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> Disorders > Disease or Syndrome > Pseudo-Hurler Polydystrophy

Pseudo-Hurler Polydystrophy

Pseudo-Hurler Polydystrophy: A rare lysosomal storage disorder characterized by a deficiency in the enzyme alpha-L-iduronidase.
This leads to the accumulation of glycosaminoglycans, causing progressive skeletal, cardiac, and neurological abnormalities.
Patients may exhibit corase facial features, joint stiffness, and impaired intellegence.
Early diagnosis and appropriate treatment are crucial for managing this condition and improving patient outcomes.

Most cited protocols related to «Pseudo-Hurler Polydystrophy»

1
Nucleosome Isolation and Chromatin Immunoprecipitation
For native ChIP, 2–5 × 107 cells were collected and resuspended in 2 ml of ice cold buffer I (0.32 M Sucrose, 60 mM KCl, 15 mM NaCl, 5 mM MgCl2, 0.1 mM EGTA, 15 mM Tris [pH 7.5], 0.5 mM DTT, 0.1 mM PMSF, 1:1000 protease inhibitor cocktail [Sigma]). 2 ml of ice cold buffer I supplemented with 0.1% IGEPAL was added and placed on ice for 10 min. The resulting 4 ml of nuclei was gently layered on top of 8 ml of ice cold buffer III (1.2 M Sucrose, 60 mM KCl, 15 mM NaCl, 5 mM MgCl2, 0.1 mM EGTA, 15 mM Tris [pH 7.5], 0.5 mM DTT, 0.1 mM PMSF, 1:1000 protease inhibitor cocktail) and centrifuged at 10,000 × g for 20 min at 4°C with no brake. Pelleted nuclei were resuspended in buffer A (0.34 M sucrose, 15 mM Hepes [pH 7.4], 15 mM NaCl, 60 mM KCl, 4 mM MgCl2, 1 mM DTT, 0.1 mM PMSF, 1:1000 protease inhibitor cocktail (Sigma)) to 400 ng/ul. MNase (Affymetrix) digestion reactions were carried out on 100 µg or more chromatin using 0.9–2.8 U/µg chromatin in buffer A supplemented with 3 mM CaCl2 for 10 min at 37°C. The reaction was quenched with 5 mM EGTA on ice and centrifuged at 13,500 × g for 10 min. The chromatin was resuspended in 10 mM EDTA [pH 8.0], 1 mM PMSF, 1:1000 protease inhibitor cocktail and rotated at 4°C for 2–4 h. The mixture was adjusted to 500 mM NaCl, allowed to rotate for another 45 min and then centrifuged at 13,500 × g for 10 min yielding nucleosomes in the supernatant. 100 µg or more of chromatin was diluted to 100 ng/µl with buffer B (20 mM Tris [pH 8.0], 5 mM EDTA, 500 mM NaCl, 0.2% Tween 20) and pre-cleared with 60 µl 50% protein G bead (GE Healthcare) slurry for 20 min at 4°C. 1–2 µg of the pre-cleared supernatant (bulk nucleosomes) was saved for further processing. To the remaining supernatant, antibody was added and rotated overnight at 4°C. Immunocomplexes were recovered by addition of 100 µl 50% protein G bead slurry followed by rotation at 4°C for 3 h. The beads were washed three times with buffer B, and once with buffer B without Tween. For the input fraction, an equal volume of input recovery buffer (0.6 M NaCl, 20 mM EDTA, 20 mM Tris [pH 7.5], 1% SDS) and 1 µl of RNAse A (10 mg/ml) was added followed by incubation for one hour at 37°C. 100µg/ml Proteinase K (Roche) was then added and was incubated for another 3 h at 37°C. For the ChIP fraction, 300 µl of ChIP recovery buffer (20 mM Tris [pH 7.5], 20 mM EDTA, 0.5% SDS, 500 µg/ml Proteinase K) was added directly to the beads and incubated for 3–4 hrs at 56°C. The resulting Proteinase K-treated samples were subjected to a phenol-chloroform extraction followed by purification using a Qiagen MinElute column. For crosslinked ChIP, 2–5 × 107 cells were processed with the SimpleChIP Enzymatic Chromatin IP Kit (Cell Signaling) using the manufacturer’s recommendations. Unamplified bulk nucleosomes or ChIP DNA was analyzed using Agilent 2100 Bionanalyzer High Sensitivity Kit. The Bioanalyzer determines the quantity of DNA based on fluorescence intensity. Antibodies used for ChIP: mouse α-CENP-A monoclonal (15 µg, ab13939 (Abcam)); rabbit α-H3K9me3 polyclonal (10 µg, ab8898 (Abcam)); rabbit α-H3.3 polyclonal (17 µg, 09–838 (Millipore)).
Hasson D., Panchenko T., Salimian K.J., Salman M.U., Sekulic N., Alonso A., Warburton P.E, & Black B.E. (2013). The octamer is the major form of CENP-A nucleosomes at human centromeres. Nature structural & molecular biology, 20(6), 687-695.
Publication 2013
Antibodies Buffers Cell Nucleus Cells Chloroform Chromatin Cold Temperature Dietary Fiber Digestion DNA Chips Edetic Acid Egtazic Acid Endopeptidase K Enzymes Fluorescence G-substrate HEPES Hypersensitivity Immunoglobulins Immunoprecipitation, Chromatin Magnesium Chloride Mus Nucleosomes Phenol Protease Inhibitors Pseudo-Hurler Polydystrophy Rabbits Ribonucleases Sodium Chloride Sucrose Tromethamine Tween 20 Tweens
2
Nucleosome Isolation and Chromatin Immunoprecipitation
For native ChIP, 2–5 × 107 cells were collected and resuspended in 2 ml of ice cold buffer I (0.32 M Sucrose, 60 mM KCl, 15 mM NaCl, 5 mM MgCl2, 0.1 mM EGTA, 15 mM Tris [pH 7.5], 0.5 mM DTT, 0.1 mM PMSF, 1:1000 protease inhibitor cocktail [Sigma]). 2 ml of ice cold buffer I supplemented with 0.1% IGEPAL was added and placed on ice for 10 min. The resulting 4 ml of nuclei was gently layered on top of 8 ml of ice cold buffer III (1.2 M Sucrose, 60 mM KCl, 15 mM NaCl, 5 mM MgCl2, 0.1 mM EGTA, 15 mM Tris [pH 7.5], 0.5 mM DTT, 0.1 mM PMSF, 1:1000 protease inhibitor cocktail) and centrifuged at 10,000 × g for 20 min at 4°C with no brake. Pelleted nuclei were resuspended in buffer A (0.34 M sucrose, 15 mM Hepes [pH 7.4], 15 mM NaCl, 60 mM KCl, 4 mM MgCl2, 1 mM DTT, 0.1 mM PMSF, 1:1000 protease inhibitor cocktail (Sigma)) to 400 ng/ul. MNase (Affymetrix) digestion reactions were carried out on 100 µg or more chromatin using 0.9–2.8 U/µg chromatin in buffer A supplemented with 3 mM CaCl2 for 10 min at 37°C. The reaction was quenched with 5 mM EGTA on ice and centrifuged at 13,500 × g for 10 min. The chromatin was resuspended in 10 mM EDTA [pH 8.0], 1 mM PMSF, 1:1000 protease inhibitor cocktail and rotated at 4°C for 2–4 h. The mixture was adjusted to 500 mM NaCl, allowed to rotate for another 45 min and then centrifuged at 13,500 × g for 10 min yielding nucleosomes in the supernatant. 100 µg or more of chromatin was diluted to 100 ng/µl with buffer B (20 mM Tris [pH 8.0], 5 mM EDTA, 500 mM NaCl, 0.2% Tween 20) and pre-cleared with 60 µl 50% protein G bead (GE Healthcare) slurry for 20 min at 4°C. 1–2 µg of the pre-cleared supernatant (bulk nucleosomes) was saved for further processing. To the remaining supernatant, antibody was added and rotated overnight at 4°C. Immunocomplexes were recovered by addition of 100 µl 50% protein G bead slurry followed by rotation at 4°C for 3 h. The beads were washed three times with buffer B, and once with buffer B without Tween. For the input fraction, an equal volume of input recovery buffer (0.6 M NaCl, 20 mM EDTA, 20 mM Tris [pH 7.5], 1% SDS) and 1 µl of RNAse A (10 mg/ml) was added followed by incubation for one hour at 37°C. 100µg/ml Proteinase K (Roche) was then added and was incubated for another 3 h at 37°C. For the ChIP fraction, 300 µl of ChIP recovery buffer (20 mM Tris [pH 7.5], 20 mM EDTA, 0.5% SDS, 500 µg/ml Proteinase K) was added directly to the beads and incubated for 3–4 hrs at 56°C. The resulting Proteinase K-treated samples were subjected to a phenol-chloroform extraction followed by purification using a Qiagen MinElute column. For crosslinked ChIP, 2–5 × 107 cells were processed with the SimpleChIP Enzymatic Chromatin IP Kit (Cell Signaling) using the manufacturer’s recommendations. Unamplified bulk nucleosomes or ChIP DNA was analyzed using Agilent 2100 Bionanalyzer High Sensitivity Kit. The Bioanalyzer determines the quantity of DNA based on fluorescence intensity. Antibodies used for ChIP: mouse α-CENP-A monoclonal (15 µg, ab13939 (Abcam)); rabbit α-H3K9me3 polyclonal (10 µg, ab8898 (Abcam)); rabbit α-H3.3 polyclonal (17 µg, 09–838 (Millipore)).
Hasson D., Panchenko T., Salimian K.J., Salman M.U., Sekulic N., Alonso A., Warburton P.E, & Black B.E. (2013). The octamer is the major form of CENP-A nucleosomes at human centromeres. Nature structural & molecular biology, 20(6), 687-695.
Publication 2013
Antibodies Buffers Cell Nucleus Cells Chloroform Chromatin Cold Temperature Dietary Fiber Digestion DNA Chips Edetic Acid Egtazic Acid Endopeptidase K Enzymes Fluorescence G-substrate HEPES Hypersensitivity Immunoglobulins Immunoprecipitation, Chromatin Magnesium Chloride Mus Nucleosomes Phenol Protease Inhibitors Pseudo-Hurler Polydystrophy Rabbits Ribonucleases Sodium Chloride Sucrose Tromethamine Tween 20 Tweens
3
Chromatin Immunoprecipitation Sequencing Protocol

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Publication 2017
Antibodies Bicarbonate, Sodium BRD4 protein, human Buffers Cell Nucleus Cells Chloroform Chromatin Chromatin Immunoprecipitation Sequencing Cold Temperature CTGF protein, human Deoxycholic Acid Dietary Fiber Digestion DNA-Directed DNA Polymerase DNA Chips DNA Library Edetic Acid Egtazic Acid Endopeptidase K Enzymes Glycine HEPES histone H3 trimethyl Lys4 Hypersensitivity Immunoglobulins IP 20 Magnesium Chloride MED1 protein, human Mus Nonidet P-40 Nucleosomes Pellets, Drug Phenol Polynucleosomes Protease Inhibitors Pseudo-Hurler Polydystrophy Rabbits Ribonucleases Sodium Chloride Staphylococcal Protein A Sucrose Technique, Dilution Tromethamine Tween 20 Tweens
4
RNA Extraction and cDNA Synthesis from Plasma
From each plasma specimen, ∼20,000 viral RNA copies were extracted using the QIAamp Viral RNA Mini kit (QIAGEN). RNA was eluted and immediately subjected to cDNA synthesis. Reverse transcription of RNA to single-stranded cDNA was performed using SuperScript III reverse transcription according to manufacturer’s recommendations (Invitrogen). In brief, each cDNA reaction included 1× RT buffer, 0.5 mM of each deoxynucleoside triphosphate, 5 mM dithiothreitol, 2 U/ml RNaseOUT (RNase inhibitor), 10 U/ml of SuperScript III reverse transcription, and 0.25 mM antisense primer SIVsm/macEnvR1 5′-TGTAATAAATCCCTTCCAGTCCCCCC-3′ (nt 9454–9479 in SIVmac239). The mixture was incubated at 50°C for 60 min, followed by an increase in temperature to 55°C for an additional 60 min. The reaction was then heat-inactivated at 70°C for 15 min and treated with 2 U of RNase H at 37°C for 20 min. The newly synthesized cDNA was used immediately or frozen at −80°C.
Keele B.F., Li H., Learn G.H., Hraber P., Giorgi E.E., Grayson T., Sun C., Chen Y., Yeh W.W., Letvin N.L., Mascola J.R., Nabel G.J., Haynes B.F., Bhattacharya T., Perelson A.S., Korber B.T., Hahn B.H, & Shaw G.M. (2009). Low-dose rectal inoculation of rhesus macaques by SIVsmE660 or SIVmac251 recapitulates human mucosal infection by HIV-1. The Journal of Experimental Medicine, 206(5), 1117-1134.
Publication 2009
Anabolism Buffers Dithiothreitol DNA, Complementary Endoribonucleases Freezing Oligonucleotide Primers Plasma Pseudo-Hurler Polydystrophy Reverse Transcription Ribonuclease H RNA, Viral triphosphate
5
Carbohydrate-Ligand-Binding Assay for VLPs
As described previously [20 (link),25 (link)], EIA plates were coated with 10 μg/ml PGM type III (Sigma Aldrich) diluted in PBS and blocked with 5% Blotto in PBS/0.05% Tween 20. VLPs (0.5 μg/ml) were pretreated with decreasing concentrations of serum for 1 h before being added to the carbohydrate-ligand-coated plates for 1 h. Ligand-bound VLP was detected with rabbit anti-GI or -GII or -GII.4 VLP hyperimmune serum followed by anti-rabbit-IgG-HRP (GE Healthcare). All tested VLPs, except for GII.4.2012 and GII.4.2006b.P.D302, were components of the VLP cocktails used to immunize rabbits. Multivalent GII.4 VLP immunization resulted in broadly reactive serum that recognizes GII.4.2012 and GII.4.2006b.P.D302 [44 (link)]. Wash steps, Ab dilutions, and color development were completed as described above. All incubations were done at room temperature. The percent control binding was defined as the binding level in the presence of Ab pretreatment divided by the binding level in the absence of Ab pretreatment multiplied by 100. Blockade data were fit using sigmoidal dose–response analysis of nonlinear data in GraphPad Prism 6.02. EC50 values were calculated for sera that demonstrated blockade of at least 50% at the dilution series (40–20480) tested. Sera that did not block 50% of binding at the highest concentration tested were assigned an EC50 of 20 for statistical comparison.
Lindesmith L.C., Ferris M.T., Mullan C.W., Ferreira J., Debbink K., Swanstrom J., Richardson C., Goodwin R.R., Baehner F., Mendelman P.M., Bargatze R.F, & Baric R.S. (2015). Broad Blockade Antibody Responses in Human Volunteers after Immunization with a Multivalent Norovirus VLP Candidate Vaccine: Immunological Analyses from a Phase I Clinical Trial. PLoS Medicine, 12(3), e1001807.
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Publication 2015
anti-IgG Carbohydrates Cardiac Arrest Ligands Oryctolagus cuniculus prisma Pseudo-Hurler Polydystrophy Rabbits Serum Technique, Dilution Tween 20 Vaccination

Most recents protocols related to «Pseudo-Hurler Polydystrophy»

1
Multiparameter Flow Cytometry Analysis
Flow cytometry analyses were performed using a BD Fortessa LSRII flow cytometer (BD Biosciences). Cells were prepared from peripheral blood, bone marrow (through flushing by centrifugation), and spleen (through crushing), lysed in red blood cell lysis buffer (155 mM NH4Cl, 12 mM NaHCO3, 0.1 mM EDTA) for 5 minutes at 4°C and washed in PBS + 1% FBS before staining. Bone marrow and spleen cells were lineage depleted using the stem cell technologies hematopoietic progenitor isolation kit as per the manufacturer’s instructions (StemCell technologies #19856) before staining. Cells were stained with cell surface antibodies (key resources table) in PBS + 1% FBS for 1 hour at 4°C, washed 3 times in PBS + 1% FBS and resuspended in PBS + 1% FBS + 4′,6-diamidino-2-phenylindole (0.1 μg/mL) before analysis by flow cytometry. For intracellular flow cytometry, cells were first stained with cell surface antibodies and fixable live dead dye (either Zombie UV Biolegend or Sytox Green Life Technologies) followed by fixation in 1.6% formaldehyde (Sigma) at room temperature for 10 minutes in the dark and permeabilized in 1 mL Perm buffer III (BD biosciences) on ice for 30 minutes in the dark. Cells were washed 3 times in PBS + 1% FBS and incubated with intracellular antibodies for 4 hours at 4°C. Stained cells were washed three times in PBS + 1% FBS and analyzed by flow cytometry.
Grey W., Atkinson S., Rix B., Casado P., Ariza-McNaughton L., Hawley C., Sopoena M.L., Bridge K.S., Kent D., Cutillas P.R, & Bonnet D. (2023). The CKS1/CKS2 Proteostasis Axis Is Crucial to Maintain Hematopoietic Stem Cell Function. HemaSphere, 7(3), e853.
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Publication 2023
Antibodies Bicarbonate, Sodium BLOOD Bone Marrow Buffers Cells Centrifugation Edetic Acid Erythrocytes Flow Cytometry Formaldehyde isolation Progressive Encephalomyelitis with Rigidity Protoplasm Pseudo-Hurler Polydystrophy Receptors, Antigen, B-Cell Spleen Stem, Plant Stem Cells Stem Cells, Hematopoietic SYTOX Green
2
Isolation of Immune Cells and Breast Cancer Cells from Tumor Samples
Primary CD45+ immune cells, CD8+ tumor-infiltrating lymphocytes (TIL), and breast cancer cells were isolated from breast carcinoma samples obtained from biopsies or surgery. Briefly, tissues were cut into fragments of approximately 1 mm3 and then digested by enzymatic hydrolysate [DMEM (Gibco, #C11995500BT) supplemented with 10% FBS (Gibco, #10099141C), 1.5 mg/mL collagenase type I (Worthington, #LS004196), 1.5 mg/mL collagenase type III (Worthington, #LS004182), and 1.5 mg/mL hyaluronidase (Sigma-Aldrich, #H3506)] at 37°C with gentle agitation for 2 hours for cancer cell isolation and 1 hour for immune cell isolation. The dissociated tissues were resuspended and filtered through a 70-μm cell strainer to obtain single-cell suspensions. Thereafter, cancer cells were acquired through centrifugation at 250 × g for 5 minutes and purified using EpCAM Microbeads (Miltenyi Biotec, #130-061-101). To isolate immune cells, primary cell suspensions were centrifuged at 400 × g for 5 minutes and then CD8+ TILs were purified using CD8 Microbeads (Miltenyi Biotec, #130-045-201). CD45+ immune cells were isolated by fluorescence-activated cell sorting (FACS) using a BD Influx flow cytometer (see “FACS”). After isolation, cell purity was determined by flow cytometry (>95%).
Lao L., Zeng W., Huang P., Chen H., Jia Z., Wang P., Huang D., Chen J., Nie Y., Yang L., Wu W, & Liu J. (2023). CD8+ T cell–Dependent Remodeling of the Tumor Microenvironment Overcomes Chemoresistance. Cancer Immunology Research, 11(3), 320-338.
Publication 2023
Biopsy Breast Carcinoma Cells Cell Separation Centrifugation Collagenase Collagenase, Clostridium histolyticum Enzymes Flow Cytometry Hyaluronidase isolation Lymphocytes, Tumor-Infiltrating Malignant Neoplasms Microspheres Operative Surgical Procedures Pseudo-Hurler Polydystrophy TACSTD1 protein, human Tissues
3
Fabrication of Organic Solar Cells with MBTR:PC71BM Blend
The OSCs were fabricated with the conventional ITO/PEDOT:PSS/MBTR:PC71BM(w/w)/Au structure. Transparent ITO glass was critically cleaned in an ultrasonic bath using 2 mL hellmanex III solution in 200 mL hot water for 5 min. Next, the substrates were sequentially cleaned with DI water, acetone, and ethanol each for 10 min and dried in a vacuum oven. Further, the cleaned substrates were placed in UV–ozone equipment and exposed to UV–ozone for surface treatment for 15 min to remove the surface impurities and improve adhesion properties. We used solar-grade PEDOT:PSS (HTL Solar) for deposition of the buffer layer, which was filtered through a 0.45 μm polytetrafluoroethylene (PTFE) filter using a rubber-free syringe. The freshly prepared PEDOT:PSS solution was spin coated on the cleaned substrates at the rate of 4000 RPM for 30 s and annealed over a previously heated hot plate. Varying blend ratio (w/w) solutions were prepared by mixing MBTR and PC71BM in absolute chlorobenzene using a constant concentration of 30 mg/mL. The blend solution with 3% DIO additive for optimized devices was prepared in a volume ratio of chlorobenzene/DIO (97/3 v/v%) with a fixed active material concentration of 30 mg/mL. Next, the blend solution with and without DIO was spin-coated on ITO/PEDOT:PSS at a rate of 3000 RPM for 40 s and immediately baked at 80 °C for 10 min. Finally, the ITO/PEDOT:PSS/MBTR:PC71BM-deposited substrate was placed in a shadow mask, and a metal electrode layer of Au (gold) was thermally evaporated under a high vacuum of 1 × 10−6 Torr. The BHJ PV devices were fabricated at ambient temperature with an active area of 0.12 cm2.
A.b.d.u.l.l.a.h., Lee S.J., Park J.B., Kim Y.S., Shin H.S., Kotta A., Siddiqui Q.T., Lee Y.S, & Seo H.K. (2023). Linear-Shaped Low-Bandgap Asymmetric Conjugated Donor Molecule for Fabrication of Bulk Heterojunction Small-Molecule Organic Solar Cells. Molecules, 28(4), 1538.
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Publication 2023
Acetone Bath Buffers chlorobenzene Ethanol Gold Medical Devices Metals Osteopathia striata cranial sclerosis Ozone Polytetrafluoroethylene Pseudo-Hurler Polydystrophy Rubber Syringes Ultrasonics Vacuum
4
Determination of Fe(III) Reduction Activity
The FRA was determined as described by García et al. [56 (link)]. Previously to determine FRA, plants were subjected to a pre-treatment for 30 min in plastic vessels with 50 mL of a nutrient solution without micronutrients, pH 5.5. Then they were transferred into 50 mL of a Fe (III) reduction assay solution for 1 h. This assay solution consisted of nutrient solution without micronutrients, 100μM Fe(III)-EDTA and 300 μM Ferrozine, pH was adjusted to 5.0 with KOH. The environmental conditions during the measurement of Fe (III) reduction were the same as the growth conditions described above. FRA was determined spectrophotometrically by measuring the absorbance (562 nm) of the Fe(II)-Ferrozine complex and by using an extinction coefficient of 29.800 M−1 cm−1. After that, roots were excised and weighed, and the results were expressed on a root fresh weight basis. Also, SPAD values (as a proxy of the chlorophyll concentration in leaf) were measured daily with a portable chlorophyllmeter (SPAD 502 Minolta Camera Co., Osaka, Japan).
García-Espinoza F., Quesada-Moraga E., García del Rosal M.J, & Yousef-Yousef M. (2023). Entomopathogenic Fungi-Mediated Solubilization and Induction of Fe Related Genes in Melon and Cucumber Plants. Journal of Fungi, 9(2), 258.
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Publication 2023
Biological Assay Blood Vessel Chlorophyll A Edetic Acid Extinction, Psychological Ferrozine Micronutrients Nutrients Plant Leaves Plant Roots Plants Pseudo-Hurler Polydystrophy SPAD
5
Fluorescence-based Assay for Salicylic Acid
For quantifying the concentration of SA, different concentrations of SA were mixed with 200 nM of Tn in reaction buffer at 37 °C for 30 min, and then 30 U/mL of Exo I and 50 U/mL of Exo III were added and incubated for 30 min at 37 °C. Next, 80 μM of CuSO4 and 1 mM of Vc were added into the reaction system for 10 min at room temperature. An F-2700 fluorescence spectrophotometer was used to measure the fluorescence intensity. For verifying the application of this assay, different concentrations of SA in 1% human serum were measured.
Xiao Q., Chen M., Nie W., Xie F., Yu X, & Ma C. (2023). A Fluorescent Biosensor for Streptavidin Detection Based on Double-Hairpin DNA-Templated Copper Nanoparticles. Biosensors, 13(2), 168.
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Publication 2023
Biological Assay Buffers Fluorescence Homo sapiens Pseudo-Hurler Polydystrophy Serum

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Collagenase 3 by Worthington
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Collagenase III is a laboratory enzyme used for the digestion of collagen. It functions by breaking down the collagen matrix, which is a key component of the extracellular matrix in various tissues. This enzyme is commonly used in cell isolation and tissue dissociation procedures.
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Collagenase type 3 by Worthington
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Collagenase type III is a purified enzyme derived from Clostridium histolyticum. It is used for the digestion and dissociation of connective tissue, such as cartilage and other extracellular matrices.
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Hyaluronidase is an enzyme used in laboratory settings. It functions by breaking down hyaluronic acid, a component of the extracellular matrix.
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More about "Pseudo-Hurler Polydystrophy"

Pseudo-Hurler Polydystrophy, also known as Mucopolysaccharidosis type IIIA (MPS IIIA), is a rare lysosomal storage disorder characterized by a deficiency in the enzyme alpha-L-iduronidase.
This deficiency leads to the accumulation of glycosaminoglycans, such as heparan sulfate and dermatan sulfate, within the body's cells.
The progressive buildup of these complex carbohydrates can cause a wide range of physical, cognitive, and neurological abnormalities in affected individuals.
Patients may exhibit coarse facial features, joint stiffness, impaired intellligence, and a range of other skeletal, cardiac, and neurological issues.
Early diagnosis and appropriate treatment, which may include enzyme replacement therapy, hematopoietic stem cell transplantation, or other management strategies, are crucial for improving patient outcomes and quality of life.
Researchers investigating Pseudo-Hurler Polydystrophy often utilize techniques and reagents like Collagenase III, Collagenase type III, DNase I, Filipin III, FBS, Hyaluronidase, and Perm Buffer III to study the underlying mechanisms and develop new therapeutic approaches.
By understanding the complex nature of this rare disorder and the latest research advances, clinicians and scientists can work together to provide the best possible care and support for individuals affected by Pseudo-Hurler Polydystrophy.