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Dendritic cells (DCs) docked to the basolateral surface of lymphatic vessels and transited to the lumen through hyaluronan-mediated interactions with the lymph-specific endothelial receptor LYVE-1. Targeted deletion of the gene Lyve1, antibody blockade or depletion of the DC hyaluronan coat not only delayed lymphatic trafficking of dermal DCs but also blunted their capacity to prime CD8 (show CD8A Proteins)(+) T cell responses in LNs.
These findings reveal binding is dependent not just on clustering but also on the biochemical properties of LYVE-1 homodimers. They also mark LYVE-1 as the first Link protein (show HAPLN1 Proteins) superfamily member requiring covalent homodimerization for function and suggest the interchain disulfide acts as a redox switch in vivo.
LYVE1 expression is significantly upregulated in human masticatory mucosa during wound healing
Immunostaining analyses in psoria (show VEGFA Proteins)sis skin lesions suggested that the ectodomain shedding of LYVE-1 occurred in lymphatic vessels undergoing chronic inflammation. These results indicate that the ectodomain shedding of LYVE-1 might be involved in promoting pathological lymphangiogenesis.
These results demonstrate the prerequisite of a critical LYVE-1 threshold density and show that hyaluronan binding may be elicited in lymphatic endothelium by surface clustering with divalent LYVE-1 mAbs.
We have established a novel, three-protein biomarker panel that is able to detect patients with early-stage pancreatic cancer in urine specimens:LYVE-1, REG1A (show REG1A Proteins), and TFF1 (show TFF1 Proteins) were selected as candidate biomarkers
Data (including data from studies in knockout mice) suggest LYVE1 mediates adhesion of group A Streptococci (GAS) to lymphatic vesicular endothelium via capsular hyaluronan; this appears to be critical factor for lymphatic trafficking of GAS in vivo.
High expression of LYVE-1 is associated with atherosclerotic arteries.
Data indicate that detection of lymphatic vascular invasion (LVI) can be optimized by specific D2-40 or LYVE-1 staining.
High-low cell surface HA content of tumor cells through the interaction with LYVE-1 leads to adhesion differences.
the LYVE-1-expressing cells might be involved in the uptake of hyaluronan and other waste products as well as foreign particles circulating in the blood and lymph while participating in the subsequent degradation in relay with adjacent macrophage populations.
Immunostaining analyses in VEGF-A (show VEGFA Proteins) transgenic skin suggested that the ectodomain shedding of LYVE-1 occurred in lymphatic vessels undergoing chronic inflammation. These results indicate that the ectodomain shedding of LYVE-1 might be involved in promoting pathological lymphangiogenesis.
Endogenous hyaluronan on the surface of macrophages can engage LYVE-1, facilitating their adhesion and transit across lymphatic endothelium.
MT1-MMP (show MMP14 Proteins) directly cleaves LYVE-1 on lymphatic endothelial cells to inhibit LYVE-1-mediated lymphangiogenic responses and restrains the production of VEGF-C (show VEGFC Proteins).
Data (including data from studies in knockout mice) suggest Lyve1 mediates adhesion of group A Streptococci (GAS) to lymphatic vesicular endothelium via capsular hyaluronan; this appears to be critical factor for lymphatic trafficking of GAS in vivo.
Data show that the expression of lymphatic vessel endothelial hyaluronan receptor 1 (LYVE 1) was similar with vascular endothelial growth factor C (VEGF-C (show VEGFC Proteins)), but its peak appeared 1-2 d later than that of VEGF-C (show VEGFC Proteins).
LMW-HA may play a critical role in the processes required for lymphangiogenesis through interactions with its receptor LYVE-1 and triggering intracellular signal cascades.
Studied the specific targeting property of lymphatic vessel endothelial hyaluronan receptor-1 binding polyethylene glycol-coated ultrasmall superparamagnetic iron oxide (LYVE-1-PEG (show PAEP Proteins)-USPIO) nanoparticles to mouse lymphatic endothelial cells.
Reelin (show RELN Proteins)-deficient mice showed abnormal collecting lymphatic vessels, characterized by a reduced number of SMCs, abnormal expression of lymphatic capillary marker lymphatic vessel endothelial hyaluronan receptor 1 (LYVE-1), and impaired function
CRSBP-1 plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence.
This gene encodes a type I integral membrane glycoprotein. The encoded protein acts as a receptor and binds to both soluble and immobilized hyaluronan. This protein may function in lymphatic hyaluronan transport and have a role in tumor metastasis.
lymphatic vessel endothelial hyaluronan receptor 1
, extracellular link domain containing 1
, lymphatic endothelial hyaluronan receptor LYVE-1
, lymphatic vessel endothelial hyaluronic acid receptor 1
, cell surface retention sequence binding protein-1
, cell surface retention sequence-binding protein 1
, extracellular link domain-containing 1
, extracellular link domain-containing protein 1
, hyaluronic acid receptor
, extra cellular link domain-containing 1
, lymphatic vessel endothelial HA receptor-1
, lymphatic vessel endothelial HA recptor-1