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Journal articles on the topic 'Secretory leukocyte proteinase inhibitor (SLPI)'

Author: Grafiati

Published: 24 April 2022

Last updated: 30 July 2025

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1

van Wetering, Sandra, Abraham C. van der Linden, Marianne A. J. A. van Sterkenburg, et al. "Regulation of SLPI and elafin release from bronchial epithelial cells by neutrophil defensins." American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 1 (2000): L51—L58. http://dx.doi.org/10.1152/ajplung.2000.278.1.l51.

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Secretory leukocyte proteinase inhibitor (SLPI) is a serine proteinase inhibitor that is produced locally in the lung by cells of the submucosal bronchial glands and by nonciliated epithelial cells. Its main function appears to be the inhibition of neutrophil elastase (NE). Recently, NE was found to enhance SLPI mRNA levels while decreasing SLPI protein release in airway epithelial cells. Furthermore, glucocorticoids were shown to increase both constitutive and NE-induced SLPI mRNA levels. In addition to NE, stimulated neutrophils also release α-defensins. Defensins are small, antimicrobial po

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2

Chuluyan, Eduardo, Nella Ambrosi, Nicolas Fraunhoffer, et al. "Secretory leukocyte proteinase inhibitor: A key player in the dialogue between the tumor and its microenvironment in pancreatic cancer patients." Journal of Clinical Oncology 40, no. 4_suppl (2022): 592. http://dx.doi.org/10.1200/jco.2022.40.4_suppl.592.

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592 Background: Secretory leukocyte proteinase inhibitor (SLPI) is a non-glycosylated pleiotropic protein with anti-protease, microbicidal, healing, anti-inflammatory and immunomodulatory activity. Previous studies have shown that SLPI is associated with pancreatic tumor progression by promoting cancer cell survival and proliferation. However, SLPI can also act on the tumor microenvironment to affect the local immune response. In the present work we evaluate the role of SLPI in patients with pancreatic cancer and its activity as a tumor escape factor from the immune response. Methods: Serum le

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3

Jiménez-Vega, Florinda, and Francisco Vargas-Albores. "A secretory leukocyte proteinase inhibitor (SLPI)-like protein from Litopenaeus vannamei haemocytes." Fish & Shellfish Immunology 23, no. 5 (2007): 1119–26. http://dx.doi.org/10.1016/j.fsi.2007.06.006.

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4

Fernie-King, Barbara A., David J. Seilly, Alexandra Davies, and Peter J. Lachmann. "Streptococcal Inhibitor of Complement Inhibits Two Additional Components of the Mucosal Innate Immune System: Secretory Leukocyte Proteinase Inhibitor and Lysozyme." Infection and Immunity 70, no. 9 (2002): 4908–16. http://dx.doi.org/10.1128/iai.70.9.4908-4916.2002.

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ABSTRACT Streptococcal inhibitor of complement (SIC) is a 31-kDa extracellular protein of a few, very virulent, strains of Streptococcus pyogenes (particularly M1 strains). It is secreted in large quantities (about 5 mg/liter) and inhibits complement lysis by blocking the membrane insertion site on C5b67. We describe investigations into the interaction of SIC with three further major components of the innate immune system found in airway surface liquid, namely, secretory leukocyte proteinase inhibitor (SLPI), lysozyme, and lactoferrin. Enzyme-linked immunosorbent assays showed that SIC binds t

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NANDEDKAR, S. "The effect of secretory leukocyte proteinase inhibitor (SLPI) in a murine model of asthma*1." Journal of Allergy and Clinical Immunology 113, no. 2 (2004): S220. http://dx.doi.org/10.1016/j.jaci.2004.01.244.

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6

Moreau, Thierry, Kévin Baranger, Sébastien Dadé, Sandrine Dallet-Choisy, Nicolas Guyot, and Marie-Louise Zani. "Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family." Biochimie 90, no. 2 (2008): 284–95. http://dx.doi.org/10.1016/j.biochi.2007.09.007.

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7

Xie, WenTing, Han Zhang, ShanShan Qin, et al. "The expression and clinical significance of secretory leukocyte proteinase inhibitor (SLPI) in mammary carcinoma using bioinformatics analysis." Gene 720 (December 2019): 144088. http://dx.doi.org/10.1016/j.gene.2019.144088.

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8

Skott, P., E. Lucht, M. Ehnlund, and E. Björling. "Inhibitory function of secretory leukocyte proteinase inhibitor (SLPI) in human saliva is HIV-1 specific and varies with virus tropism." Oral Diseases 8, no. 3 (2002): 160–67. http://dx.doi.org/10.1034/j.1601-0825.2002.01807.x.

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9

Sakunwattana, Taksaorn, Phattarunda Jaree, Vichien Rimphanitchayakit, Anchalee Tassanakajon, and Sirinit Tharntada. "Antibacterial and antiproteinase activities of a double whey acidic protein domain-containing protein from Penaeus vannamei Boone, 1931 (Decapoda, Penaeidae)." Crustaceana 93, no. 1 (2020): 51–69. http://dx.doi.org/10.1163/15685403-00003962.

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Abstract Double whey acidic protein domain-containing proteins (DWDs) or secretory leukocyte protease inhibitor (SLPI)-like proteins, have been identified in many species of Crustacea. The PvDWD1 from Penaeus vannamei was the first SLPI-like protein identified in a crustacean. Herein, we report that the expression of PvDWD1 was up-regulated at 6 h after acute hepatopancreatic necrosis disease (AHPND)-causing Vibrio parahaemolyticus (VPAHPND) challenge. Similarly, after a different stress other than bacterial infection, the chronic non-lethal heat shock (NLHS) induction, the expression of the P

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10

Sallenave, J. M., J. Shulmann, J. Crossley, M. Jordana, and J. Gauldie. "Regulation of secretory leukocyte proteinase inhibitor (SLPI) and elastase-specific inhibitor (ESI/elafin) in human airway epithelial cells by cytokines and neutrophilic enzymes." American Journal of Respiratory Cell and Molecular Biology 11, no. 6 (1994): 733–41. http://dx.doi.org/10.1165/ajrcmb.11.6.7946401.

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11

Ochi, Akinobu, Dong Chen, Wibke Schulte, et al. "MIF-2/D-DT enhances proximal tubular cell regeneration through SLPI- and ATF4-dependent mechanisms." American Journal of Physiology-Renal Physiology 313, no. 3 (2017): F767—F780. http://dx.doi.org/10.1152/ajprenal.00683.2016.

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Macrophage migration inhibitory factor (MIF) is a cytokine with pleiotropic actions that is produced by several organs and cell types. Depending on the target cell and the inflammatory context, MIF can engage its two component receptor complex CD74 and CD44 and the chemokine receptors CXCR2/4. MIF is constitutively expressed in renal proximal tubular cells, stored in intracellular preformed pools, and released at a low rate. Recently, a second MIF-like protein (i.e., MIF-2/D-DT) has been characterized in mammals. Our study was aimed at examining the role of MIF-2/D-DT, which mediates tissue pr

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12

Zhang, Dongjie, Qian Zhang, Xiaoxu Wu, et al. "Integrative Analysis of Chromatin Accessibility and Transcriptional Landscape Identifies Key Genes During Muscle Development in Pigs." Cells 13, no. 24 (2024): 2118. https://doi.org/10.3390/cells13242118.

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Many efforts have been made to reveal the mechanisms underlying skeletal muscle development because of its importance in animals. However, knowledge on chromatin accessibility, a prerequisite for gene expression, remains limited. Here, dynamic changes in chromatin accessibility were analyzed in the skeletal muscles of Min pigs at the ages of 30, 90, and 210 d using an assay for transposase-accessible chromatin with high-throughput sequencing (ATAC-seq). A total of 16,301 differentially accessible regions (DARs) associated with 7455 genes were identified among three developmental stages. Seven

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Shalko, M. N., and K. V. Sereda. "Effectiveness of vaccination in the treatment of early lesions of the cervix in women with infertility." UKRAINIAN JOURNAL HEALTH OF WOMAN, no. 2(171) (March 30, 2024): 51–56. http://dx.doi.org/10.15574/hw.2024.171.51.

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Infertility is a common pathology that has not only medical, but powerful social and economic consequences. The aim of the study - to investigate the impact of human papillomavirus (HPV) vaccination on indicators of local cervical immunity in women with infertility. Materials and methods. 133 patients with infertility were examined, in whom abnormal cytological findings and DNA of one or more HPV strains were detected during the initial examination. Among them, 28 women had infertility of endocrine origin (the Group I), 52 women had tubo-peritoneal origin (the Group II) and 53 patients had mal

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14

Hannila, Sari S. "Secretory Leukocyte Protease Inhibitor (SLPI)." Neuroscientist 21, no. 6 (2014): 630–36. http://dx.doi.org/10.1177/1073858414546000.

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15

Ohlsson, Sophie, Irena Ljungkrantz, Kjell Ohlsson, Mårten Segelmark, and Jörgen Wieslander. "Novel distribution of the secretory leucocyte proteinase inhibitor in kidney." Mediators of Inflammation 10, no. 6 (2001): 347–50. http://dx.doi.org/10.1080/09629350120102389.

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The secretory leucocyte proteinase inhibitor (SLPI) is a low molecular weight, tissue-specific inhibitor of, for example, elastase and cathepsin G, which also have antimicrobial capacity. SLPI has been localised to the respiratory, gastrointestinal and genital tracts, but so far not to the kidney. The presence of SLPI in renal tubuli cells was demonstrated using immunohistochemistry and, by means ofin situhybridisation on human renal biopsies, we were able to demonstrate SLPI production. In various inflammatory conditions in the kidneys, the protease-antiprotease balance is disturbed. For this

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Mihaila, Alina, and Guy M. Tremblay. "Human Alveolar Macrophages Express Elafin and Secretory Leukocyte Protease Inhibitor." Zeitschrift für Naturforschung C 56, no. 3-4 (2001): 291–97. http://dx.doi.org/10.1515/znc-2001-3-420.

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Abstract Elafin and secretory leukocyte protease inhibitor (SLPI) are two structurally related serine protease inhibitors present in the lung. The cellular origin of elafin in the alveolar space is unknown. It has been suggested that at least one alveolar leukocyte population express elafin. We therefore postulated that the alveolar macrophage, as the most numerous leukocyte in the alveolar space, express elafin. On the other hand, it is unclear whether human alveolar macrophages are a source of SLPI. In the present study, we showed by RT-PCR that human alveolar macrophages, but not peripheral

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Zhong, Qiao-Qing, Xiang Wang, Yun-Feng Li, Li-Jun Peng, and Zhi-Sheng Jiang. "Secretory leukocyte protease inhibitor promising protective roles in obesity-associated atherosclerosis." Experimental Biology and Medicine 242, no. 3 (2016): 250–57. http://dx.doi.org/10.1177/1535370216672747.

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Secretory leukocyte protease inhibitor (SLPI), a serine protease inhibitor, which was most commonly examined in mucosal fluids such as saliva, is a versatile molecule and plays non-redundant roles. In addition to its anti-protease activity, SLPI has been shown to express anti-bacterial, anti-viral, anti-fungal, and anti-inflammatory properties as well as participating in innate and adaptive immune responses, most of which has been well documented. Recently, it is reported that SLPI is expressed in adipocytes and adipose tissue where it could play an important feedback role in the resolution of

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18

Ding, Aihao, Nathalie Thieblemont, Jing Zhu, Fenyu Jin, Jenny Zhang, and Samuel Wright. "Secretory Leukocyte Protease Inhibitor Interferes with Uptake of Lipopolysaccharide by Macrophages." Infection and Immunity 67, no. 9 (1999): 4485–89. http://dx.doi.org/10.1128/iai.67.9.4485-4489.1999.

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ABSTRACT Macrophages are among the most sensitive targets of bacterial endotoxin (LPS), responding to minute amounts of LPS by releasing a battery of inflammatory mediators. Transfection of macrophages with secretory leukocyte protease inhibitor (SLPI) renders these cells refractory to LPS stimulation. Here we show that uptake of LPS from soluble CD14 (sCD14)-LPS complexes by SLPI-overexpressing cells was only 50% of that seen in control cells. SLPI transfectants and mock transfectants did not differ in the surface expression of CD14 or CD18. We show, in addition, that recombinant human SLPI c

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Nyström, Max, Ulla Peterson Westin, Carina Linder, and Kjell Ohlsson. "Secretory leukocyte protease inhibitor in punch biopsies from human colonic mucosa." Mediators of Inflammation 10, no. 5 (2001): 269–72. http://dx.doi.org/10.1080/09629350120093740.

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Secretory leukocyte protease inhibitor (SLPI) is a wellknown protease inhibitor. Its function is thought to be protease/protease-inhibitor balance. Free proteolytic activity, mainly pancreatic elastase, anionic trypsin and granulocytic elastase, has been demonstrated in faecal extracts from patients with ulcerative colitis. We wanted to verify that SLPI is actually secreted from normal human colonic mucosa. Also, we wanted to ascertain whether studies of SLPI secretion based on punch biopsies were dependent on biopsy area or on biopsy circumference. Normal colonic mucosa was sampled during sur

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Abbinante-Nissen, J. M., L. G. Simpson, and G. D. Leikauf. "Corticosteroids increase secretory leukocyte protease inhibitor transcript levels in airway epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 268, no. 4 (1995): L601—L606. http://dx.doi.org/10.1152/ajplung.1995.268.4.l601.

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Secretory leukocyte protease inhibitor (SLPI) is the predominant antiprotease of the conducting airways and may play a role in reducing airway inflammation. In this study, the effect of corticosteroids used in the treatment of inflammatory airway disease on SLPI transcript levels was investigated. When human airway epithelial cells (9HTEo-) were treated continuously with 10 nM fluticasone propionate, SLPI transcript levels increased within 12 h, with maximal transcript accumulation occurring at 24–48 h. Several corticosteroids (0.1-1,000 nM) were compared, and the following potency in increasi

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21

Saitoh, Hiroki, Tohru Masuda, Sanae Shimura, Toshiaki Fushimi, and Kunio Shirato. "Secretion and gene expression of secretory leukocyte protease inhibitor by human airway submucosal glands." American Journal of Physiology-Lung Cellular and Molecular Physiology 280, no. 1 (2001): L79—L87. http://dx.doi.org/10.1152/ajplung.2001.280.1.l79.

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Submucosal glands were isolated within 4 h of death from tracheae and bronchi obtained from autopsied lungs, and the secretory response of secretory leukocyte protease inhibitor (SLPI) was examined with ELISA and a secretory index. Although human neutrophil elastase (HNE) at low concentrations increased SLPI secretion above the control level (i.e., 149% of control level at 10−11 M), HNE at high concentrations significantly decreased it below the control level (i.e., 16% of control level at 10−7 M). The decrease in SLPI concentration was shown to result from the degradation of SLPI by excessive

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22

Lai, Jengyu, Jeffrey R. Basford, and Mark R. Pittelkow. "Levels of secretory leukocyte protease inhibitor expression in acute wounds." Journal of Wound Care 31, Sup7 (2022): S15—S19. http://dx.doi.org/10.12968/jowc.2022.31.sup7.s15.

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Objective: Even with our best practices, we are frequently unable to prevent slow and stalled wound healing—particularly in people with impaired circulation and conditions such as diabetes. As a result, greater insight into the nature of wound healing and alternative treatment approaches is needed. An avenue that may be of particular promise is increasing understanding of the role of secretory leukocyte protease inhibitor (SLPI) as there is evidence that it enhances wound healing, its expression increases in response to inflammation and infection, and it exhibits anti-protease, anti-inflammato

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Reviglio, Victor E., Ruben H. Sambuelli, Alejandra Olmedo, et al. "Secretory Leukocyte Protease Inhibitor Is an Inducible Antimicrobial Peptide Expressed inStaphylococcus aureusEndophthalmitis." Mediators of Inflammation 2007 (2007): 1–6. http://dx.doi.org/10.1155/2007/93857.

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Purpose. To describe the presence of secretory leukocyte protease inhibitor (SLPI), a cationic peptide with antimicrobial and antiprotease activity, in the innate ocular immune reaction in a rat model ofStaphylococcus aureusendophthalmitis.Methods. Seventy-five female Lewis rats were divided into three groups: the endophthalmitis group received an intravitreal injection of 65 colony-forming units of viableS. aureus, the vehicle-injected group received balanced sterile saline solution (BSS), and the control group was not injected. Eyes were enucleated at 24 and 48 hours and processed for immuno

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Jin, Fenyu, Carl F. Nathan, Danuta Radzioch, and Aihao Ding. "Lipopolysaccharide-Related Stimuli Induce Expression of the Secretory Leukocyte Protease Inhibitor, a Macrophage-Derived Lipopolysaccharide Inhibitor." Infection and Immunity 66, no. 6 (1998): 2447–52. http://dx.doi.org/10.1128/iai.66.6.2447-2452.1998.

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ABSTRACT Mouse secretory leukocyte protease inhibitor (SLPI) was recently characterized as a lipopolysaccharide (LPS)-induced product of macrophages that antagonizes their LPS-induced activation of NF-κB and production of NO and tumor necrosis factor (TNF) (F. Y. Jin, C. Nathan, D. Radzioch, and A. Ding, Cell 88:417–426, 1997). To better understand the role of SLPI in innate immune and inflammatory responses, we examined the kinetics of SLPI expression in response to LPS, LPS-induced cytokines, and LPS-mimetic compounds. SLPI mRNA was detectable in macrophages by Northern blot analysis within

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Dickey, Brittney L., Bradley Sirak, Laura Martin-Gomez, et al. "Oral secretory leukocyte protease inhibitor (SLPI): Associations with oropharyngeal cancer and treatment outcome." PLOS ONE 16, no. 7 (2021): e0254161. http://dx.doi.org/10.1371/journal.pone.0254161.

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Background Rates of oropharyngeal cancer (OPC) associated with alcohol & tobacco use have decreased, while human papillomavirus (HPV) associated OPC has increased among men in the US. Secretory leukocyte protease inhibitor (SLPI), detectable in a variety of secretions, has been implicated in cancers of the head and neck, associated with tumor progression and anti-viral activity. Using the recently verified oral gargle specimen, this study aimed to assess the association of salivary SLPI expression with risk of OPC and response to treatment. Methods A case-control study design compared leve

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Klimenkova, Olga, Wienke Ellerbeck, Ana Gigina, Karl Welte, and Julia Skokowa. "A Lack of Secretory Leukocyte Protease Inhibitor (SLPI) Causes Defects in Myeloid Differentiation." Blood 120, no. 21 (2012): 10. http://dx.doi.org/10.1182/blood.v120.21.10.10.

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Abstract Abstract 10 Previously, we demonstrated severe diminished mRNA and protein levels of secretory leukocyte protease inhibitor (SLPI) in CD33+ myeloid cells in PMNs and in plasma of patients with severe congenital neutropenia (CN), as compared to G-CSF treated healthy individuals. We further analysed whether diminished levels of SLPI are associated with the “maturation arrest“ of myeloid cells seen in CN patients. We inhibited SLPI in the CD34+ bone marrow hematopoietic progenitor cells and in the acute myelid leukemia cell line NB4 using lentivirus-based transduction with SLPI-specific

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Jeong, Moon-Jin, Salvador Nares, Gillian Ashcroft, Nikola Angelov, Niki Moutsopoulos, and Sharon Wahl. "Aberrant mucosal wound repair in the absence of secretory leukocyte protease inhibitor." Thrombosis and Haemostasis 92, no. 08 (2004): 288–97. http://dx.doi.org/10.1160/th03-07-0446.

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SummarySecretory leukocyte protease inhibitor (SLPI) is a cationic serine protease inhibitor with anti-microbial and anti-inflammatory properties found in large quantities in mucosal fluids, including saliva. SLPI is expressed during cutaneous wound healing, however, its role in oral wound repair is unknown. We have used a novel approach involving a murine buccal mucosal acute wound model to investigate the role of SLPI in oral healing. In parallel to the observed cutaneous healing phenotype, an absence of SLPI results in markedly impaired oral wound healing associated with increased inflammat

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Abbinante-Nissen, J. M., L. G. Simpson, and G. D. Leikauf. "Neutrophil elastase increases secretory leukocyte protease inhibitor transcript levels in airway epithelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 265, no. 3 (1993): L286—L292. http://dx.doi.org/10.1152/ajplung.1993.265.3.l286.

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Airway inflammation is often associated with the infiltration of activated neutrophils and subsequent protease release. Although aiding in the digestion and phagocytosis of foreign proteins and microorganisms, neutrophil proteases can indiscriminately damage healthy lung tissue. In the conducting airway, proteases, particularly neutrophil elastase, are counter-balanced by several antiproteases, including secretory leukocyte protease inhibitor (SLPI). SLPI can be produced locally by a number of cells including the airway epithelial cell. To examine the effects of neutrophil granule components o

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Fakioglu, Esra, Sarah S. Wilson, Pedro M. M. Mesquita, et al. "Herpes Simplex Virus Downregulates Secretory Leukocyte Protease Inhibitor: a Novel Immune Evasion Mechanism." Journal of Virology 82, no. 19 (2008): 9337–44. http://dx.doi.org/10.1128/jvi.00603-08.

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ABSTRACT Secretory leukocyte protease inhibitor (SLPI), an anti-inflammatory mediator of mucosal immunity, inhibits human immunodeficiency virus (HIV) and herpes simplex virus (HSV) in cell culture. Epidemiological studies demonstrate that higher concentrations of SLPI in mucosal secretions are associated with a reduced risk of HIV transmission. The current studies were designed to test the hypothesis that HSV triggers a loss of SLPI to evade innate immunity and that this response may contribute to the increased risk of HIV infection in the setting of HSV infection. Exposure of human cervical

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Wex, Thomas, Gerhard Treiber, Manfred Nilius, Michael Vieth, Albert Roessner, and Peter Malfertheiner. "Helicobacter pylori-Mediated Gastritis Induces Local Downregulation of Secretory Leukocyte Protease Inhibitor in the Antrum." Infection and Immunity 72, no. 4 (2004): 2383–85. http://dx.doi.org/10.1128/iai.72.4.2383-2385.2004.

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ABSTRACT Helicobacter pylori-infected subjects exhibited a strong decline in antral secretory leukocyte protease inhibitor (SLPI) levels compared to H. pylori-negative subjects and subjects from whom H. pylori had been eradicated (P = 0.002). This reduction was specific for the antrum, whereas SLPI expression in corpus and duodenum was not affected. Antral SLPI levels were inversely correlated with inflammatory scores of antrum-predominant gastritis.

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Westin, U., E. Lundberg, and K. Ohlsson. "IgE-mediated histamine release from nasal mucosa is inhibited by SLPI (secretory leukocyte protease inhibitor) to the level of spontaneous release." Mediators of Inflammation 7, no. 3 (1998): 217–20. http://dx.doi.org/10.1080/09629359891162.

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The secretory leukocyte protease inhibitor (SLPI) is a low-molecular-weight inhibitor of proteases, such as elastase and cathepsin G which are released from leukocytes during phagocytosis. The purpose of this study was to determine whether or not SLPI is able to inhibit IgE-mediated histamine release. Nasal mucosa from 11 test subjects without atopic disposition was used for thisin vitrostudy. We found that SLPI inhibited histamine release in a dose-dependent way but was without influence on the spontaneous release.

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Baqui, A. A. M. A., Timothy F. Meiller, and William A. Falkler. "Enhanced Secretory Leukocyte Protease Inhibitor in Human Immunodeficiency Virus Type 1-Infected Patients." Clinical Diagnostic Laboratory Immunology 6, no. 6 (1999): 808–11. http://dx.doi.org/10.1128/cdli.6.6.808-811.1999.

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ABSTRACT Secretory leukocyte protease inhibitor (SLPI) has been found to possess activity against the human immunodeficiency virus type 1 (HIV-1) in vitro at physiological concentrations. A study was undertaken to evaluate SLPI levels in human saliva and plasma among HIV-positive (HIV+) patients with various HIV-1 viral loads in comparison to uninfected controls. Whole blood in EDTA and unstimulated saliva samples were collected from 37 HIV+patients, of whom 20 had a history of intravenous drug abuse (IVDA). Control samples were collected from 20 appropriate age- and sex-matched HIV-1-negative

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Klimenkova, Olga, Wienke Ellerbeck, Maksim Klimiankou, et al. "A lack of secretory leukocyte protease inhibitor (SLPI) causes defects in granulocytic differentiation." Blood 123, no. 8 (2014): 1239–49. http://dx.doi.org/10.1182/blood-2013-06-508887.

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Key Points The natural inhibitor of neutrophil elastase, SLPI, is severely reduced in severe congenital neutropenia patients. SLPI controls myeloid differentiation by regulation of NFκB, ERK1/2:LEF-1, and c-myc activation.

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Ying, Q. L., M. Kemme, D. Saunders, and S. R. Simon. "Glycosaminoglycans regulate elastase inhibition by oxidized secretory leukoprotease inhibitor." American Journal of Physiology-Lung Cellular and Molecular Physiology 272, no. 3 (1997): L533—L541. http://dx.doi.org/10.1152/ajplung.1997.272.3.l533.

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Secretory leukoprotease inhibitor (SLPI) is one of the major physiological inhibitors protecting respiratory epithelium from attack by excess human leukocyte elastase (HLE), a serine protease released by neutrophils upon activation in response to inflammatory stimuli. Reaction with N-chlorotaurine, a major long-lived oxidant generated by activated neutrophils, oxidized all four methionine residues, but no other amino acids, in SLPI, resulting in substantial diminution of its elastase inhibitory activity. Oxidation of the P1' residue, Met73, accounted for most of the diminution in activity sinc

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Sakata, M., M. Houjyo, K. Higal, and K. Tsubota. "SECRETORY LEUKOCYTE PROTEASE INHIBITOR (SLPI) IN CONJUNCTIVA OF HUMAN." Cornea 19, Supplement 2 (2000): S119. http://dx.doi.org/10.1097/00003226-200011002-00161.

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Balkus, Jennifer, Kathy Agnew, Richard Lawler, Caroline Mitchell, and Jane Hitti. "Effects of Pregnancy and Bacterial Vaginosis on Proinflammatory Cytokine and Secretory Leukocyte Protease Inhibitor Concentrations in Vaginal Secretions." Journal of Pregnancy 2010 (2010): 1–3. http://dx.doi.org/10.1155/2010/385981.

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We compared vaginal proinflammatory cytokine and secretory leukocyte protease inhibitor (SLPI) concentrations among pregnant and nonpregnant women according to bacterial vaginosis (BV) status. One-hundred and twenty-two women at 12–20 weeks' gestation and 133 nonpregnant controls had vaginal concentrations of interleukin (IL)-1β, IL-6, IL-8, and SLPI measured by enzyme immunoassay. Multivariable linear regression was used to evaluate factors independently associated with vaginal cytokine and SLPI response. Pregnancy and BV were both independently associated with increased vaginal concentration

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Mongkolpathumrat, Podsawee, Anusak Kijtawornrat, Eukote Suwan, et al. "Anti-Protease Activity Deficient Secretory Leukocyte Protease Inhibitor (SLPI) Exerts Cardioprotective Effect against Myocardial Ischaemia/Reperfusion." Biomedicines 10, no. 5 (2022): 988. http://dx.doi.org/10.3390/biomedicines10050988.

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Inhibition of proteases shows therapeutic potential. Our previous studies demonstrated the cardioprotection by the Secretory Leukocyte Protease Inhibitor (SLPI) against myocardial ischaemia/reperfusion (I/R) injury. However, it is unclear whether the cardioprotective effect of SLPI seen in our previous works is due to the inhibition of protease enzymes. Several studies demonstrate that the anti-protease independent activity of SLPI could provide therapeutic benefits. Here, we show for the first time that recombinant protein of anti-protease deficient mutant SLPI (L72K, M73G, L74G) (mt-SLPI) co

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Mongkolpathumrat, Podsawee, Anusak Kijtawornrat, Eukote Suwan, et al. "Anti-Protease Activity Deficient Secretory Leukocyte Protease Inhibitor (SLPI) Exerts Cardioprotective Effect against Myocardial Ischaemia/Reperfusion." Biomedicines 10, no. 5 (2022): 988. http://dx.doi.org/10.3390/biomedicines10050988.

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Inhibition of proteases shows therapeutic potential. Our previous studies demonstrated the cardioprotection by the Secretory Leukocyte Protease Inhibitor (SLPI) against myocardial ischaemia/reperfusion (I/R) injury. However, it is unclear whether the cardioprotective effect of SLPI seen in our previous works is due to the inhibition of protease enzymes. Several studies demonstrate that the anti-protease independent activity of SLPI could provide therapeutic benefits. Here, we show for the first time that recombinant protein of anti-protease deficient mutant SLPI (L72K, M73G, L74G) (mt-SLPI) co

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Mongkolpathumrat, Podsawee, Anusak Kijtawornrat, Eukote Suwan, et al. "Anti-Protease Activity Deficient Secretory Leukocyte Protease Inhibitor (SLPI) Exerts Cardioprotective Effect against Myocardial Ischaemia/Reperfusion." Biomedicines 10, no. 5 (2022): 988. http://dx.doi.org/10.3390/biomedicines10050988.

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Abstract:

Inhibition of proteases shows therapeutic potential. Our previous studies demonstrated the cardioprotection by the Secretory Leukocyte Protease Inhibitor (SLPI) against myocardial ischaemia/reperfusion (I/R) injury. However, it is unclear whether the cardioprotective effect of SLPI seen in our previous works is due to the inhibition of protease enzymes. Several studies demonstrate that the anti-protease independent activity of SLPI could provide therapeutic benefits. Here, we show for the first time that recombinant protein of anti-protease deficient mutant SLPI (L72K, M73G, L74G) (mt-SLPI) co

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Wei, Zhijiang, Guiying Liu, Rufu Jia, et al. "Targeting secretory leukocyte protease inhibitor (SLPI) inhibits colorectal cancer cell growth, migration and invasion via downregulation of AKT." PeerJ 8 (July 14, 2020): e9400. http://dx.doi.org/10.7717/peerj.9400.

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The secretory leukocyte protease inhibitor (SLPI) is a serine protease inhibitor which plays important role in bacterial infection, inflammation, wound healing and epithelial proliferation. Dysregulation of SLPI has been reported in a variety of human cancers including glioblastoma, lung, breast, ovarian and colorectal carcinomas and is associated with tumor aggressiveness and metastatic potential. However, the pathogenic role of SLPI in colorectal cancer is still unclear. Here we showed that SLPI mRNA level was significantly upregulated in colorectal cancer tissues compared to adjacent normal

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Song, Xiao-yu, Li Zeng, Wenwen Jin, et al. "Secretory Leukocyte Protease Inhibitor Suppresses the Inflammation and Joint Damage of Bacterial Cell Wall–Induced Arthritis." Journal of Experimental Medicine 190, no. 4 (1999): 535–42. http://dx.doi.org/10.1084/jem.190.4.535.

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Disruption of the balance between proteases and protease inhibitors is often associated with pathologic tissue destruction. To explore the therapeutic potential of secretory leukocyte protease inhibitor (SLPI) in erosive joint diseases, we cloned, sequenced, and expressed active rat SLPI, which shares the protease-reactive site found in human SLPI. In a rat streptococcal cell wall (SCW)-induced model of inflammatory erosive polyarthritis, endogenous SLPI was unexpectedly upregulated at both mRNA and protein levels in inflamed joint tissues. Systemic delivery of purified recombinant rat SLPI in

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Bingle, L., R. J. Richards, B. Fox, L. Masek, A. Guz, and T. D. Tetley. "Susceptibility of lung epithelium to neutrophil elastase: protection by native inhibitors." Mediators of Inflammation 6, no. 5-6 (1997): 345–54. http://dx.doi.org/10.1080/09629359791488.

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The development of emphysema is thought to be due to an imbalance of proteases (especially neutrophil elastase [NE]) and antiproteases with loosening of the respiratory epithelium as an early event. We investigated the effect of NE on respiratory epithelial cell adherence in vitro , in the presence of varying concentrations and combinations of native inhibitors, α-1-proteinase inhibitor (PI) and secretory leukoprotease inhibitor (SLPI). SLPI was two to 12 times more effective than PI at preventing the effects of NE, especially when enzyme:inhibitor ratios were almost equivalent. Even when the

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McGarry, Niamh, Catherine M. Greene, Noel G. McElvaney, Sinéad Weldon, and Clifford C. Taggart. "The Ability of Secretory Leukocyte Protease Inhibitor to Inhibit Apoptosis in Monocytes Is Independent of Its Antiprotease Activity." Journal of Immunology Research 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/507315.

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Secretory Leukocyte Protease Inhibitor (SLPI) is a serine protease inhibitor produced by epithelial and myeloid cells with anti-inflammatory properties. Research has shown that SLPI exerts its anti-inflammatory activity by directly binding to NF-κB DNA binding sites and, in so doing, prevents binding and subsequent transcription of proinflammatory gene expression. In the current study, we demonstrate that SLPI can inhibit TNF-α-induced apoptosis in U937 cells and peripheral blood monocytes. Specifically, SLPI inhibits TNF-α-induced caspase-3 activation and DNA degradation associated with apopt

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Ma, Ge, Teresa Greenwell-Wild, Kejian Lei, et al. "Secretory Leukocyte Protease Inhibitor Binds to Annexin II, a Cofactor for Macrophage HIV-1 Infection." Journal of Experimental Medicine 200, no. 10 (2004): 1337–46. http://dx.doi.org/10.1084/jem.20041115.

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The distribution of secretory leukocyte protease inhibitor (SLPI) at entry portals indicates its involvement in defending the host from pathogens, consistent with the ability of SLPI to inhibit human immunodeficiency virus (HIV)-1 infection by an unknown mechanism. We now demonstrate that SLPI binds to the membrane of human macrophages through the phospholipid-binding protein, annexin II. Based on the recent identification of human cell membrane phosphatidylserine (PS) in the outer coat of HIV-1, we define a novel role for annexin II, a PS-binding moiety, as a cellular cofactor supporting macr

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Chattopadhyay, Amit, Laurie R. Gray, Lauren L. Patton, et al. "Salivary Secretory Leukocyte Protease Inhibitor and Oral Candidiasis in Human Immunodeficiency Virus Type 1-Infected Persons." Infection and Immunity 72, no. 4 (2004): 1956–63. http://dx.doi.org/10.1128/iai.72.4.1956-1963.2004.

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ABSTRACT Oropharyngeal candidiasis, typically caused by Candida albicans, is the most common oral disease associated with human immunodeficiency virus type 1 (HIV-1) infection. Secretory leukocyte protease inhibitor (SLPI), a 12-kDa antiprotease, suppresses the growth of C. albicans in vitro. To determine whether the mucosal protein plays a role in protecting oral tissues against fungal infection, we conducted a cross-sectional study investigating the oral and systemic health and salivary SLPI levels in 91 dentate HIV-1-infected adults receiving medical care in the southeastern United States.

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Putra, Putu Adi Sujana, Ketut Suwiyoga, I. Nyoman Gede Budiana, I. Wayan Megadhana, I. Nyoman Bayu Mahendra, and I. Made Darmayasa. "Akurasi kadar serum Secretory Leukocyte Protease Inhibitor (SLPI) dalam menunjang diagnosis kanker ovarium: suatu uji diagnostik." Intisari Sains Medis 13, no. 2 (2022): 367–72. http://dx.doi.org/10.15562/ism.v13i2.1361.

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Background: Ovarian cancer is one of the most common malignant tumors found in reproductive organs in vitro. Secretory Leukocyte Protease Inhibitor (SLPI) protein is essential for the growth of ovarian cancer cells, a protein that maintains the survival of ovarian cancer cells, inhibits antiproliferative effects, and reverses the proapoptotic effect of elastase. This study aims to evaluate the role of SLPI in diagnosing ovarium cancer. Methods: The research was conducted at the Obstetrics and Gynecology Polyclinic, Sanglah Hospital, Denpasar and the Prodia Laboratory. Sampling of this study ha

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McNeely, Tessie B., Diane C. Shugars, Mary Rosendahl, Christina Tucker, Stephen P. Eisenberg, and Sharon M. Wahl. "Inhibition of Human Immunodeficiency Virus Type 1 Infectivity by Secretory Leukocyte Protease Inhibitor Occurs Prior to Viral Reverse Transcription." Blood 90, no. 3 (1997): 1141–49. http://dx.doi.org/10.1182/blood.v90.3.1141.

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Abstract Infection of monocytes with human immunodeficiency virus type 1Ba-L (HIV-1Ba-L ) is significantly inhibited by treatment with the serine protease inhibitor, secretory leukocyte protease inhibitor (SLPI). SLPI does not appear to act on virus directly, but rather the inhibitory activity is most likely due to interaction with the host cell. The current study was initiated to investigate how SLPI interacts with monocytes to inhibit infection. SLPI was found to bind to monocytes with high affinity to a single class of receptor sites (∼7,000 receptors per monocyte, KD = 3.6 nmol/L). The put

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McNeely, Tessie B., Diane C. Shugars, Mary Rosendahl, Christina Tucker, Stephen P. Eisenberg, and Sharon M. Wahl. "Inhibition of Human Immunodeficiency Virus Type 1 Infectivity by Secretory Leukocyte Protease Inhibitor Occurs Prior to Viral Reverse Transcription." Blood 90, no. 3 (1997): 1141–49. http://dx.doi.org/10.1182/blood.v90.3.1141.1141_1141_1149.

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Infection of monocytes with human immunodeficiency virus type 1Ba-L (HIV-1Ba-L ) is significantly inhibited by treatment with the serine protease inhibitor, secretory leukocyte protease inhibitor (SLPI). SLPI does not appear to act on virus directly, but rather the inhibitory activity is most likely due to interaction with the host cell. The current study was initiated to investigate how SLPI interacts with monocytes to inhibit infection. SLPI was found to bind to monocytes with high affinity to a single class of receptor sites (∼7,000 receptors per monocyte, KD = 3.6 nmol/L). The putative SLP

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Böhm, B., R. Deutzmann, and H. Burkhardt. "Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions." Biochemical Journal 274, no. 1 (1991): 269–73. http://dx.doi.org/10.1042/bj2740269.

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An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 2

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OHLSSON, KJELL, ANDERS BJARTELL, and HANS LILJA. "Secretory Leucocyte Protease Inhibitor in the Male Genital Tract: PSA‐Induced Proteolytic Processing in Human Semen and Tissue Localization." Journal of Andrology 16, no. 1 (1995): 64–74. http://dx.doi.org/10.1002/j.1939-4640.1995.tb01733.x.

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ABSTRACT: Secretory leucocyte protease inhibitor, SLPI, is a low‐molecular‐weight, acid‐stable protein present in the liquid part of fresh human ejaculate but not demonstrable in the gel structure. No fragmentation of SLPI occurred during gel dissolution, but a slow proteolytic cleavage of SLPI was seen on incubation of the liquified semen at 37°C. The same pattern of degradation products was seen after incubation of SLPI with prostatic secretion and also with purified prostate‐specific antigen, PSA. We could identify Arg 20‐Tyr 21 and Met 73‐Leu 74 to be the primary cleavage sites upon proteo

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