lysosomal storage diseases/protease

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Site-1 protease and lysosomal homeostasis.

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The Golgi-resident site-1 protease (S1P) is a key regulator of cholesterol homeostasis and ER stress responses by converting latent transcription factors sterol regulatory element binding proteins (SREPBs) and activating transcription factor 6 (ATF6), as well as viral glycoproteins to their active

A role for the autophagy regulator Transcription Factor EB in amiodarone-induced phospholipidosis.

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The antiarrhythmic agent amiodarone, a cationic amphiphilic drug, is known to induce phospholipidosis, i.e. the accumulation of phospholipids within lysosomal structures to give multi-lamellar inclusion bodies. Despite the concerns raised about phospholipidosis in the recent years, the molecular

Molecular heterogeneity in lysosomal storage diseases. Alpha-fucosidase and N-acetyl-beta-D-hexosaminidase deficiency variants.

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The availability of specific antibodies and cDNA probes for lysosomal hydrolases has revealed unexpected heterogeneity among the human inherited lysosomal storage diseases. Using alpha-fucosidase and N-acetyl-beta-D-hexosaminidase deficiency variants as examples, it has been determined that a

Cysteine protease inhibitors as chemotherapy: lessons from a parasite target.

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Papain family cysteine proteases are key factors in the pathogenesis of cancer invasion, arthritis, osteoporosis, and microbial infections. Targeting this enzyme family is therefore one strategy in the development of new chemotherapy for a number of diseases. Little is known, however, about the

Inherited lysosomal storage disease associated with deficiencies of beta-galactosidase and alpha-neuraminidase in sheep.

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Histopathologic, ultrastructural and Golgi impregnation studies disclosed lesions characteristic of a neuronal lysosomal storage disease in related sheep with onset of neurologic signs at 4-6 months. Biochemical and enzymatic evaluation disclosed storage of GM1 ganglioside, asialo-GM1, and neutral

Protease-resistant modified human β-hexosaminidase B ameliorates symptoms in GM2 gangliosidosis model.

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GM2 gangliosidoses, including Tay-Sachs and Sandhoff diseases, are neurodegenerative lysosomal storage diseases that are caused by deficiency of β-hexosaminidase A, which comprises an αβ heterodimer. There are no effective treatments for these diseases; however, various strategies aimed at restoring

The lysosomal protein cathepsin L is a progranulin protease.

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Haploinsufficiency of GRN, the gene encoding progranulin (PGRN), causes frontotemporal lobar degeneration (FTLD), the second most common cause of early-onset dementia. Receptor-mediated lysosomal targeting has been shown to regulate brain PGRN levels, and complete deficiency of PGRN is a direct

Inherited diseases caused by mutations in cathepsin protease genes.

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Lysosomal cathepsins are proteolytic enzymes increasingly recognized as prognostic markers and potential therapeutic targets in a variety of diseases. In those conditions, the cathepsins are mostly overexpressed, thereby driving the respective pathogenic processes. Although less known, there are

Pathogenic mutations cause rapid degradation of lysosomal storage disease-related membrane protein CLN6.

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One variant form of late infantile neuronal ceroid lipofuscinosis is an autosomal recessive inherited neurodegenerative lysosomal storage disorder caused by mutations in the CLN6gene. The function of the polytopic CLN6 membrane protein localized in the endoplasmic reticulum is unknown. Here we

Glial fibrillary acidic protein is elevated in the lysosomal storage disease classical late-infantile neuronal ceroid lipofuscinosis, but is not a component of the storage material.

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Classical late-infantile neuronal ceroid lipofuscinosis (LINCL) is a fatal neurodegenerative disease of children caused by mutations in TPP1, the gene encoding the lysosomal protease tripeptidyl peptidase 1. LINCL is characterized by lysosomal accumulation of storage material of which only a single

Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.

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Pycnodysostosis, an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature, maps to chromosome 1q21. Cathepsin K, a cysteine protease gene that is highly expressed in osteoclasts, localized to the pycnodysostosis region. Nonsense, missense, and stop codon

Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism.

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BACKGROUND The human 'protective protein' (HPP) forms a multi-enzyme complex with beta-galactosidase and neuraminidase in the lysosomes, protecting these two glycosidases from degradation. In humans, deficiency of HPP leads to the lysosomal storage disease galactosialidosis. Proteolytic cleavage of

Proteolytic activation of human cathepsin A.

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Galactosialidosis is a human lysosomal storage disease caused by deficiency in the multifunctional lysosomal protease cathepsin A (also known as protective protein/cathepsin A, PPCA, catA, HPP, and CTSA; EC 3.4.16.5). Previous structural work on the inactive precursor human cathepsin A (zymogen) led

Mice with Catalytically Inactive Cathepsin A Display Neurobehavioral Alterations.

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The lysosomal carboxypeptidase A, Cathepsin A (CathA), is a serine protease with two distinct functions. CathA protects β-galactosidase and sialidase Neu1 against proteolytic degradation by forming a multienzyme complex and activates sialidase Neu1. CathA deficiency causes the lysosomal storage

[Disorders of glycoprotein degradation].

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Glycoprotein consist of oligosaccharides chains covalently attached to the polypeptide backbone. They are synthesized by two pathways; sugar nucleotide pathway and dolichol pathway. The degradation of glycoproteins occurs predominantly in the lysosomes through the ordered actions of lysosomal

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