PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19451301-1 2009 Lactoferrin (LF) is an iron-binding antimicrobial protein present in saliva and gingival crevicular fluids, and it is possibly associated with host defense against oral pathogens, including periodontopathic bacteria. Iron 23-27 HLF transcription factor, PAR bZIP family member Homo sapiens 13-15 22274938-4 2013 Interestingly, hLF transgenic tobacco showed higher level of transcript expression for genes related to iron content regulation like iron transporter and metal transporter. Iron 104-108 HLF transcription factor, PAR bZIP family member Homo sapiens 15-18 22789477-1 2012 Human Lactoferrin (hLF) is an iron-binding protein with multiple physiological functions. Iron 30-34 HLF transcription factor, PAR bZIP family member Homo sapiens 19-22 25433245-6 2015 hLF-hinge-CH2-CH3 was significantly expressed in CHO cells (~100mg/l culture), was readily purified, and exhibited 98.3% of the non-fused rhLF iron-binding activity. Iron 143-147 HLF transcription factor, PAR bZIP family member Homo sapiens 0-3 22274938-1 2013 This study was aimed at to check the influence of human lactoferrin (hLF) expression on iron homeostasis, flavonoids, and antioxidants in transgenic tobacco. Iron 88-92 HLF transcription factor, PAR bZIP family member Homo sapiens 69-72 22806010-4 2012 Lf is an iron binding protein produced in mammals that has antimicrobial and immunomodulatory properties. Iron 9-13 HLF transcription factor, PAR bZIP family member Homo sapiens 0-2 22806010-6 2012 We found that H. pylori was able to use iron from fully iron-saturated human Lf (hLf) whereas partially iron-saturated hLf (apo) did not increase H. pylori growth. Iron 40-44 HLF transcription factor, PAR bZIP family member Homo sapiens 77-79 22806010-6 2012 We found that H. pylori was able to use iron from fully iron-saturated human Lf (hLf) whereas partially iron-saturated hLf (apo) did not increase H. pylori growth. Iron 40-44 HLF transcription factor, PAR bZIP family member Homo sapiens 81-84 22806010-6 2012 We found that H. pylori was able to use iron from fully iron-saturated human Lf (hLf) whereas partially iron-saturated hLf (apo) did not increase H. pylori growth. Iron 56-60 HLF transcription factor, PAR bZIP family member Homo sapiens 77-79 22806010-6 2012 We found that H. pylori was able to use iron from fully iron-saturated human Lf (hLf) whereas partially iron-saturated hLf (apo) did not increase H. pylori growth. Iron 56-60 HLF transcription factor, PAR bZIP family member Homo sapiens 77-79 19451301-5 2009 These results demonstrate the antibiofilm activity of LF with lower iron dependency against P. gingivalis and P. intermedia and the potential usefulness of LF for the prevention and treatment of periodontal diseases and as adjunct therapy for periodontal diseases. Iron 68-72 HLF transcription factor, PAR bZIP family member Homo sapiens 54-56 15192265-1 2004 BACKGROUND: Lactoferrin, LF, a multifunctional iron- and heparin-binding protein, present in exocrine body secretions and leukocytes, is remarkably resistant to proteolysis. Iron 47-51 HLF transcription factor, PAR bZIP family member Homo sapiens 25-27 19502737-2 2009 The hydrolysates of rhLF and hLF were found to be more active than native proteins against E. coli O157:H7, and their activity was independent of their iron saturation. Iron 152-156 HLF transcription factor, PAR bZIP family member Homo sapiens 21-24 18941633-8 2008 Biochemical analysis revealed that the iron-binding and releasing properties of rhLF were identical to that of native hLF. Iron 39-43 HLF transcription factor, PAR bZIP family member Homo sapiens 81-84 16707273-0 2006 Functional role of DMT1 in transferrin-independent iron uptake by human hepatocyte and hepatocellular carcinoma cell, HLF. Iron 51-55 HLF transcription factor, PAR bZIP family member Homo sapiens 118-121 16707273-5 2006 In addition, iron-depleted HLF increased membrane expression of DMT1, suggesting that the intracellular iron concentration regulated the DMT1 expression in hepatocytes via the iron regulatory protein (IRP)/IRE system. Iron 13-17 HLF transcription factor, PAR bZIP family member Homo sapiens 27-30 16707273-5 2006 In addition, iron-depleted HLF increased membrane expression of DMT1, suggesting that the intracellular iron concentration regulated the DMT1 expression in hepatocytes via the iron regulatory protein (IRP)/IRE system. Iron 104-108 HLF transcription factor, PAR bZIP family member Homo sapiens 27-30 18355020-2 2008 The dissociation constant for the apo form was (Kd)=2.2 x 10(-7) M; however, the specific binding of the iron-saturated rhLF and of lactoferrin from human milk (hLF) was too low to calculate the binding parameters. Iron 105-109 HLF transcription factor, PAR bZIP family member Homo sapiens 121-124 18355020-5 2008 Nevertheless, the amount of iron-saturated hLF transported across Caco-2 monolayers was significantly higher than that of rhLF. Iron 28-32 HLF transcription factor, PAR bZIP family member Homo sapiens 43-46 17211147-8 2007 Our study indicates that apo-hLf alleviates H2O2-induced oxidative damage in intestinal cells due to the iron-chelating capacity. Iron 105-109 HLF transcription factor, PAR bZIP family member Homo sapiens 29-32 15192265-2 2004 Ingested bovine iron-unsaturated LF, apo-bLF, suppresses VEGF-A-mediated angiogenesis in a previously described rat mesentery angiogenesis assay, possibly explaining, at least in part, its established anticancer effect in rats and mice. Iron 16-20 HLF transcription factor, PAR bZIP family member Homo sapiens 33-35 12165435-6 2002 The dissociation constant of the distinct mAbs for hLF ranged from 0.5 to 18 nM, without differences in affinity for unsaturated or iron-saturated hLF, indicating that the conformational changes subject to incorporation of iron do not seem to affect the exposure and/or conformation of the antibody epitopes. Iron 223-227 HLF transcription factor, PAR bZIP family member Homo sapiens 51-54 15222471-1 2004 One component of the anti-microbial function of lactoferrin (Lf) is its ability to sequester iron from potential pathogens. Iron 93-97 HLF transcription factor, PAR bZIP family member Homo sapiens 61-63 15222471-3 2004 This mechanism involves surface receptors capable of specifically binding Lf from the host, removing iron and transporting it across the outer membrane. Iron 101-105 HLF transcription factor, PAR bZIP family member Homo sapiens 74-76 15222471-8 2004 We propose that the receptor proteins, LbpA and LbpB, induce conformational changes in human Lf (hLf) that lower its affinity for iron that binding by FbpA can drive the transport across the outer membrane, a mechanism shared with transferrin (Tf) receptors. Iron 130-134 HLF transcription factor, PAR bZIP family member Homo sapiens 93-95 15222471-8 2004 We propose that the receptor proteins, LbpA and LbpB, induce conformational changes in human Lf (hLf) that lower its affinity for iron that binding by FbpA can drive the transport across the outer membrane, a mechanism shared with transferrin (Tf) receptors. Iron 130-134 HLF transcription factor, PAR bZIP family member Homo sapiens 97-100 11583400-6 2001 This study hints that hLf might participate in recovery from AT in several ways, e.g. by binding to the S. pyogenes pathogens, in addition to its well-known virtue of iron-binding capacity. Iron 167-171 HLF transcription factor, PAR bZIP family member Homo sapiens 22-25 12076509-1 2002 Both dimethylarsinic acid (DMA(V)) and dimethylarsinous acid (DMA(III)) release iron from human liver ferritin (HLF) with or without the presence of ascorbic acid. Iron 80-84 HLF transcription factor, PAR bZIP family member Homo sapiens 112-115 12076509-2 2002 With ascorbic acid the rate of iron release from HLF by DMA(V) was intermediate (3.37 nM/min, P<0.05) and by DMA(III) was much higher (16.3 nM/min, P<0.001). Iron 31-35 HLF transcription factor, PAR bZIP family member Homo sapiens 49-52 11981562-4 2002 Natural hLF from human milk and rhLF had identical iron-binding and -release properties. Iron 51-55 HLF transcription factor, PAR bZIP family member Homo sapiens 8-11 10085004-1 1999 Lactoferrin (Lf), an iron-sequestering glycoprotein, predominates in mucosal secretions, where the level of free extracellular iron (10(-18) M) is not sufficient for bacterial growth. Iron 21-25 HLF transcription factor, PAR bZIP family member Homo sapiens 13-15 10085004-3 1999 In this study we were able to show that Streptococcus pneumoniae specifically recognizes and binds the iron carrier protein human Lf (hLf). Iron 103-107 HLF transcription factor, PAR bZIP family member Homo sapiens 130-132 10085004-3 1999 In this study we were able to show that Streptococcus pneumoniae specifically recognizes and binds the iron carrier protein human Lf (hLf). Iron 103-107 HLF transcription factor, PAR bZIP family member Homo sapiens 134-137 10085004-8 1999 S. pneumoniae may use the hLf-PspA interaction to overcome the iron limitation at mucosal surfaces, and this might represent a potential virulence mechanism. Iron 63-67 HLF transcription factor, PAR bZIP family member Homo sapiens 26-29 9009306-3 1997 We had previously demonstrated that human lactoferrin (HLf) supported full growth of the bacteria in media lacking other iron sources. Iron 121-125 HLF transcription factor, PAR bZIP family member Homo sapiens 55-58 9079716-6 1997 SDS-polyacrylamide gel electrophoresis and absorbance measurements of purified transgenic hLF showed this protein was 90% saturated with iron, whereas natural hLF is only 3% saturated. Iron 137-141 HLF transcription factor, PAR bZIP family member Homo sapiens 90-93 9079716-7 1997 The pH-mediated release of iron from transgenic hLF was not different from that of iron-saturated natural hLF. Iron 27-31 HLF transcription factor, PAR bZIP family member Homo sapiens 48-51 9079716-8 1997 Unsaturated transgenic hLF could be completely resaturated upon addition of iron. Iron 76-80 HLF transcription factor, PAR bZIP family member Homo sapiens 23-26 9009306-4 1997 The ability of H. pylori to use HLf as an iron source had been found to be dependent on cell-to-protein contact. Iron 42-46 HLF transcription factor, PAR bZIP family member Homo sapiens 32-35 9009306-5 1997 Since lactoferrin has been found in significant amounts in human stomach resection specimens from patients with superficial or atrophic gastritis, the iron uptake of H. pylori via a specific HLf receptor may play a major role in the virulence of H. pylori infection. Iron 151-155 HLF transcription factor, PAR bZIP family member Homo sapiens 191-194 30575774-1 2018 Lactoferrin (LF) is an 80 KDa iron-binding glycoprotein that plays a significant role in the innate immune system and is considered to be an important microbicide molecule. Iron 30-34 HLF transcription factor, PAR bZIP family member Homo sapiens 13-15 7662812-6 1995 The iron-saturated forms of human (S-hLf), bovine (S-bLf) lactoferrins and human transferrin (S-hTf) enhanced cell proliferation, while iron-unsaturated forms (U-hLf, U-bLf, and U-hTf) suppressed it. Iron 4-8 HLF transcription factor, PAR bZIP family member Homo sapiens 37-40 7662812-6 1995 The iron-saturated forms of human (S-hLf), bovine (S-bLf) lactoferrins and human transferrin (S-hTf) enhanced cell proliferation, while iron-unsaturated forms (U-hLf, U-bLf, and U-hTf) suppressed it. Iron 4-8 HLF transcription factor, PAR bZIP family member Homo sapiens 162-165 8074229-1 1994 The role of human lactoferrin (hLf) in alimentary iron absorption across intestinal cells was explored using a human differentiated colon carcinoma cell line, HT-29cl.19A. Iron 50-54 HLF transcription factor, PAR bZIP family member Homo sapiens 31-34 1452033-6 1992 Furthermore, re-hLF is functional by the criterion of iron-binding capacity. Iron 54-58 HLF transcription factor, PAR bZIP family member Homo sapiens 16-19 34630348-2 2021 Moraxella catarrhalis resides exclusively on the mucosal surfaces of the upper respiratory tract of humans and is capable of directly acquiring iron for growth from the host glycoproteins human transferrin (hTf) and human lactoferrin (hLf). Iron 144-148 HLF transcription factor, PAR bZIP family member Homo sapiens 235-238 34630348-4 2021 The extraction of iron involves conformational changes in Lf and Tf to facilitate iron removal followed by its transport across the outer membrane by a well characterized process for TBDTs. Iron 18-22 HLF transcription factor, PAR bZIP family member Homo sapiens 58-60 34630348-4 2021 The extraction of iron involves conformational changes in Lf and Tf to facilitate iron removal followed by its transport across the outer membrane by a well characterized process for TBDTs. Iron 82-86 HLF transcription factor, PAR bZIP family member Homo sapiens 58-60 34630348-9 2021 We propose that the indirect effect on iron transport from Tf and Lf by CopB could possibly be explained by the association of TBDTs at gaps in the peptidoglycan layer that may enhance the efficiency of the process. Iron 39-43 HLF transcription factor, PAR bZIP family member Homo sapiens 66-68 8739601-4 1996 HLf and BLf exerted their activity through the inhibition of adsorption of virions to the cells independently of their iron withholding property showing similar activity in the apo- and iron-saturated form. Iron 119-123 HLF transcription factor, PAR bZIP family member Homo sapiens 0-3 8739601-4 1996 HLf and BLf exerted their activity through the inhibition of adsorption of virions to the cells independently of their iron withholding property showing similar activity in the apo- and iron-saturated form. Iron 186-190 HLF transcription factor, PAR bZIP family member Homo sapiens 0-3 8142485-7 1994 (C) The removal of iron leads to thermal destabilization of HST, HLF and RST. Iron 19-23 HLF transcription factor, PAR bZIP family member Homo sapiens 65-68 29516297-1 2018 Human and bovine lactoferrin (hLf and bLf) are multifunctional iron-binding glycoprotein constitutively synthesized and secreted by glandular epithelial cells and by neutrophils following induction. Iron 63-67 HLF transcription factor, PAR bZIP family member Homo sapiens 30-33 28878310-7 2017 A total of 400-450 g of rhLF protein, which shows similar enzymatic activity to natural hLF in iron binding and release, can be purified on a large scale from >100 L of milk per day. Iron 95-99 HLF transcription factor, PAR bZIP family member Homo sapiens 25-28 28079060-1 2017 Growing evidence suggests that lactoferrin (Lf), an iron-binding glycoprotein, is a pleiotropic functional nutrient. Iron 52-56 HLF transcription factor, PAR bZIP family member Homo sapiens 44-46 28914813-1 2017 Human lactoferrin (hLf), an iron-binding multifunctional cationic glycoprotein secreted by exocrine glands and by neutrophils, is a key element of host defenses. Iron 28-32 HLF transcription factor, PAR bZIP family member Homo sapiens 19-22 28914813-2 2017 HLf and bovine Lf (bLf), possessing high sequence homology and identical functions, inhibit bacterial growth and biofilm dependently from iron binding ability while, independently, bacterial adhesion to and the entry into cells. Iron 138-142 HLF transcription factor, PAR bZIP family member Homo sapiens 1-3 28763236-8 2017 Both hLF-hinge-CH2-CH3 and hLF-CH2-CH3 exhibited iron-binding activity, superior uptake by Caco-2 cells, similar thermal stability, and longer plasma half-life compared to recombinant hLF. Iron 49-53 HLF transcription factor, PAR bZIP family member Homo sapiens 5-8 27569531-2 2016 In the absence of PspA Streptococcus pneumoniae becomes more susceptible to killing by human apolactoferrin (apo-hLf), the iron-free form of lactoferrin. Iron 123-127 HLF transcription factor, PAR bZIP family member Homo sapiens 113-116 28169552-1 2017 Lactoferrin (Lf) is an iron-binding multifunctional protein, mainly present in external secretions. Iron 23-27 HLF transcription factor, PAR bZIP family member Homo sapiens 13-15 28663751-1 2017 Human lactoferrin (hLf), an 80-kDa multifunctional iron-binding cationic glycoprotein, is constitutively secreted by exocrine glands and by neutrophils during inflammation. Iron 51-55 HLF transcription factor, PAR bZIP family member Homo sapiens 19-22 28257520-5 2017 The formation of a 1:1 complex of iron-loaded Lf and LbpB involves an interaction between the Lf C-lobe and LbpB N-lobe, comparable to TbpB, consistent with a potential role in iron acquisition. Iron 34-38 HLF transcription factor, PAR bZIP family member Homo sapiens 46-48 28257520-5 2017 The formation of a 1:1 complex of iron-loaded Lf and LbpB involves an interaction between the Lf C-lobe and LbpB N-lobe, comparable to TbpB, consistent with a potential role in iron acquisition. Iron 34-38 HLF transcription factor, PAR bZIP family member Homo sapiens 94-96 28257520-5 2017 The formation of a 1:1 complex of iron-loaded Lf and LbpB involves an interaction between the Lf C-lobe and LbpB N-lobe, comparable to TbpB, consistent with a potential role in iron acquisition. Iron 177-181 HLF transcription factor, PAR bZIP family member Homo sapiens 46-48 28257520-7 2017 Our results are consistent with LbpB serving dual roles focused primarily on iron acquisition when exposed to limited levels of iron-loaded Lf on the mucosal surface and effectively binding apo Lf when exposed to high levels at sites of inflammation. Iron 128-132 HLF transcription factor, PAR bZIP family member Homo sapiens 140-142