bims-supasi 2025-06-01 papers

bims-supasi

Biomed News

on Sulfation pathways and signalling

Issue of 2025–06–01
fifteen papers selected by
Jonathan Wolf Mueller, University of Birmingham

FAM20B Gain-of-Function Blocks the Synthesis of Glycosaminoglycan Chains of Proteoglycans and Inhibits Proliferation and Migration of Glioblastoma Cells.
Design of Paromomycin and Neomycin as Sulfated and Hydrophobic Glycans to Target Heparanase-Driven Tumor Progression and Metastasis.
Investigation into the binding domains of platelet factor 4 unlocks new avenues for the design and synthesis of selective sulfated pseudo-tetrasaccharide aminoglycoside ligands.
Reprogramming FGF1 from the natural growth factor to the engineered heparan sulphate biosensor.
Systematic studies toward the synthesis of D-galactosamine-containing coumarin glycosides.
Revealing a novel Decorin-expressing tumor stromal subset in hepatocellular carcinoma via integrative analysis single-cell RNA sequencing.
Homogeneous sulfation of polyguluronic acids (poly-G-s) with Py·SO3 in DMSO and their characterization with NMR-spectroscopy.
Primary Cells from a CD46-Edited Bovine Heifer Have Reduced BVDV Susceptibility Despite Viral Adaptation to Heparan Sulfate.
Structural Features of Glypicans and their Impact on Wnt Signaling in Cancer.
Rab27a-mediated extracellular vesicle release drives astrocytic CSPG secretion and glial scarring in spinal cord injury.
Identification of Surrogate Biomarkers for Mucopolysaccharidosis Type IVA.
Shed Syndecan-4 and Its Possible Roles in Osteoarthritis.
Cholesterol Sulfate: Pathophysiological Implications and Potential Therapeutics.
An oxidized chondroitin sulfate-crosslinked and CuCDs-loaded decellularized bovine pericardium with improved anti-coagulation, pro-endothelialization and anti-calcification properties for BHVs.
TaSULTR1;2 regulates sulfur and selenium uptake in wheat.

Cells. 2025 05 14. pii: 712. [Epub ahead of print]14(10):

FAM20B Gain-of-Function Blocks the Synthesis of Glycosaminoglycan Chains of Proteoglycans and Inhibits Proliferation and Migration of Glioblastoma Cells.

Lydia Barré, Irfan Shaukat, Mohamed Ouzzine.

  Heparan sulfate (HS) and chondroitin sulfate (CS) proteoglycans (PGs) are essential regulators of many biological processes including cell differentiation, signalization, and proliferation. PGs interact mainly via their glycosaminoglycan (GAG) chains, with a large number of ligands including growth factors, enzymes, and extracellular matrix components, thereby modulating their biological activities. HSPGs and CSPGs share a common tetrasaccharide linker region, which undergoes modifications, particularly the phosphorylation of the xylose residue by the kinase FAM20B. Here, we demonstrated that FAM20B gain-of-function decreased, in a dose dependent manner, the synthesis of both CS- and HS-attached PGs. In addition, we showed that blockage of GAG chain synthesis by FAM20B was suppressed by the mutation of aspartic acid residues D289 and D309 of the catalytic domain. Interestingly, we bring evidence that, in contrast to FAM20B, expression of the 2-phosphoxylose phosphatase XYLP increases, in a dose dependent manner, GAG chain synthesis and rescues the blockage of GAG chains synthesis induced by FAM20B. In line with previous reports, we found that FAM20B loss-of-function reduced GAG chain synthesis. Finally, we found that FAM20B inhibited proliferation and migration of glioblastoma cells, thus revealing the critical role of GAG chains of PGs in glioblastoma cell tumorigenesis. This study revealed that both gain- and loss-of-function of FAM20B led to decreased GAG chain synthesis, therefore suggesting that a balance between phosphorylation and dephosphorylation of the xylose by FAM20B and XYLP, respectively, is probably an essential factor for the regulation of the rate of PG synthesis.

Keywords:  FAM20B; glioblastoma; glycosaminoglycan synthesis; proteoglycans

DOI:  https://doi.org/10.3390/cells14100712
J Med Chem. 2025 May 28.

Design of Paromomycin and Neomycin as Sulfated and Hydrophobic Glycans to Target Heparanase-Driven Tumor Progression and Metastasis.

Hawau Abdulsalam, Livia Philip, Kartikey Singh, Malik Farhoud, Neta Ilan, Israel Vlodavsky, Hien M Nguyen.

Heparanase (HPSE) is the sole mammalian endoglycosidase that degrades heparan sulfate (HS) proteoglycans, disrupting the extracellular matrix (ECM) and promoting cancer invasion and metastasis. Although HPSE overexpression is linked to tumor progression, no clinically approved HPSE inhibitors exist. We developed aminoglycoside-based HS mimetics with defined sulfation and hydrophobic modifications to target HPSE's lipophilic pockets, a novel approach distinct from traditional HS glycans. Computational modeling showed that these mimetics engage HPSE through hydrophobic and π-π stacking interactions, enhancing affinity. The most potent compounds inhibited HPSE-driven ECM degradation, tumor cell proliferation, and invasion. In vivo, the lead candidate significantly reduced metastatic burden in B16 melanoma and MPC-11 myeloma models, showing tumor growth inhibition (TGI = 83.1%) versus SST0001 (TGI = 58.6%) and matching bortezomib. Importantly, the compound was well-tolerated with no notable toxicity. These results support HPSE as a cancer target and highlight aminoglycoside-based HS mimetics as promising therapeutics for metastatic cancer.

DOI: https://doi.org/10.1021/acs.jmedchem.5c00937
Eur J Med Chem. 2025 May 21. pii: S0223-5234(25)00557-4. [Epub ahead of print]295 117792

Investigation into the binding domains of platelet factor 4 unlocks new avenues for the design and synthesis of selective sulfated pseudo-tetrasaccharide aminoglycoside ligands.

Livia Philip, Hawau Abdulsalam, Kartikey Singh, Hien M Nguyen.

  Platelet factor 4 (PF4) is a natural chemokine that binds to negatively charged glycosaminoglycans (GAGs), including the anticoagulant heparin. The formation of the PF4-heparin complex elicits an immune response that results in platelet activation, leading to serious thrombotic complications. This study explores the structure-activity relationships (SAR) of sulfated pseudo-tetrasaccharide aminoglycoside ligands. The binding interactions of these synthetically designed compounds with heparanase (HPSE) and PF4 were systematically elucidated. Through computational design, a library of sulfated aminoglycoside ligands was synthesized in 10-13 steps from readily available paromomycin and neomycin. The SAR studies revealed that hydroxyl-capped ligands interacted with the fondaparinux-binding domain of PF4, while hydrophobic-capped ligands bound to the heparin-binding domain. Notably, steric hindrance imposed by hydrophobic groups impedes the binding of the ligands to PF4's shallow binding site. In contrast, these hydrophobic-capped ligands demonstrated a strong binding affinity for HPSE. The most selective ligands reduced the viability of HPSE-overexpressing cancer cells, highlighting their potential efficacy in modulating the enzymatic activity of HPSE. This SAR study provides a foundational framework for the design of sulfated aminoglycoside-based therapeutics with minimized adverse effects associated with PF4.

Keywords:  Heparan sulfate; Heparanase; Heparin; Paromomycin; Platelet factor 4; and Neomycin

DOI:  https://doi.org/10.1016/j.ejmech.2025.117792
Cell Commun Signal. 2025 May 28. 23(1): 248

Reprogramming FGF1 from the natural growth factor to the engineered heparan sulphate biosensor.

Krzysztof Ciura, Olimpia Sobota, Aleksandra Chorążewska, Daniel Krowarsch, Natalia Porębska, Łukasz Opaliński.

  Heparan sulphate proteoglycans (HSPGs) are cell surface and extracellular matrix proteoglycan family members, playing a key role in diverse biological activities including signal transduction or endocytosis. To date, many HSPG ligands have been identified, including growth factors interacting via sulfated domains of heparan sulphate (HS) chains. Due to significant overexpression of HSPGs in various cancers, discovering novel biomolecules capable of HSPGs recognition, which may act as HSPGs biosensors or drug carriers targeting HSPGs, is essential. Fibroblast growth factors (FGFs), mainly paracrine FGFs, are natural ligands of membrane-bound HSPGs, forming ternary signaling complex with HSPGs and fibroblast growth factor receptors (FGFRs). Here we employed the natural capability of FGF1 to bind HSPGs to develop HSPGs-specific proteinaceous probe. We identified three point mutations within FGF1 that elevate its affinity for heparin-S116R, S17K and L72R, named B, C and D respectively. Together with substitutions increasing FGF1 stability and abolishing FGF1 binding to FGFRs, we have generated eight HSPGs-specific variants. Among tested mutants, FGF1HSBCD exhibits the highest affinity for heparin and HS/HSPGs, showing over 20-fold increase in affinity for glypican-4 and requiring 0.23 M higher salt concentration for elution from heparin column compared to the initial FGF1HS molecule. Finally, we demonstrated FGF1HSBCD potential to act as a molecular sensor of HSPGs level in cancer cell lines overproducing HSPGs, implicating that FGF1HSBCD can be used as HSPGs biosensor or as a drug delivery carrier in protein-drug conjugates (PDC) targeting HSPGs.

Keywords:  Biosensor; FGF1; FGFR; HSPG; Heparan sulfate; Heparin; Protein engineering

DOI:  https://doi.org/10.1186/s12964-025-02269-x
Org Biomol Chem. 2025 May 27.

Systematic studies toward the synthesis of D-galactosamine-containing coumarin glycosides.

Hannah S Wootton, Gavin J Miller.

An O-glycosylation method for accessing coumarin glycosides is presented. We report the reaction of 6,8-difluoro-7-hydroxy-4-methylcoumarin and 4-methylumbelliferone with a variety of glycosyl imidate donors using BF3·Et2O as activator to access a series of coumarin glycosides in 64%-76% isolated yields. Several reaction parameters are evaluated including promotors, temperature and reagent equivalents. Following initial methodology development using simple D-glucose donors, D-galactosamino mono- and disaccharides are explored as substrates, showcasing applicability towards late-stage transformation of biologically relevant chondroitin sulfate glycosides. Glycosylation diastereoselectivity trends were also considered, proposing that the identity of the D-galactosamino N-protecting group and the coumarin acceptor contribute to observed anomeric product ratios. This methodology provides a convenient access to D-galactosamino-coumarin glycoconjugates and provides a benchmark for the development of related systems for biological evaluation.

DOI: https://doi.org/10.1039/d5ob00746a
Cancer Cell Int. 2025 May 26. 25(1): 194

Revealing a novel Decorin-expressing tumor stromal subset in hepatocellular carcinoma via integrative analysis single-cell RNA sequencing.

Chi Hsiao, Wen-Chieh Liao, Ju-Pi Li, Yu-Cheng Chou, Yu-Lun Chou, Jeng-Rong Lin, Chia-Hua Chen, Chiung-Hui Liu.

  Hepatocellular carcinoma (HCC) remains a leading cause of cancer-related mortality, emphasizing the need for novel therapeutic strategies. Decorin (DCN), a chondroitin sulfate proteoglycan (CSPG), has been proposed as a tumor suppressor, yet its precise role in HCC and the tumor microenvironment (TME) remains underexplored. Through integrated analyses of bulk RNA and single-cell RNA sequencing datasets, we identified a distinct tumor stromal subset highly expressing DCN and associated chondroitin sulfate (CS) synthases. Our findings revealed that DCN expression is significantly downregulated in HCC tissue, but upregulated in peri-tumor stroma, where it correlates with better prognosis and reduced capsular invasion. Western blot analysis demonstrated that CS-DCN, the glycosylated form of DCN, plays a dominant role in this context. Single-cell clustering analysis identified a unique stromal subset in HCC characterized by elevated expression of DCN, CSPGs, and CS synthases, associated with extracellular matrix (ECM) remodeling and protective barrier functions. A six-gene DCN-associated signature derived from this subset, including DCN, BGN, SRPX, CHSY3, CHST3, and CHPF, was validated as a prognostic marker for HCC. Furthermore, functional assays demonstrated that CS-DCN significantly inhibited HCC cell proliferation and invasion. Our study highlights the critical role of DCN in HCC TME and provides insights into its therapeutic potential. Modulating CSPG pathways, particularly on CS-DCN-expressing stromal cells, may offer a promising approach for improving HCC treatment and patient outcomes.

Keywords:  Chondroitin polymerizing factor; Chondroitin sulfate; Decorin; Hepatocellular carcinoma; Tumor microenvironment

DOI:  https://doi.org/10.1186/s12935-025-03811-0
Carbohydr Res. 2025 May 21. pii: S0008-6215(25)00169-7. [Epub ahead of print]554 109543

Homogeneous sulfation of polyguluronic acids (poly-G-s) with Py·SO3 in DMSO and their characterization with NMR-spectroscopy.

Karl M Ingerma, Indrek Reile, Angelica Närep, Rando Tuvikene.

Sulfated polyguluronates (poly-G) have shown promising bioactivities, including immunomodulatory, anticoagulative, antiviral and anti-inflammatory activity. However they have seen only a limited amount of structural characterization, making it difficult to determine structure-activity relationships and thus complicating their application into practice. Therefore poly-G-s were sulfated with Py·SO3 in DMSO and the resulting derivatives were systematically characterized with NMR-spectroscopy to assign the signals of sulfated residues and to identify how different sulfation patterns manifest in NMR spectra. With lower concentration of the sulfating reagent, a slight preference for G-3 was found, while with higher concentration, G-2 preference increased alongside G-2,3-disulfation. Protecting groups (PG) were additionally used to direct selectivity and thus aid structural characterization. A degree of G-2 sulfation preference was achieved with TBDMS-ether as PG, while with Bz-ester PG, G-3 preference was achieved. Degradation by β-elimination of poly-G was found to be minimal under the developed experimental conditions.

DOI: https://doi.org/10.1016/j.carres.2025.109543
Viruses. 2025 Apr 28. pii: 634. [Epub ahead of print]17(5):

Primary Cells from a CD46-Edited Bovine Heifer Have Reduced BVDV Susceptibility Despite Viral Adaptation to Heparan Sulfate.

Alexandria C Krueger, Brian L Vander Ley, Michael P Heaton, Tad S Sonstegard, Aspen M Workman.

  A precision genome edit in the bovine CD46 gene (A82LPTFS87) dramatically reduced bovine viral diarrhea virus (BVDV) susceptibility in a cloned heifer. However, pathogen evolution threatens the long-term efficacy of such interventions. Here, our aim is two-fold: first, to determine whether BVDV can adapt in vitro to use the edited CD46 receptor to infect Madin-Darby bovine kidney (MDBK) cells, and second, to evaluate the ex vivo infectivity of culture-adapted viruses in cells from the CD46-edited heifer. Serial passage of BVDV on CD46-edited MDBK cells selected for virus variants capable of CD46-independent infection. Virus genome sequencing revealed mutations in the viral ERNS gene predicted to enhance HS-mediated entry. HS adaptation was confirmed by inhibiting virus infection with heparin or Heparinase I/III treatment. A naturally occurring HS-adapted field isolate from a persistently infected calf showed similar results. However, when tested on primary cells from the CD46-edited heifer, HS-adapted viruses showed reduced infectivity in skin fibroblasts, monocytes, and lymphocytes in a manner that correlated with HS expression. Thus, although BVDV can adapt to use HS as an alternative entry receptor, HS adaptation does not overcome the protection conferred by the CD46 edit in all relevant cell types.

Keywords:  BVDV; CD46; MDBK; bovine viral diarrhea virus; cattle; gene editing; heparan sulfate

DOI:  https://doi.org/10.3390/v17050634
Proteoglycan Res. 2025 Apr;pii: e70029. [Epub ahead of print]3(2):

Structural Features of Glypicans and their Impact on Wnt Signaling in Cancer.

Hsi-En Tsao, Mitchell Ho.

  Glypicans (GPCs) are a family of cell surface proteoglycans involved in multiple signaling pathways that regulate cell fate and proliferation. They share a characteristic structure composed of a core protein with two or more heparan sulfate chains and a glycosyl-phosphatidylinositol anchor that attaches them to the cell membrane. Aberrant expression of certain glypicans such as GPC1, GPC2, and GPC3 has been found in multiple types of cancer and causes the dysregulation of Wnt, hedgehog, and other signaling pathways, making them emerging targets for cancer immunotherapy. The molecular mechanism by which glypicans interact with signaling factors will provide insights for the development of cancer therapeutics. However, the structural complexes of human glypicans with Wnt and other key signaling factors remain unsolved. In this brief review, we analyze the current protein structural evidence for glypicans, with an emphasis on their interaction with Wnt, in an effort to provide insights to understand the molecular mechanisms by which glypicans play positive or negative roles in Wnt signaling in cancer and to discuss their translational potentials.

Keywords:  Wnt signaling; cancer targets; glypicans; heparan sulfate proteoglycan; protein structure

DOI:  https://doi.org/10.1002/pgr2.70029
Biomater Adv. 2025 May 19. pii: S2772-9508(25)00184-0. [Epub ahead of print]176 214357

Rab27a-mediated extracellular vesicle release drives astrocytic CSPG secretion and glial scarring in spinal cord injury.

Nidhi Singh, Zarna Pathak, Hemant Kumar.

  Traumatic spinal cord injury (SCI) prevents axonal regeneration by impairing neuronal function and causing glial scarring. Chondroitin sulfate proteoglycans (CSPGs) from astrocytes drive this process, yet the release mechanism, potentially involving extracellular vesicles (EVs), remains unclear. Rab27a releases EVs from multivesicular bodies (MVBs) by enabling their docking and fusion with the plasma membrane. We confirmed Rab27a expression, and its localization, subsequently, EV release was validated with CD9, Alix, and TSG101 markers. Rab27a-mediated EV release was confirmed in both Rab27a-induced and Rab27a-siRNA-treated cells. Rab27a-derived EVs inhibited neuronal cell growth, while Rab27a-siRNA EVs promoted neuronal growth. Our study also observed upregulated Rab27a expression in the rat contusion model of SCI. Further analysis showed increased CSPG expression in Rab27a-induced conditions via the Rho/ROCK pathway, with altered pAkt, and β-tubulin III, levels. Immunohistochemistry confirmed CSPG/Rab27a/GFAP and CSPG/CD9 co-localization in tissue sections, verifying that Rab27a mediates EV release containing CSPG from astrocytes. These findings suggest that Rab27a plays a crucial role in CSPG release via EVs and scar formation. Functional recovery was significantly improved with Rab27a-siRNA treatment, suggesting Rab27a as a potential target for astrocytic scar modulation in SCI. The study reveals the detailed mechanistic insight of Rab27a-dependent CSPG release via EVs for sub-acute scar formation in contusion SCI.

Keywords:  Astrocytes; Chondroitin sulfate proteoglycans; Extracellular vesicles; Glial scar; Ras-associated protein Rab27a; Spinal cord injury

DOI:  https://doi.org/10.1016/j.bioadv.2025.214357
Int J Mol Sci. 2025 May 21. pii: 4940. [Epub ahead of print]26(10):

Identification of Surrogate Biomarkers for Mucopolysaccharidosis Type IVA.

Yasuhiko Ago, Shaukat Khan, Kimberly Klipner, Allison Bradford, Shunji Tomatsu.

  Mucopolysaccharidosis type IVA (MPS IVA, Morquio A syndrome) is a rare inherited disorder characterized by skeletal dysplasia due to deficient N-acetylgalactosamine-6-sulfate sulfatase activity, resulting in glycosaminoglycan (GAG) accumulation. Identifying accurate biomarkers reflecting clinical severity and therapeutic response remains challenging. This study evaluated potential surrogate biomarkers, including N-terminal pro-C-type natriuretic peptide (NT-proCNP), collagen types I and II, mono-sulfated keratan sulfate (KS), di-sulfated KS, and chondroitin-6-sulfate (C6S), in blood and urine samples from 60 patients ranging from 1 to 62 years of age. NT-proCNP levels were significantly elevated in patients of all ages and negatively correlated with growth impairment, especially after 8 years of age. Collagen type I levels significantly increased in adult patients, whereas collagen type II showed age-dependent elevations. Urinary KS, in mono- and di-sulfated forms, demonstrated moderate negative correlations with growth impairment. Moreover, NT-proCNP, mono- and di-sulfated KS in plasma, and urinary di-sulfated KS were not affected by enzyme replacement therapy in patients younger than 12 years, unlike urinary mono-sulfated KS. In conclusion, NT-proCNP has emerged as a promising independent biomarker reflecting the severity of skeletal dysplasia and possibly the near-future growth rate. These findings highlight the potential role of NT-proCNP in clinical assessment and monitoring therapeutic efficacy, addressing current unmet needs in MPS IVA management.

Keywords:  NT-proCNP; biomarkers; enzyme replacement therapy; keratan sulfate; mucopolysaccharidosis IVA; skeletal dysplasia

DOI:  https://doi.org/10.3390/ijms26104940
Biomedicines. 2025 Apr 25. pii: 1037. [Epub ahead of print]13(5):

Shed Syndecan-4 and Its Possible Roles in Osteoarthritis.

Kangping He, Haozhe Ren, Xiaohua Chen, Feng He, Yueying Zhang, Hongyun Zhang, Feifei Li, Shibin Yu.

  The specific pathogenesis of osteoarthritis (OA) remains not fully understood. As a transmembrane heparan sulfate proteoglycan, syndecan-4 (SDC4) has been proven to play an important role in the development of OA. Notably, the extracellular domain of SDC4 can be cleaved by proteolytic enzymes, leading to the release of shed SDC4 (sSDC4), which subsequently regulates various biological processes in an autocrine or paracrine manner. This review analyzed 97 publications (1987-2025) from Pubmed and the Web of Science Core Collection using specific key words (syndecan-4, shed syndecan-4, and osteoarthritis), providing a comprehensive overview of the current research on sSDC4, including its shedding enzymes and specific cleavage sites, as well as the factors and mechanisms that influence SDC4 shedding. Furthermore, it summarizes the functions of both sSDC4 and its remaining membrane-bound domain. Finally, the roles of sSDC4 in OA are discussed to identify potential therapeutic targets and explore new strategies for the treatment of OA.

Keywords:  cartilage; heparan sulfate proteoglycan; osteoarthritis; shed syndecan-4; syndecan-4

DOI:  https://doi.org/10.3390/biomedicines13051037
Biomolecules. 2025 Apr 30. pii: 646. [Epub ahead of print]15(5):

Cholesterol Sulfate: Pathophysiological Implications and Potential Therapeutics.

Xiaoqian Yu, Siman Lei, Ying Shen, Tao Liu, Jun Li, Jia Wang, Zhiguang Su.

  Cholesterol sulfate (CS) is a naturally occurring cholesterol derivative that is widely distributed across various tissues and body fluids. In humans, its biosynthesis is primarily mediated by the sulfotransferase (SULT) 2B1b (SULT2B1b). Over the years, CS has been found to play critical roles in various physiological processes, including epidermal cell adhesion, sperm capacitation, platelet adhesion, coagulation, glucolipid metabolism, bone metabolism, gut microbiota metabolism, neurosteroid biosynthesis, T-cell receptor signaling, and immune cell migration. In this review, we first introduce the endogenous regulation of CS biosynthesis and metabolism. We then highlight current advances in the understanding of the physiological roles of CS. Finally, we delve into the implications of CS in various diseases, with a particular focus on its mechanism of action and potential therapeutic applications. A comprehensive understanding of CS's physiological function, biosynthesis regulation, and role as a disease modifier offers novel insights that could pave the way for innovative therapeutic strategies targeting a wide range of conditions.

Keywords:  Alzheimer’s disease; cancer; cholesterol; gut microbiota; immune response; keratinocyte; metabolism; signal transduction; sterol; sulfotransferase

DOI:  https://doi.org/10.3390/biom15050646
J Mater Chem B. 2025 May 27.

An oxidized chondroitin sulfate-crosslinked and CuCDs-loaded decellularized bovine pericardium with improved anti-coagulation, pro-endothelialization and anti-calcification properties for BHVs.

Shubin Shi, Xu Wei, Xu Peng, Xinyun Pu, Shaoxiong Feng, Xi Gao, Xixun Yu.

With the growth of the elderly people and the development of transcatheter aortic valve replacement (TAVR) technology, bioprosthetic heart valves (BHVs) originating from the decellularized bovine pericardium (DBP) have become a favourable option for severe valvular heart disease (VHD). However, currently, available commercial bioprosthetic heart valves prepared from glutaraldehyde (GA)-crosslinked xenografts have limited durability because of various factors, including severe cytotoxicity, inflammatory response, poor pro-endothelialization ability and calcification. Therefore, the development of valve materials with better performance is urgent. In this work, we first synthesized Cu-doped carbon dots (CuCDs) with excellent biocompatibility and high stability using sodium citrate, ethylenediamine and copper chloride. Subsequently, oxidized chondroitin sulfate (OCS) was used to crosslink the decellularized bovine pericardium to obtain OCS-BP followed by loading CuCDs onto the surface of this OCS-fixed BP sample through amide bonds formed by an EDC/NHS-catalyzed reaction between the functional groups on CuCDs and OCS-BP to prepare the BHV (CuCDs-OCS-BP) with specific properties. Relevant experiments conducted both in vivo and in vitro indicate that CuCDs-OCS-BP with good stability showed improved mechanical properties, compliance and flexibility, encouraging HUVEC-cytocompatibility, excellent anti-blood cell adhesion, antithrombogenic properties, anti-inflammatory and anti-calcification properties, and a good endothelialisation ability due to the catalytic generation of endogenous nitric oxide. Overall, CuCDs-OCS-BP is a promising material for BHVs.

DOI: https://doi.org/10.1039/d5tb00827a
Plant Physiol Biochem. 2025 May 25. pii: S0981-9428(25)00599-6. [Epub ahead of print]226 110071

TaSULTR1;2 regulates sulfur and selenium uptake in wheat.

Ziyuan Yang, Zhaojun Nie, Fuqing Sui, Yi Wang, Jiayang Xu, Yupeng Zhang, Chang Li, Shiyu Qin, Haiyang Liu, Chen Yao, Peng Zhao, Hongen Liu.

  Sulfur (S) and selenium (Se) are essential nutrients for living organisms, playing a critical role in plant growth and development. The sulfate transporter (SULTR) serves as the primary carrier for sulfate uptake, transport and redistribution. However, functions of SULTRs in wheat remain completely unknown. Here, through genome-wide identification, phylogenetic analysis, gene expression pattern analysis, subcellular localization analysis and heterogenous expression in yeast and Arabidopsis, we functionally characterized wheat SULTRs. A total of 30 TaSULTR genes were identified, which can be categorized into four subfamilies in wheat. All TaSULTRs were predicted, and TaSULTR1;1, TaSULTR1;2, and TaSULTR1;3 were tested to be localized on the plasma membrane, except for the vacuolar membrane-localized TaSULTR2;1. TaSULTR1;1, TaSULTR1;2 and TaSULTR1;3, TaSULTR3;1, TaSULTR3;2 and TaSULTR3;5 and TaSULTR4;1 show high expression in roots, and TaSULTR1;1, TaSULTR1;3, TaSULTR2;1, TaSULTR3;2, TaSULTR3;3, and TaSULTR4;1 expression in shoots is upregulated by S deficiency, while TaSULTR2;1 and TaSULTR4;1 expression in root is induced by S deficiency. TaSULTR1;1, TaSULTR1;2 and TaSULTR1;3 showed sulfate and selenate transport activities when heterologously expressed in yeast. TaSULTR1;2 complemented the Arabidopsis mutant atsultr1;2 in sulfate and selenate uptake. Taken together, these results suggest that TaSULTR1;2 function in wheat S and Se uptake. The present study firstly and systematically investigated functions of SULTRs in wheat, providing basis and guidance for future wheat S and Se metabolism research and biofortification.

Keywords:  Genome-wide identification; Selenium; Sulfur; TaSULTR1；2; Transporter; Wheat

DOI:  https://doi.org/10.1016/j.plaphy.2025.110071