Potential Involvement of Keratan Sulfate in the Heterogeneity of Microglia

2021 ◽  
Vol 33 (196) ◽  
pp. E135-E139
Author(s):  
Tomohiro Ohgomori ◽  
Shozo Jinno
Keyword(s):  
Keratan Sulfate

scholarly journals Characterization of New Proteomic Biomarker Candidates in Mucopolysaccharidosis Type IVA

2020 ◽  
Vol 22 (1) ◽  
pp. 226
Author(s):  
Víctor J. Álvarez ◽  
Susana B. Bravo ◽  
Maria Pilar Chantada-Vazquez ◽  
Cristóbal Colón ◽  
María J. De Castro ◽  
...  
Keyword(s):  
Keratan Sulfate ◽  
Bone Lesions ◽  
Mucopolysaccharidosis Type ◽  
Lysosomal Storage ◽  
Protein Biomarkers ◽  
Enzyme Replacement ◽  
Endurance Tests ◽  
Mps Iva ◽  
Mucopolysaccharidosis Type Iva ◽  
Potential Biomarkers

Mucopolysaccharidosis type IVA (MPS IVA) is a lysosomal storage disease caused by mutations in the N-acetylgalactosamine-6-sulfatase (GALNS) gene. Skeletal dysplasia and the related clinical features of MPS IVA are caused by disruption of the cartilage and its extracellular matrix, leading to a growth imbalance. Enzyme replacement therapy (ERT) with recombinant human GALNS has yielded positive results in activity of daily living and endurance tests. However, no data have demonstrated improvements in bone lesions and bone grow thin MPS IVA after ERT, and there is no correlation between therapeutic efficacy and urine levels of keratan sulfate, which accumulates in MPS IVA patients. Using qualitative and quantitative proteomics approaches, we analyzed leukocyte samples from healthy controls (n = 6) and from untreated (n = 5) and ERT-treated (n = 8, sampled before and after treatment) MPS IVA patients to identify potential biomarkers of disease. Out of 690 proteins identified in leukocytes, we selected a group of proteins that were dysregulated in MPS IVA patients with ERT. From these, we identified four potential protein biomarkers, all of which may influence bone and cartilage metabolism: lactotransferrin, coronin 1A, neutral alpha-glucosidase AB, and vitronectin. Further studies of cartilage and bone alterations in MPS IVA will be required to verify the validity of these proteins as potential biomarkers of MPS IVA.

scholarly journals Arterial lumican. Properties of a corneal-type keratan sulfate proteoglycan from bovine aorta.

1991 ◽  
Vol 266 (36) ◽  
pp. 24773-24777 ◽  
Author(s):  
J.L. Funderburgh ◽  
M.L. Funderburgh ◽  
M.M. Mann ◽  
G.W. Conrad
Keyword(s):  
Keratan Sulfate ◽  
Sulfate Proteoglycan

scholarly journals Membrane-bound mucins of the airway mucosal surfaces are densely decorated with keratan sulfate: revisiting their role in the Lung’s innate defense

Glycobiology ◽  
2020 ◽  
Author(s):  
Jerome Carpenter ◽  
Mehmet Kesimer
Keyword(s):  
Light Scattering ◽  
Keratan Sulfate ◽  
Mucosal Barrier ◽  
Airway Epithelial ◽  
Surface Binding ◽  
Force Microscopy ◽  
Innate Defense ◽  
Chronic Lung Diseases ◽  
Mucosal Surfaces ◽  
Membrane Bound

Abstract Understanding the basic elements of the airway mucosal surfaces and how they form a functional barrier is essential in understanding disease initiation, progression, pathogenesis and ultimately treating chronic lung diseases. Using primary airway epithelial cell cultures, atomic force microscopy (AFM), multiangle light scattering and quartz crystal micro balance with dissipation monitoring techniques, here we report that the membrane bound mucins (MBMs) found in the periciliary layer (PCL) of the airway surface are densely decorated with keratan sulfate (KS). AFM and immunoblotting show that the KS sidechains can be removed enzymatically with keratanase II (KII) treatment, and the antibody accessibility for B2729 (MUC1), MUCH4 (MUC4) and OC125 (MUC16) was substantially enhanced. Light scattering analysis confirmed that KII treatment removed ~40% of the mass from the mucin fractions. Surface binding experiments indicated that MBMs were able to pack into a tighter conformation following KS removal, suggesting that negatively charged KS sidechains play a role in mucin–mucin repulsion and contribute to “space filling” in the PCL. We also observed that soluble filtrate from the common airway pathogen Pseudomonas aeruginosa is capable of stripping KS from MBMs. Altogether, our findings indicate that KS glycosylation of MBMs may play an important role in the integrity of the airway mucosal barrier and its compromise in disease.

Immunocytochemical Study of Proteoglycans in Vocal Folds

1996 ◽  
Vol 105 (1) ◽  
pp. 6-11 ◽  
Author(s):  
Agnieszka S. Pawlak ◽  
Elizabeth Hammond ◽  
Thomas Hammond ◽  
Steven D. Gray
Keyword(s):  
Chondroitin Sulfate ◽  
Lamina Propria ◽  
Vocal Fold ◽  
Keratan Sulfate ◽  
Vocal Folds ◽  
Basement Membrane Zone ◽  
Immunocytochemical Study ◽  
Frozen Sections ◽  
Intense Staining ◽  
Immunocytochemical Techniques

We evaluated the proteoglycan composition of normal vocal folds using immunocytochemical techniques. Frozen sections of 14 normal cadaveric vocal folds were obtained within 12 hours of death and sectioned immediately. Vocal fold sections were stained with antibodies against keratan sulfate, chondroitin sulfate, heparan sulfate proteoglycan (HSPG), decorin, and hyaluronate receptor. We found that the lamina propria has diffuse staining of fibrillar components with keratan sulfate and decorin. Intense staining was observed in the vocal ligament area with keratan sulfate. The HSPG was localized to the basement membrane zone. Chondroitin sulfate, HSPG, and hyaluronate receptor were detected in the cytoplasm of interstitial cells with immunocytochemical characteristics of macrophages. The keratan sulfate distribution suggests that fibromodulin may be significant in normal vocal folds. Production of HSPG and probably versican occurs in macrophages and fibroblasts in the lamina propria.

Exploring the sulfate patterns of chondroitin sulfate/dermatan sulfate and keratan sulfate in human pancreatic cancer

2021 ◽  
Vol 205 ◽  
pp. 114339
Author(s):  
Qiang Ren ◽  
Jian Wang ◽  
Chao Liu ◽  
Ling-xin Meng ◽  
Rui-kun Qian ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Keratan Sulfate ◽  
Human Pancreatic Cancer

Biochemical defect of non-keratan-sulfate-excreting Morquio syndrome

1983 ◽  
Vol 15 (2) ◽  
pp. 265-273 ◽  
Author(s):  
Atsuko Fujimoto ◽  
Allen L. Horwitz ◽  
John M. Opitz
Keyword(s):  
Keratan Sulfate ◽  
Morquio Syndrome
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