genes are expressed in a highly tissue-specific fashion, whereas others are transcribed in a wide range of tissue types. Taken together, these data suggest that the Arabidopsis SCPL gene family encodes a diverse group of enzymes whose functions are likely to extend beyond protein degradation and processing to include activities such as the production of secondary metabolites.Serine carboxypeptidases (SCPs) are members of the a/b hydrolase family of proteins, which make use of a Ser-Asp-His catalytic triad to cleave the carboxyterminal peptide bonds of their protein or peptide substrates (Hayashi et al., 1973(Hayashi et al., , 1975Bech and Breddam, 1989;Liao and Remington, 1990;Liao et al., 1992;Ollis et al., 1992). Proteins that contain this catalytic triad and are otherwise homologous to SCPs have been found in a variety of organisms (Doi et al., 1980;Kim and Hayashi, 1983;Breddam, 1986;Baulcombe et al., 1987;Galjart et al., 1988;Bradley, 1992;Degan et al., 1994;Endrizzi et al., 1994;Wajant et al., 1994;Jones et al., 1996;Li and Steffens, 2000). Many of these serine carboxypeptidase-like (SCPL) proteins have been annotated as peptidases based only on this shared sequence similarity; however, studies have shown that some of them function not as peptidases, but as acyltransferases and lyases (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000;Shirley et al., 2001). For example, several SCPL proteins have been shown to catalyze the production of plant secondary metabolites involved in herbivory defense and UV protection (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000), including the hydroxynitrile lyase from Sorghum bicolor (SbHNL) necessary for cyanogenesis, and the acyltransferases in wild tomato (Lycopersicon pennellii) that catalyze the formation 2,3,4-isobutyryl-Glc (Wajant et al., 1994;Lehfeldt et al., 2000). Two enzymes in Arabidopsis (Arabidopsis thaliana) responsible for sinapate ester biosynthesis are also SCPL proteins. Sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the formation of s...

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Section: Animal and Fungal Scpl Proteins Help To Define Four Additionmentioning

confidence: 99%

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confidence: 99%

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

2005

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“…Cathepsin A stabilizes the catalytically active conformation of sialidase and protects it against rapid proteolytic degradation in the lysosome [d'Azzo et al, 1982;van der Horst et al, 1989;Vinogradova et al, 1998]. Cathepsin A was cloned and its mutations in galactosialidosis were first characterized 15 years ago [Galjart et al, 1988], but cloning of sialidase has been hampered for almost two decades by the low tissue content and instability of this enzyme. Three groups simultaneously identified the human sialidase cDNA and gene by a homologous search in the Expressed Sequence Tags Database (dbEST, National Center for Biotechnology Information) and direct sequencing of human chromosome 6 [Bonten et al, 1996;Milner et al, 1997;Pshezhetsky et al, 1997].…”

Section: Introductionmentioning

confidence: 99%

Molecular pathology of NEU1 gene in sialidosis

Poupětová²,

et al. 2003

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Communicated by Mark H. PaalmanLysosomal sialidase (EC 3.2.1.18) has a dual physiological function; it participates in intralysosomal catabolism of sialylated glycoconjugates and is involved in cellular immune response. Mutations in the sialidase gene NEU1, located on chromosome 6p21.3, result in autosomal recessive disorder, sialidosis, which is characterized by the progressive lysosomal storage of sialylated glycopeptides and oligosaccharides. Sialidosis type I is a milder, late-onset, normosomatic form of the disorder. Type I patients develop visual defects, myoclonus syndrome, cherry-red macular spots, ataxia, hyperreflexia, and seizures. The severe early-onset form, sialidosis type II, is also associated with dysostosis multiplex, Hurler-like phenotype, mental retardation, and hepatosplenomegaly. We summarize information on the 34 unique mutations determined so far in the sialidase gene, including four novel missense and one novel nonsense mutations found in two Czech and two French sialidosis patients. The analysis of sialidase mutations in sialidosis revealed considerable molecular heterogeneity, reflecting the diversity of clinical phenotypes that make molecular diagnosis difficult. The majority of sialidosis patients have had missense mutations, many of which have been expressed; their effects on activity, stability, intracellular localization, and supramolecular organization of sialidase were studied. A structural model of sialidase allowed us to localize mutations in the sialidase molecule and to predict their impact on the tertiary structure and biochemical properties of the enzyme. Hum Mutat 22:343-352,

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“…The precursor undergoes dimerization at neutral pH and is then transported to an acidic compartment. Then it is further processed to a mature active form comprising 32-kDa and 20-kDa subunits held together by disulfide bridges (d'Azzo et al 1982;Galjart et al 1988;Bonten et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Structural and functional study of K453E mutant protective protein/cathepsin A causing the late infantile form of galactosialidosis

et al. 2000

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To clarify the molecular basis of the late infantile form of galactosialidosis, we characterized a defective protective protein/cathepsin A (PPCA) gene product with the K453E mutation newly found in an Arabic patient with this disease. Immunocytochemical, expression, and metabolic studies revealed that the precursor PPCA was synthesized but not processed to the mature form, and it was degraded in the mutant. A structural model of the mutant PPCA was constructed by amino acid substitution of 453 glutamic acid for lysine in the crystal structure of the wild type PPCA precursor reported. The results show that the K453E mutation is located at the dimer interface of the PPCA and reduces the hydrogen bond formation in the dimer. This structural change may cause instability of the PPCA dimer.

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Expression of cDNA encoding the human “protective protein≓ associated with lysosomal β-galactosidase and neuraminidase: Homology to yeast proteases

Cited by 220 publications

References 35 publications

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

Molecular pathology of NEU1 gene in sialidosis

Structural and functional study of K453E mutant protective protein/cathepsin A causing the late infantile form of galactosialidosis

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