Disease relevance of Ambp

• These results indicate that endogenous UTI is protective against acute lung injury induced by bacterial endotoxin, at least partly, via the antioxidative properties [1].
• Our results show that the UTI receptors of some tumor cells have a possible role in modulating plasmin activity on the cell surface and prevention of tumor cell invasion and metastasis (H. Kobayashi et al., J. Biol. Chem., 269; 20642-20647, 1994) [2].
• UTI can bind easily to its receptors on various types of tumor cells (human ovarian cancer HOC-I cells, human choriocarcinoma SMT-cc1 cells, and murine Lewis lung carcinoma 3LL cells) [2].
• The adherence of uropathogenic Escherichia coli to the urothelial surface, a critical first step in the pathogenesis of urinary tract infection (UTI), is controlled by three key elements: E. coli adhesins, host receptors, and host defense mechanisms [3].
• A novel murine model of UTI reinfection was developed using the prototypic cystitis UPEC isolate NU14 harboring a plasmid encoding OVA as a unique antigenic marker [4].

Psychiatry related information on Ambp

• We have found previously that the lack of a positive correlation between urinary levels of alpha 1M and UT distinguishes Parkinson's disease from other neuropsychiatric diseases such as dementia (Alzheimer-type and vascular dementia), schizophrenia and mood disorders [5].

High impact information on Ambp

• This study examined the change in susceptibility to urinary tract infection (UTI) after deletion of the murine interleukin 8 receptor homologue (mIL-8Rh) [6].
• The experimental UTI model demonstrated that IL-8R-dependent mechanisms control the urinary tract defense, and that neutrophils are essential host effector cells [6].
• UTI derivatized with biotin or FITC was taken up by tumor cells in a dose-dependent manner [2].
• This cell association was inhibited with a monoclonal antibody D1, which specifically recognizes NH2 terminus (domain I) of UTI [2].
• The present study was undertaken to determine whether highly purified human urinary trypsin inhibitor (UTI) efficiently inhibits the soluble and the tumor cell receptor-bound plasmin [7].

Chemical compound and disease context of Ambp

• Antioxidative role of urinary trypsin inhibitor in acute lung injury induced by lipopolysaccharide [1].
• A highly purified urinary trypsin inhibitor (UTI) inhibits not only tumor cell invasion in an in vitro assay but also production of experimental and spontaneous lung metastasis in an in vivo mouse model [8].
• We designed a study using an experimental model of UTI in which surgically menopausal mice were supplemented with estrogen and the susceptibility to UTI was evaluated after experimental Escherichia coli infection [9].
• The antimicrobial activity of the intraurethrally administered probiotic Lactobacillus casei strain Shirota against Escherichia coli in a murine urinary tract infection (UTI) model was examined [10].
• Proteus mirabilis, a common cause of urinary tract infections (UTI) in individuals with functional or structural abnormalities or with long-term catheterization, forms bladder and kidney stones as a consequence of urease-mediated urea hydrolysis [11].

Biological context of Ambp

• Linkage mapping of the Aldo-2, Pax-5, Ambp, and D4h9S3E loci on mouse chromosome 4 in the region of homology with human chromosome 9 [12].
• Expression of early growth response factor-1 (Egr-1) and phosphorylation of extracellular signal-regulated protein kinases 1/2 in monocytes stimulated with LPS were inhibited by UTI [13].
• These results demonstrate that UTI plays an important role in the formation of the stable cumulus-oocyte complex that is essential for oocyte maturation and ovulation [14].
• An Msp I restriction fragment length polymorphism (RFLP) in the mouse L gene (proposed symbol, Intin-4) links this gene to other genes already mapped at mouse Chr 4 near the brown (b) locus, a homologous region to the human chr 9q32-34 band where the human I alpha I L gene is located [15].
• In the present study, we addressed whether UTI regulates oxidative stress generated by LPS challenge in the lung [1].

Anatomical context of Ambp

• After LPS (1 mg/kg) challenge, UTI (-/-) mice revealed a significant elevation of plasma fibrinogen and fibrinogen/fibrin degradation products and a decrease in white blood cell counts compared with WT mice [16].
• The protein levels of proinflammatory mediators, such as macrophage chemoattractant protein (MCP)-1 in the lungs, MCP-1 and keratinocyte chemoattractant (KC) in the kidneys, and interleukin-1beta, macrophage inflammatory protein-2, MCP-1, and KC in the liver, were significantly greater in UTI (-/-) mice than in WT mice after LPS challenge [16].
• TNF-alpha production by monocytes stimulated with LPS (100 ng/ml) was inhibited by UTI at concentrations higher than 100 U/ml [13].
• The number of naturally ovulated oocytes from UTI-deficient mice was greatly reduced compared with that from wild-type mice [14].
• Using a modified Boyden chamber and an artificial basement membrane, Matrigel, it was found that UTI, but not alpha 2AP or alpha 2M, can inhibit HOC-I and SMT-ccl cells invasion in vitro [7].

Associations of Ambp with chemical compounds

• Urinary trypsin inhibitor protects against systemic inflammation induced by lipopolysaccharide [16].
• Although urinary trypsin inhibitor (UTI) has been shown to inhibit tumor necrosis factor (TNF)-alpha- production, the detailed mechanism(s) remains unclear [13].
• Urinary trypsin inhibitor (UTI) is a serine proteinase inhibitor that is found in blood and urine [14].
• Immunohistochemistry showed that the formations of 8-hydroxy-2'-deoxyguanosine and nitrotyrosine in the lung were more intense in UTI (-/-) mice than in WT mice after LPS challenge [1].
• All assignable residues of ECGF-2b were identical with urinary glycoprotein proteinase inhibitor (HI-30/EDC1) [17].

Regulatory relationships of Ambp

• Impairment of the correlation between urinary contents of alpha-1-microglobulin and ulinastatin is induced by intracerebroventricularly administered interleukin-6 in mice [18].
• OBJECTIVE: To investigate the precise mechanism by which urinary trypsin inhibitor suppresses cytokine production in the prevention of preterm delivery [19].
• As urinary trypsin inhibitor suppressed the lipopolysaccharide-induced uterine contractions, this inhibitor may be a hopeful candidate of a drug for prevention of preterm delivery [20].

Other interactions of Ambp

• In the interspecific backcross, wi was found to be non-recombinant with Orm1, 0.12 cM distal of D4Mit87 and Ambp, and 0.12 cM proximal of CD301 [21].
• The mouse genes for Pax-5 and Ambp previously have been shown to map to MMU4 [12].
• OBJECTIVE: To investigate the mechanisms whereby urinary trypsin inhibitor prevents lipopolysaccharide-induced preterm delivery in mice [22].
• At 3, 6, 9, and 18 hours after the second dose of lipopolysaccharide, and at delivery in the control and urinary trypsin inhibitor-treated groups, the concentrations, of interleukin-1 alpha and tumor necrosis factor-alpha were determined in serum and amniotic fluid [23].
• Urinary trypsin inhibitor (UTI; Mr 40 kDa) is a Kunitz-type protease inhibitor that efficiently inhibits cell-associated trypsin and plasmin activities [24].

Analytical, diagnostic and therapeutic context of Ambp

• To investigate the physiological functions of UTI in vivo, we generated UTI-deficient mice by gene targeting [14].
• Cell-binding experiments employing cell enzyme-linked immunosorbent assay and flow cytometry indicated that tumor cells (SMT-cc1 and 3LL cells) have specific binding sites for UTI on their cell surface [8].
• Purification of the two UTI receptor proteins by ligand affinity chromatography (ligand-blotting analysis) yielded two bands when analyzed by SDS-polyacrylamide gel electrophoresis, corresponding in electrophoretic mobility to those calculated by cross-linking analysis [8].
• Despite the association of numerous bacterial factors with uropathogenic E. coli (UPEC), few such factors have been proved to be required for UTI in animal models [25].
• Proteus mirabilis is a common cause of urinary tract infection (UTI) in individuals with structural abnormalities or long-term catheterization [26].

References