Results 21 to 30 of about 6,390 (173)
Hemopexin Modulates Expression of Complement Regulatory Proteins in Rat Glomeruli
In systemic hemolysis and in hematuric forms of kidney injury, the major heme scavenging protein, hemopexin (HPX), becomes depleted, and the glomerular microvasculature (glomeruli) is exposed to high concentrations of unbound heme, which, in addition to ...
Maria G. Detsika, Elias A. Lianos
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Proinflammatory cytokines, including TNF-α and IL-6, can contribute to insulin resistance. Conversely, insulin has some actions that can be considered anti-inflammatory.
J. Lee Franklin +2 more
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Shiga-toxin (Stx)-producing Escherichia coli hemolytic-uremic syndrome (STEC-HUS) is one of the most common causes of acute kidney injury in children.
Kioa L. Wijnsma +10 more
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Pancreatic ductal adenocarcinoma is one of the most aggressive types of cancer. Certain proteins in the tumor microenvironment have attracted considerable attention owing to their association with tumor invasion and metastasis.
Yukie Suzuki +17 more
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TLR4 Signaling by Heme and the Role of Heme-Binding Blood Proteins
Toll-like receptors (TLRs), also known as pattern recognition receptors, respond to exogenous pathogens and to intrinsic danger signals released from damaged cells and tissues.
Sabina Janciauskiene +2 more
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Development of high throughput robust methods is a prerequisite for a successful clinical use of LC-MS/MS assays. In earlier studies, we reported that nLC-MS/MS measurement of the O-glycoforms of HPX is an indicator of liver fibrosis.
Aswini Panigrahi +5 more
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Heme‐hemopexin: A ‘Chronosteric’ heme‐protein [PDF]
AbstractHemopexin (HPX) serves as scavenger and transporter of toxic plasma heme to the liver. HPX is formed by two four‐bladed β‐propeller domains, resembling two thick disks that lock together at a 90° angle. The heme is bound between the two β‐propeller domains in a pocket formed by the interdomain linker peptide.
ASCENZI P, FASANO, MAURO
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Iron is an essential micronutrient for most living species. In mammals, hemoglobin (Hb) stores more than two thirds of the body's iron content. In the bloodstream, haptoglobin (Hp) and hemopexin (Hpx) sequester free Hb or heme.
Alessandra Mozzi +5 more
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Plasmin cleaves rabbit serum apohemopexin (Mr = 60,000) at a single site producing a heme-binding domain (I, Mr = 35,000) and a second domain (II, Mr = 25,000) (W. T. Morgan and A. Smith (1984) J. Biol. Chem. 259, 12001-12005). The absorbance spectra of heme-domain I are indicative of a bis-histidyl coordination complex with the central heme iron atom.
W T, Morgan +6 more
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Intravascular erythrocyte destruction, accompanied by the release of pro-oxidative and pro-inflammatory components hemoglobin and heme, is a common event in the pathogenesis of numerous diseases with heterogeneous etiology and clinical features.
Nicolas S. Merle +47 more
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