scholarly journals Regulation of re-epithelialization and immune modulation by surfactant, surfactant protein A and transforming growth factor β

2012 ◽  
Author(s):  
C.H.M.P. Willems
Keyword(s):  
Growth Factor ◽  
Immune Modulation ◽  
Transforming Growth Factor ◽  
Protein A ◽  
Transforming Growth Factor Β ◽  
Surfactant Protein ◽  
Surfactant Protein A

Transforming growth factor-β inhibits surfactant protein A expression in vitro

1992 ◽  
Vol 1123 (3) ◽  
pp. 257-262 ◽  
Author(s):  
Jeffrey A. Whitsett ◽  
Ailsa Budden ◽  
William M. Hull ◽  
Jean C. Clark ◽  
Michael A. O'Reilly
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Protein A ◽  
Transforming Growth Factor Β ◽  
Surfactant Protein ◽  
Surfactant Protein A

Surfactant protein A is a required mediator of keratinocyte growth factor after experimental marrow transplantation

2003 ◽  
Vol 285 (3) ◽  
pp. L602-L610 ◽  
Author(s):  
Imad Y. Haddad ◽  
Carlos Milla ◽  
Shuxia Yang ◽  
Angela Panoskaltsis-Mortari ◽  
Samuel Hawgood ◽  
...  
Keyword(s):  
Weight Loss ◽  
Growth Factor ◽  
Marrow Transplantation ◽  
Keratinocyte Growth Factor ◽  
Allogeneic Bone Marrow Transplantation ◽  
Protein A ◽  
Conditioning Regimen ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Allogeneic Bone

We reported an association between the ability of recombinant human keratinocyte growth factor (rHuKGF) to upregulate the expression of surfactant protein A (SP-A) and to downregulate pulmonary inflammation that occurs after allogeneic bone marrow transplantation (BMT). To establish a causal relationship, rHuKGF (5 mg/kg) was administered subcutaneously for three consecutive days before irradiation to SP-A-sufficient and -deficient [SP-A(+/+) and SP-A(-/-), respectively] mice given inflammation-inducing allogeneic spleen T cells at the time of BMT. In contrast with SP-A(+/+) mice, rHuKGF failed to suppress the high levels of TNF-α, IFN-γ, and nitric oxide contained in bronchoalveolar lavage fluids collected on day 7 after BMT from SP-A(-/-) mice. Early post-BMT weight loss was attenuated by rHuKGF in both SP-A(+/+) and SP-A(-/-) recipients. In the absence of supportive respiratory care, however, SP-A deficiency eventually abolished the ability of rHuKGF to prevent weight loss and to improve survival monitored for 1 mo after allogeneic BMT. In further experiments, the addition of cyclophosphamide (which is known to cause severe injury to the alveolar epithelium in donor T cell-recipient mice) to the conditioning regimen prevented rHuKGF-induced upregulation of SP-A and suppression of lung inflammation in both SP-A(+/+) and SP-A(-/-) mice. We conclude that endogenous baseline SP-A levels and optimal upregulation of SP-A are required for the anti-inflammatory protective effects of KGF after allogeneic transplantation.

Transforming growth factor-β is a potent inhibitor of basal and stimulated relaxin release by porcine luteal cells maintained in monolayer culture

1992 ◽  
Vol 135 (3) ◽  
pp. 543-550 ◽  
Author(s):  
M. J. Taylor ◽  
C. L. Clark
Keyword(s):  
Growth Factor ◽  
Time Course ◽  
Transforming Growth Factor ◽  
Protein A ◽  
Plaque Assay ◽  
Transforming Growth Factor Β ◽  
Luteal Cell ◽  
Prostaglandin E ◽  
Hormone Release ◽  
Luteal Cells

ABSTRACT The effect of transforming growth factor-β (TGF-β) on relaxin release by porcine large luteal cells (LLC) was examined by use of a reverse haemolytic plaque assay. In this assay, mixed luteal cells were co-cultured in monolayers with protein A-coupled sheep erythrocytes. In the presence of complement and porcine relaxin antiserum, a zone of haemolysis (a plaque) developed around relaxin-releasing LLCs. The rate of plaque development in time-course experiments and the average size of plaque areas were used to monitor the rate of relaxin release and cumulative amounts of hormone respectively. Monolayers were bathed in medium containing TGF-β alone, or in the co-presence of a stimulatory secretagogue (prostaglandin E2; PGE2). Exposure of luteal cell-containing monolayers to TGF-β (1 ng/1–100 μg/l) elicited a dose-related inhibition in the rate of basal relaxin release. Minimal and maximal concentrations were approximately 10 ng/l and 10 μg/l respectively. Treatment with 1 μg TGF-β/l reduced the cumulative amount of relaxin released to 63 ± 6% of control values (mean ± s.d., P < 0·05, n = 6; averaged over the whole course of the experimental incubation). Exposure of monolayers treated with TGF-β to the relaxin-stimulatory secretagogue PGE2 (0·1 μmol) resulted in a significant (P < 0·05) increase in the amount of relaxin released by TGF-β-suppressed LLCs, and restored rates of hormone release to control levels. This is evidence that TGF-β and PGE2 interact antagonistically in the modulation of relaxin. The effect of TGF-β was strictly time-dependent. A period of at least 16 h of treatment with TGF-β was required to induce an inhibitory effect on relaxin. These results implicate TGF-β as a novel inhibitor of relaxin release, and the presence of TGF-β in porcine luteal tissue suggests that such regulation may be achieved via paracrine or autocrine routes. It is possible that TGF-β interacts functionally during luteal life with other secretagogues to achieve integrated control of hormone release. Journal of Endocrinology (1992) 135, 543–550

scholarly journals Mechanical Ventilation Down-Regulates Surfactant Protein A and Keratinocyte Growth Factor Expression in Premature Rabbits

2007 ◽  
Vol 62 (3) ◽  
pp. 277-282 ◽  
Author(s):  
Robert J Digeronimo ◽  
Shamimunisa B Mustafa ◽  
Rita M Ryan ◽  
Zohara Z Sternberg ◽  
Daniel J Ashton ◽  
...  
Keyword(s):  
Mechanical Ventilation ◽  
Growth Factor ◽  
Keratinocyte Growth Factor ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Factor Expression ◽  
Growth Factor Expression

scholarly journals Surfactant Protein A, a Novel Regulator for Smooth Muscle Phenotypic Modulation and Vascular Remodeling

2020 ◽  
Author(s):  
Ran Ran ◽  
Dunpeng Cai ◽  
Skylar D. King ◽  
Xingyi Que ◽  
Jonathan M. Bath ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Growth Factor ◽  
Protein Expression ◽  
Vascular Remodeling ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Contractile Protein ◽  
Phenotypic Modulation

Objective: The objective of this study is to determine the role of SPA (surfactant protein A) in vascular smooth muscle cell (SMC) phenotypic modulation and vascular remodeling. Approach and Results: PDGF-BB (Platelet-derived growth factor-BB) and serum induced SPA expression while downregulating SMC marker gene expression in SMCs. SPA deficiency increased the contractile protein expression. Mechanistically, SPA deficiency enhanced the expression of myocardin and TGF (transforming growth factor)-β, the key regulators for contractile SMC phenotype. In vivo, SPA was induced in medial and neointimal SMCs following mechanical injury in both rat and mouse carotid arteries. SPA knockout in mice dramatically attenuated the wire injury-induced intimal hyperplasia while restoring SMC contractile protein expression in medial SMCs. These data indicate that SPA plays an important role in SMC phenotype modulation and vascular remodeling in vivo. Conclusions: SPA is a novel protein factor modulating SMC phenotype. Blocking the abnormal elevation of SPA may be a potential strategy to inhibit the development of proliferative vascular diseases.

An In Silico Investigation of Potential EGFR Inhibitors for the Clinical Treatment of Colorectal Cancer

2019 ◽  
Vol 18 (27) ◽  
pp. 2355-2366 ◽  
Author(s):  
Manisha Majhi ◽  
Meer Asif Ali ◽  
Akanksha Limaye ◽  
Kritika Sinha ◽  
Praveena Bairagi ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Molecular Docking ◽  
Growth Factor ◽  
Virtual Screening ◽  
Transforming Growth Factor ◽  
Transmembrane Protein ◽  
Protein A ◽  
Growth Factor Receptor ◽  
Transforming Growth Factor Β ◽  
Egfr Inhibitors

Colorectal cancer possesses the third highest diagnostic rate and is the second leading cause of cancer death in the USA as reported by NIH. Epidermal Growth Factor Receptor (EGFR), a transmembrane protein, participates in PLC gamma-1, RAS-RAF-MEK-MAPKs, phosphatidylinositol-3 kinase, Akt pathways and plays a key role in normal functioning of cell division, cell differentiation, apoptosis and migration. This protein is found to be overexpressed in more than 60% of the colorectal cancers. Overexpressed EGFR advances the tumorigenic properties through cell cycle dysregulation and activates signaling pathways linked to cancer such as WNT/β-catenin, transforming growth factor β (TGF-β) and phosphoinositide-3-kinase (PI3K). Inhibiting the overexpressed EGFR protein has been proposed for the treatment and many inhibitors have been reported suppressing the activity of EGFR. However, patients in malignant state of cancer show resistance to those inhibitors, which open a wide space to research for the discovery of novel inhibitors. The present study employed Molecular Docking and Virtual Screening to find novel inhibitors with high affinity against EGFR. Molecular docking of existing inhibitors resulted in the compound titled as BGB-283 (PubChem CID-89670174) having the highest score, which was subjected to similarity search to retrieve the drugs with similar structure. The virtual screening concluded a compound SCHEMBL18435602 (PubChem CID-126517400) which revealed a better affinity with the target protein. A comparative study of both the compounds showed equivalent pharmacokinetic properties. These identified drugs have a high potential to act as EGFR inhibitors and can show promising results in the research of colorectal cancer.

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