HYAL1_MOUSE Hyal1 ELISA tesk kit
- Known as:
- HYAL1_MOUSE Hyal1 Enzyme-linked immunosorbent assay test tesk reagent
- Catalog number:
- gen15662
- Product Quantity:
- 1
- Category:
- Peptides
- Supplier:
- Other suppliers
- Gene target:
- HYAL1_MOUSE Hyal1 ELISA tesk kit
Related genes to: HYAL1_MOUSE Hyal1 ELISA tesk kit
- Gene:
- HYAL1 NIH gene
- Name:
- hyaluronidase 1
- Previous symbol:
- -
- Synonyms:
- LUCA1, HYAL-1
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1997-10-09
- Date modifiied:
- 2018-08-02
Related products to: HYAL1_MOUSE Hyal1 ELISA tesk kit
Related articles to: HYAL1_MOUSE Hyal1 ELISA tesk kit
- Vascular calcification is a strong predictor of cardiovascular mortality and lacks effective treatment. The transformation of vascular smooth muscle cells (VSMCs) into osteoblast-like phenotypes is a key driver of calcification. This study identifies a regulatory role for Hyaluronan (HA) in VSMC osteogenic differentiation and arterial calcification. Human aortic VSMCs stimulated with high phosphate and/or pro-inflammatory cytokines (IL6 and TGF-β1) exhibited increased RUNX2, alkaline phosphatase and osteopontin expression, along with reduced contractility and elevated calcium deposition. This corresponded with reduced HA deposition and downregulation of HA synthase enzymes (HAS1, HAS2), Hyaluronidase enzymes (Hyal1), and HA binding proteins (CD44, TSG-6), whilst HAS3 and versican were upregulated. Comparable alterations in HA and protein expression were observed in an in vivo model of arterial calcification using vitamin K-deficient warfarin-fed mice. Pharmacological inhibition of HA synthesis, enzyme-mediated HA degradation and siRNA/plasmid modulation of HAS isoenzymes demonstrated a possible functional link between HA regulation and VSMC osteogenic differentiation. This study establishes HA and its associated binding proteins as key regulators of arterial calcification, highlighting a novel pathway for potential therapeutic intervention. - Source: PubMed
Publication date: 2026/05/15
Roy ShreaKane JamieGrigorieva IrinaRoche-Dugmore DylanMoore SachaSteadman RobertRaby Anne-CatherineJakulj LilySchurgers LeonLutgens EstherEringa Etto CVervloet MarcFraser DonaldMeran Soma - Hyaluronidases degrade hyaluronic acid and participate in physiological processes, including tissue remodeling and fertilization. Vertebrate and venom hyaluronidases share a conserved Asp-X-Glu catalytic motif in the β4 loop (X = Trp or Phe). Here, we investigated HYAL1, a lysosomal enzyme, and compared it with PH20, a sperm surface hyaluronidase, to elucidate how conserved aromatic residues surrounding this motif stabilize the active site, particularly under acidic conditions. In HYAL1, Tyr82 (β3' loop), Trp130 (X residue), and Trp133 form an aromatic cluster adjacent to the active site. Substitutions at these positions reduced activity at pH 4, indicating that this cluster is required to maintain a catalytically competent conformation, with Tyr82 stabilizing the β3'-β4 loops through hydrogen bonding and Trp130 and Trp133 providing aromatic stabilization, with Trp133 playing a dominant role. A Phe-Phe interaction, analogous to that in insect venom hyaluronidases (Y82F/W130F), partially rescued activity and active-site stability compared with single substitutions. In PH20, corresponding substitutions caused greater activity losses at pH 4, indicating increased structural sensitivity to acidic conditions despite its broad pH range. pH-dependent ANS fluorescence revealed more pronounced acid-induced conformational changes at pH 4 than at pH 7 in both enzymes. Molecular dynamics simulations indicated that HYAL1, PH20, and bee venom hyaluronidase retain a rigid catalytic core, with differences arising primarily from loop and domain flexibility. These findings show that aromatic interactions surrounding the Asp-X-Glu motif stabilize the active site, whereas Phe-Phe interactions represent an alternative active-site stabilization strategy in insect venom hyaluronidases. - Source: PubMed
Publication date: 2026/05/20
Nguyen KhangHo Oanh MaiVu LuyenNguyen Tu AnhTran Kiet NChoi Mal-GiLee ChangWoo - L. (Fabaceae), commonly known as spiny restharrow, is a widely distributed medicinal plant traditionally used in European and Middle Eastern phytotherapy, particularly for the management of urological and inflammatory conditions. Despite its long-standing ethnomedicinal relevance, comprehensive syntheses of its phytochemical profile and biological activities remain limited. This review aimed to summarize current evidence regarding the chemical constituents and pharmacological effects of . Four electronic databases (PubMed, Scopus, Web of Science, and SpringerLink) were searched for studies published between 1997 and 2024. The search yielded 308 records; after duplicate removal and eligibility screening, 34 studies met the inclusion criteria. The phytochemical profile of is characterized predominantly by isoflavonoids (e.g., ononin and other formononetin derivatives), triterpenes, phenolic acids, and additional polyphenolic compounds. Although the phytochemical profile of includes multiple classes of secondary metabolites, this review places particular emphasis on phenolic compounds, given their prevalence and well-documented biological activities. Experimental evidence indicates a broad spectrum of biological activities, including anti-inflammatory effects (associated with cPLA2α inhibition and cytokine modulation), antibacterial and antifungal activity, antioxidant capacity, wound-healing and dermatological benefits, as well as diuretic and anti-adhesive effects in urinary models. Additional reported properties include antiproliferative, anti-adipogenic, analgesic, and neurotrophic activities. Proposed mechanisms of action involve enzyme inhibition (e.g., Hyal-1 and COX-2), modulation of transient receptor potential (TRP) channels, redox regulation, and interference with microbial adhesion and inflammatory signaling pathways. Overall, contains bioactive compounds exhibiting a wide range of pharmacological activities supported by in vitro and in vivo studies. Among the investigated effects, anti-inflammatory, urological, and wound-healing activities appear to be the most promising targets for future research. These findings highlight its therapeutic potential while emphasizing the need for well-designed clinical studies to further validate its medicinal applications. - Source: PubMed
Publication date: 2026/05/05
Nechita Vlad-IonuțTărău Alexia-PaulaŞuster Angie-IoanaNechita Mihaela-AncuțaToiu AncaBenedec DanielaHanganu DanielaSiserman CostelDrugan CristinaOniga Ilioara - Hepatic gluconeogenesis is a critical process that generates glucose from non-carbohydrate precursors during fasting to support vital organs like the brain and red blood cells. Postprandially, this process is rapidly suppressed to allow for glucose storage as glycogen and lipids in the liver. Failure to suppress gluconeogenesis after meals leads to elevated postprandial glucose levels, a key feature of type 2 diabetes. This dynamic switch is regulated by insulin and glucagon, but insulin resistance impairs this regulation. In this study, we identified a novel mechanism involving postprandial circulating hyaluronan (HA) and lysosomal hyaluronidase-1 (HYAL1) that suppresses hepatic gluconeogenesis by rewiring hepatic metabolism and mitochondrial function. knockout ( KO) mice exhibited increased gluconeogenesis, while liver-specific overexpression (Liv-) mice showed reduced gluconeogenic activity. Transcriptomic analysis revealed minimal changes in liver gene expression due to deletion, but metabolomic profiling demonstrated that overexpression mitigated high-fat diet (HFD)-induced elevations in gluconeogenic pathway metabolites. Mechanistically, HYAL1-mediated HA digestion activates a feedback loop in HA synthesis, repartitioning the cellular uridine diphospho-N-acetyl-D-glucosamine (UDP-GlcNAc) pool. This reduces O-linked N-acetylglucosamine modification (O-GlcNAcylation) of mitochondrial ATP synthase subunits, decreasing ATP production and suppressing gluconeogenesis. Importantly, this pathway remains intact in the livers of HFD-fed, insulin-resistant mice. In summary, our findings reveal a new postprandial mechanism for regulating hepatic gluconeogenesis, highlighting the potential of enhancing postprandial HA levels or hepatic HYAL1 activity as a therapeutic strategy for managing excessive gluconeogenesis in insulin-resistant conditions, such as type 2 diabetes. - Source: PubMed
Publication date: 2025/05/13
Chen XiDogné SophieDeng YanruLi HuiqiaoMeng JieyiGiang CharliseFuncke Jan-BerndStraub Leon GDias MichelleThevananther SundararajahTong QiangKamal Abu Hena MostafaAmbati Chandra Shekar RLiu Yu'ePutluri NagireddyGao XiaChen Miao-HsuehGuan DongyinYalamanchili Hari KrishnaZhao ShangangCaron NathalieZhu Yi - Hyaluronan (HA), a polysaccharide present in tissues throughout the body, exhibits various physiological functions depending on its molecular weight. Although high-molecular-weight HA (HM-HA) is produced in large amounts in the epidermal basal layer, low-molecular-weight HA (LM-HA) exists and acts as a moisturizing factor in the epidermal stratum corneum. However, the mechanism and physiological role of the HA metabolism in the epidermis remains unknown. The present study investigated the effects of various molecular weights of HA treatments and HA metabolism-related factor knockdown on the epidermal barrier function mediated by intercellular tight junctions (TJs) using human epidermal-derived HaCaT cells. The HA-metabolizing enzymes responsible for HA production and degradation in epidermal cells were also examined. Treatment with HM-HA (1400 kDa) decreased mRNA and protein expression of claudin-1 (CLDN1), which is an essential protein in the epidermal TJ component. In contrast, no change was observed in LM- HA (3 kDa). Knockdown of the HA receptor CD44 by siRNA suppressed the HM-HA-induced CLDN1 down-regulation. Among the HA-degrading enzymes, the knockdown of hyaluronidase (HYAL) 1, decreased HA-degrading activity and increased HA content in the lysates using a competition assay with an HA-binding protein. CLDN1 expression was decreased upon HYAL1 knockdown. These results suggest that HYAL1 is the main enzyme responsible for HA degradation in human epidermal keratinocytes. HYAL1 degrades HM-HA under acidic conditions, suggesting that HYAL1 expression is involved in TJ barrier regulation. The HYAL-mediated epidermal HA metabolism regulates TJ function. In the future, it is anticipated that HA metabolism-targeting novel therapeutics will be developed for skin diseases associated with TJ barrier dysfunction. - Source: PubMed
Publication date: 2026/03/23
Yoshino YutaGenkawa NatsukiHirose MaiNakamura SotaTanaka ToshihiroMiyamoto ChikaEndo SatoshiIkari Akira