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Article ; Online: Delayed vascular complication after collagenase injection for Dupuytren disease.

Nordenskjöld, Jesper / Nilsson, Jonas / Kalaf, Roua / Atroshi, Isam

2023 Volume 24, Issue 1, Page(s) 837

Abstract: Background: Vascular adverse events after collagenase injection for Dupuytren disease are absent in large trials and systematic reviews. The aim of this study is to present a case series of delayed vascular complications after collagenase treatment.: ... ...

Abstract	Background: Vascular adverse events after collagenase injection for Dupuytren disease are absent in large trials and systematic reviews. The aim of this study is to present a case series of delayed vascular complications after collagenase treatment. Methods: A prospective evaluation of 1181 consecutively treated patients at one orthopedic department identified three patients reporting symptoms of possible vascular complication. Baseline demographics and description of symptoms were collected, with a physical examination documenting extension deficit and neurovascular status. All patients completed the Cold Intolerance Symptom Severity (CISS) scale (range 4-100, lower is better) and underwent Doppler sonography examination of the digital arteries. Results: All patients were treated in the small finger and two had an isolated proximal interphalangeal joint contracture. All patients had a delayed presentation of a few months, with episodes of white discoloration of the treated finger relieved within 30 min and associated with variable pain, paresthesia, stiffness and weakness. Two of the patients reported cold exposure as an episode trigger and had a pathological CISS score (40 and 36, respectively). Doppler sonography identified a nonpatent ulnar digital artery in one patient. Conclusions: Delayed vascular complication after collagenase treatment is rare, but surgeons and patients should be aware of the risk, especially when treating the small finger.
MeSH term(s)	Humans ; Dupuytren Contracture/diagnostic imaging ; Dupuytren Contracture/drug therapy ; Dupuytren Contracture/surgery ; Microbial Collagenase/adverse effects ; Treatment Outcome ; Collagenases/adverse effects ; Injections
Chemical Substances	Microbial Collagenase (EC 3.4.24.3) ; Collagenases (EC 3.4.24.-)
Language	English
Publishing date	2023-10-23
Publishing country	England
Document type	Journal Article
ZDB-ID	2041355-5
ISSN	1471-2474 ; 1471-2474
ISSN (online)	1471-2474
ISSN	1471-2474
DOI	10.1186/s12891-023-06964-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides.

Nilsson, Jonas

Glycoconjugate journal

2016 Volume 33, Issue 3, Page(s) 261–272

Abstract: The use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS(n)) for the glycoproteomic characterization of glycopeptides is a growing field of research. The N- and O-glycosylated peptides (N- and O-glycopeptides) analyzed ...

Abstract	The use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS(n)) for the glycoproteomic characterization of glycopeptides is a growing field of research. The N- and O-glycosylated peptides (N- and O-glycopeptides) analyzed typically originate from protease-digested glycoproteins where many of them are expected to be biomedically important. Examples of LC-MS(2) and MS(3) fragmentation strategies used to pursue glycan structure, peptide identity and attachment-site identification analyses of glycopeptides are described in this review. MS(2) spectra, using the CID and HCD fragmentation techniques of a complex biantennary N-glycopeptide and a core 1 O-glycopeptide, representing two examples of commonly studied glycopeptide types, are presented. A few practical tips for accomplishing glycopeptide analysis using reversed-phase LC-MS(n) shotgun proteomics settings, together with references to the latest glycoproteomic studies, are presented.
Language	English
Publishing date	2016-06
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	283770-5
ISSN	1573-4986 ; 0282-0080
ISSN (online)	1573-4986
ISSN	0282-0080
DOI	10.1007/s10719-016-9649-3
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Zs.A 2171: Show issues

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Article: Characterization of MdpS: an in-depth analysis of a MUC5B-degrading protease from

Leo, Fredrik / Lood, Rolf / Thomsson, Kristina A / Nilsson, Jonas / Svensäter, Gunnel / Wickström, Claes

Frontiers in microbiology

2024 Volume 15, Page(s) 1340109

Abstract: Oral biofilms, comprising hundreds of bacteria and other microorganisms on oral mucosal and dental surfaces, play a central role in oral health and disease dynamics. ...

Abstract	Oral biofilms, comprising hundreds of bacteria and other microorganisms on oral mucosal and dental surfaces, play a central role in oral health and disease dynamics.
Language	English
Publishing date	2024-01-18
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2024.1340109
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Article ; Online: Site-specific glycosylation of proteoglycans: A revisited frontier in proteoglycan research.

Noborn, Fredrik / Nilsson, Jonas / Larson, Göran

Matrix biology : journal of the International Society for Matrix Biology

2022 Volume 111, Page(s) 289–306

Abstract: Proteoglycans (PGs), a class of carbohydrate-modified proteins, are present in essentially all metazoan organisms investigated to date. PGs are composed of glycosaminoglycan (GAG) chains attached to various core proteins and are important for ... ...

Abstract	Proteoglycans (PGs), a class of carbohydrate-modified proteins, are present in essentially all metazoan organisms investigated to date. PGs are composed of glycosaminoglycan (GAG) chains attached to various core proteins and are important for embryogenesis and normal homeostasis. PGs exert many of their functions via their GAG chains and understanding the details of GAG-ligand interactions has been an essential part of PG research. Although PGs are also involved in many diseases, the number of GAG-related drugs used in the clinic is yet very limited, indicating a lack of detailed structure-function understanding. Structural analysis of PGs has traditionally been obtained by first separating the GAG chains from the core proteins, after which the two components are analyzed separately. While this strategy greatly facilitates the analysis, it precludes site-specific information and introduces either a "GAG" or a "core protein" perspective on the data interpretation. Mass-spectrometric (MS) glycoproteomic approaches have recently been introduced, providing site-specific information on PGs. Such methods have revealed a previously unknown structural complexity of the GAG linkage regions and resulted in identification of several novel CSPGs and HSPGs in humans and in model organisms, thereby expanding our view on PG complexity. In light of these findings, we discuss here if the use of such MS-based techniques, in combination with various functional assays, can also be used to expand our functional understanding of PGs. We have also summarized the site-specific information of all human PGs known to date, providing a theoretical framework for future studies on site-specific functional analysis of PGs in human pathophysiology.
MeSH term(s)	Animals ; Extracellular Matrix Proteins/metabolism ; Glycosaminoglycans/metabolism ; Glycosylation ; Humans ; Proteoglycans/metabolism
Chemical Substances	Extracellular Matrix Proteins ; Glycosaminoglycans ; Proteoglycans
Language	English
Publishing date	2022-07-15
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/j.matbio.2022.07.002
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Article ; Online: Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected Correlation Between Glycan Sulfation and Attachment Site Characteristics.

Noborn, Fredrik / Nilsson, Jonas / Sihlbom, Carina / Nikpour, Mahnaz / Kjellén, Lena / Larson, Göran

Molecular & cellular proteomics : MCP

2023 Volume 22, Issue 8, Page(s) 100617

Abstract: Chondroitin sulfate proteoglycans (CSPGs) control key events in human health and disease and are composed of chondroitin sulfate (CS) polysaccharide(s) attached to different core proteins. Detailed information on the biological effects of site-specific ... ...

Abstract	Chondroitin sulfate proteoglycans (CSPGs) control key events in human health and disease and are composed of chondroitin sulfate (CS) polysaccharide(s) attached to different core proteins. Detailed information on the biological effects of site-specific CS structures is scarce as the polysaccharides are typically released from their core proteins prior to analysis. Here we present a novel glycoproteomic approach for site-specific sequencing of CS modifications from human urine. Software-assisted and manual analysis revealed that certain core proteins carried CS with abundant sulfate modifications, while others carried CS with lower levels of sulfation. Inspection of the amino acid sequences surrounding the attachment sites indicated that the acidity of the attachment site motifs increased the levels of CS sulfation, and statistical analysis confirmed this relationship. However, not only the acidity but also the sequence and characteristics of specific amino acids in the proximity of the serine glycosylation site correlated with the degree of sulfation. These results demonstrate attachment site-specific characteristics of CS polysaccharides of CSPGs in human urine and indicate that this novel method may assist in elucidating the biosynthesis and functional roles of CSPGs in cellular physiology.
MeSH term(s)	Humans ; Chondroitin Sulfates/chemistry ; Chondroitin Sulfate Proteoglycans/chemistry ; Chondroitin Sulfate Proteoglycans/metabolism ; Polysaccharides ; Amino Acid Sequence
Chemical Substances	Chondroitin Sulfates (9007-28-7) ; Chondroitin Sulfate Proteoglycans ; Polysaccharides
Language	English
Publishing date	2023-07-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2075924-1
ISSN	1535-9484 ; 1535-9476
ISSN (online)	1535-9484
ISSN	1535-9476
DOI	10.1016/j.mcpro.2023.100617
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Zs.A 5599: Show issues

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Article ; Online: Prospective Study of Preferred Versus Actual Place of Death Among Swedish Palliative Cancer Patients.

Nilsson, Jonas / Bergström, Stefan / Hållberg, Hampus / Berglund, Anders / Bergqvist, Michael / Holgersson, Georg

The American journal of hospice & palliative care

2023 , Page(s) 10499091231213640

Abstract: Background: ...

Abstract	Background:
Language	English
Publishing date	2023-11-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	1074344-3
ISSN	1938-2715 ; 1049-9091
ISSN (online)	1938-2715
ISSN	1049-9091
DOI	10.1177/10499091231213640
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Zs.B 3090: Show issues

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Article ; Online: A glycomic workflow for LC-MS/MS analysis of urine glycosaminoglycan biomarkers in mucopolysaccharidoses.

Nilsson, Jonas / Persson, Andrea / Vorontsov, Egor / Nikpour, Mahnaz / Noborn, Fredrik / Larson, Göran / Blomqvist, Maria

Glycoconjugate journal

2023 Volume 40, Issue 5, Page(s) 523–540

Abstract: In recent years, several rational designed therapies have been developed for treatment of mucopolysaccharidoses (MPS), a group of inherited metabolic disorders in which glycosaminoglycans (GAGs) are accumulated in various tissues and organs. Thus, ... ...

Abstract	In recent years, several rational designed therapies have been developed for treatment of mucopolysaccharidoses (MPS), a group of inherited metabolic disorders in which glycosaminoglycans (GAGs) are accumulated in various tissues and organs. Thus, improved disease-specific biomarkers for diagnosis and monitoring treatment efficacy are of paramount importance. Specific non-reducing end GAG structures (GAG-NREs) have become promising biomarkers for MPS, as the compositions of the GAG-NREs depend on the nature of the lysosomal enzyme deficiency, thereby creating a specific pattern for each subgroup. However, there is yet no straightforward clinical laboratory platform which can assay all MPS-related GAG-NREs in one single analysis. Here, we developed and applied a GAG domain mapping approach for analyses of urine samples of ten MPS patients with various MPS diagnoses and corresponding aged-matched controls. We describe a nano-LC-MS/MS method of GAG-NRE profiling, utilizing 2-aminobenzamide reductive amination labeling to improve the sensitivity and the chromatographic resolution. Diagnostic urinary GAG-NREs were identified for MPS types IH/IS, II, IIIc, IVa and VI, corroborating GAG-NRE as biomarkers for these known enzyme deficiencies. Furthermore, a significant reduction of diagnostic urinary GAG-NREs in MPS IH (n = 2) and MPS VI (n = 1) patients under treatment was demonstrated. We argue that this straightforward glycomic workflow, designed for the clinical analysis of MPS-related GAG-NREs in one single analysis, will be of value for expanding the use of GAG-NREs as biomarkers for MPS diagnosis and treatment monitoring.
MeSH term(s)	Humans ; Aged ; Glycosaminoglycans ; Chromatography, Liquid/methods ; Tandem Mass Spectrometry/methods ; Glycomics ; Workflow ; Mucopolysaccharidoses/diagnosis ; Mucopolysaccharidoses/urine ; Biomarkers
Chemical Substances	Glycosaminoglycans ; Biomarkers
Language	English
Publishing date	2023-07-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	283770-5
ISSN	1573-4986 ; 0282-0080
ISSN (online)	1573-4986
ISSN	0282-0080
DOI	10.1007/s10719-023-10128-5
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Zs.A 2171: Show issues

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Article ; Online: Pharmacologic RNA splicing modulation: a novel mechanism to enhance neoantigen-directed anti-tumor immunity and immunotherapy response.

Elliott, Kerryn / Nilsson, Jonas / Van den Eynden, Jimmy

Signal transduction and targeted therapy

2021 Volume 6, Issue 1, Page(s) 373

MeSH term(s)	Antigens, Neoplasm/genetics ; Antigens, Neoplasm/metabolism ; Immunologic Factors ; Immunotherapy ; RNA Splicing
Chemical Substances	Antigens, Neoplasm ; Immunologic Factors
Language	English
Publishing date	2021-10-28
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2886872-9
ISSN	2059-3635 ; 2095-9907
ISSN (online)	2059-3635
ISSN	2095-9907
DOI	10.1038/s41392-021-00789-9
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Article ; Online: A macrophage-collagen fragment axis mediates subcutaneous adipose tissue remodeling in mice.

Vujičić, Milica / Broderick, Isabella / Salmantabar, Pegah / Perian, Charlène / Nilsson, Jonas / Sihlbom Wallem, Carina / Wernstedt Asterholm, Ingrid

Proceedings of the National Academy of Sciences of the United States of America

2024 Volume 121, Issue 6, Page(s) e2313185121

Abstract: Efficient removal of fibrillar collagen is essential for adaptive subcutaneous adipose tissue (SAT) expansion that protects against ectopic lipid deposition during weight gain. Here, we used mice to further define the mechanism for this collagenolytic ... ...

Abstract	Efficient removal of fibrillar collagen is essential for adaptive subcutaneous adipose tissue (SAT) expansion that protects against ectopic lipid deposition during weight gain. Here, we used mice to further define the mechanism for this collagenolytic process. We show that loss of collagen type-1 (CT1) and increased CT1-fragment levels in expanding SAT are associated with proliferation of resident M2-like macrophages that display increased CD206-mediated engagement in collagen endocytosis compared to chow-fed controls. Blockage of CD206 during acute high-fat diet-induced weight gain leads to SAT CT1-fragment accumulation associated with elevated inflammation and fibrosis markers. Moreover, these SAT macrophages' engagement in collagen endocytosis is diminished in obesity associated with elevated levels collagen fragments that are too short to assemble into triple helices. We show that such short fragments provoke M2-macrophage proliferation and fibroinflammatory changes in fibroblasts. In conclusion, our data delineate the importance of a macrophage-collagen fragment axis in physiological SAT expansion. Therapeutic targeting of this process may be a means to prevent pathological adipose tissue remodeling, which in turn may reduce the risk for obesity-related metabolic disorders.
MeSH term(s)	Mice ; Animals ; Obesity/metabolism ; Weight Gain/physiology ; Macrophages/metabolism ; Collagen/metabolism ; Inflammation/metabolism ; Collagen Type I/metabolism ; Subcutaneous Fat/metabolism ; Subcutaneous Fat/pathology ; Adipose Tissue/metabolism ; Diet, High-Fat/adverse effects
Chemical Substances	Collagen (9007-34-5) ; Collagen Type I
Language	English
Publishing date	2024-02-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2313185121
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Zs.A 1148: Show issues

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Article ; Online: N-glycoproteomic analyses of human intestinal enteroids, varying in histo-blood group geno- and phenotypes, reveal a wide repertoire of fucosylated glycoproteins.

Nilsson, Jonas / Rimkute, Inga / Sihlbom, Carina / Tenge, Victoria R / Lin, Shih-Ching / Atmar, Robert L / Estes, Mary K / Larson, Göran

Glycobiology

2024 Volume 34, Issue 6

Abstract: Human noroviruses, globally the main cause of viral gastroenteritis, show strain specific affinity for histo-blood group antigens (HBGA) and can successfully be propagated ex vivo in human intestinal enteroids (HIEs). HIEs established from jejunal stem ... ...

Abstract	Human noroviruses, globally the main cause of viral gastroenteritis, show strain specific affinity for histo-blood group antigens (HBGA) and can successfully be propagated ex vivo in human intestinal enteroids (HIEs). HIEs established from jejunal stem cells of individuals with different ABO, Lewis and secretor geno- and phenotypes, show varying susceptibility to such infections. Using bottom-up glycoproteomic approaches we have defined and compared the N-linked glycans of glycoproteins of seven jejunal HIEs. Membrane proteins were extracted, trypsin digested, and glycopeptides enriched by hydrophilic interaction liquid chromatography and analyzed by nanoLC-MS/MS. The Byonic software was used for glycopeptide identification followed by hands-on verifications and interpretations. Glycan structures and attachment sites were identified from MS2 spectra obtained by higher-energy collision dissociation through analysis of diagnostic saccharide oxonium ions (B-ions), stepwise glycosidic fragmentation of the glycans (Y-ions), and peptide sequence ions (b- and y-ions). Altogether 694 unique glycopeptides from 93 glycoproteins were identified. The N-glycans encompassed pauci- and oligomannose, hybrid- and complex-type structures. Notably, polyfucosylated HBGA-containing glycopeptides of the four glycoproteins tetraspanin-8, carcinoembryonic antigen-related cell adhesion molecule 5, sucrose-isomaltase and aminopeptidase N were especially prominent and were characterized in detail and related to donor ABO, Lewis and secretor types of each HIE. Virtually no sialylated N-glycans were identified for these glycoproteins suggesting that terminal sialylation was infrequent compared to fucosylation and HBGA biosynthesis. This approach gives unique site-specific information on the structural complexity of N-linked glycans of glycoproteins of human HIEs and provides a platform for future studies on the role of host glycoproteins in gastrointestinal infectious diseases.
MeSH term(s)	Humans ; Glycoproteins/metabolism ; Glycoproteins/chemistry ; Proteomics/methods ; Blood Group Antigens/metabolism ; Blood Group Antigens/chemistry ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Fucose/metabolism ; Fucose/chemistry ; Phenotype ; Glycosylation ; ABO Blood-Group System/metabolism ; ABO Blood-Group System/chemistry
Chemical Substances	Glycoproteins ; Blood Group Antigens ; Polysaccharides ; Fucose (28RYY2IV3F) ; ABO Blood-Group System
Language	English
Publishing date	2024-04-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwae029
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