Evidence of surfactant protein A and D expression decrement and their localizations in human prostate adenocarcinomas

Kankavi, Orhan; Baykara, Mehmet; Karanis, Meryem İlkay Eren; Başsorgun, Cumhur İ̇brahim; Ergin, Hale; Çiftçioğlu, M. Akif

doi:10.3109/0886022x.2013.846831

Cited by 13 publications

(11 citation statements)

References 27 publications

(33 reference statements)

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“…This fact has already been described for other tissue and results from intensive post-translational processing of the surfactant proteins [ 20 , 21 ]. As the presence of surfactant proteins within human and murine prostate has qualitatively already been described by others the corresponding results of this study are not entirely novel [ 22 – 24 ]. As the intensity of the protein bands obtained in the Western blot experiments does not stoichiometric correlate with the protein concentration only subjective quantification would be possible.…”

Section: Discussionsupporting

confidence: 81%

Expression and Localization of Lung Surfactant Proteins in Human Testis

Beileke

Claassen

Wagner³

et al. 2015

PLoS ONE

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BackgroundSurfactant proteins (SPs) have been described in various tissues and fluids including tissues of the nasolacrimal apparatus, airways and digestive tract. Human testis have a glandular function as a part of the reproductive and the endocrine system, but no data are available on SPs in human testis and prostate under healthy and pathologic conditions.ObjectiveThe aim of the study was the detection and characterization of the surfactant proteins A, B, C and D (SP-A, SP-B, SP-C, SP-D) in human testis. Additionally tissue samples affected by testicular cancer were investigated.ResultsSurfactant proteins A, B, C and D were detected using RT-PCR in healthy testis. By means of Western blot analysis, these SPs were detected at the protein level in normal testis, seminoma and seminal fluid, but not in spermatozoa. Expression of SPs was weaker in seminoma compared to normal testicular tissue. SPs were localized in combination with vimentin immunohistochemically in cells of Sertoli and Leydig.ConclusionSurfactant proteins seem to be inherent part of the human testis. By means of physicochemical properties the proteins appear to play a role during immunological and rheological process of the testicular tissue. The presence of SP-B and SP-C in cells of Sertoli correlates with their function of fluid secretion and may support transportation of spermatozoa. In seminoma the expression of all SP's was generally weaker compared to normal germ cells. This could lead to a reduction of immunomodulatory and rheology processes in the germ cell tumor.

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Section: Discussionsupporting

confidence: 81%

Expression and Localization of Lung Surfactant Proteins in Human Testis

Beileke

Claassen

Wagner³

et al. 2015

PLoS ONE

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“…Lysate proteins (30 μg) were separated on 15% SDS-PAGE polyacrylamide gel and electrophoretically transferred onto PVDF membranes (Pall Corporation, NY, USA). The blot was probed with primary antibodies raised against human SP-D [a gift from Uffe Holmskov, (13)], Phosphorylated-p53 (Ser 15) (Cell Signaling Technology), pAKT (PathScan® Multiplex Western Cocktail I), pan Akt (ABclonal), phospho-Bad-S155 (ABclonal), Bcl-2 associated death promoter (Bad) (Apoptosis I sampler Kit), Bcl-2-associated X protein (Bax) (Apoptosis I sampler Kit), B-cell lymphoma 2 (Bcl2) (Apoptosis I sampler Kit) or caspase 7 (Cell Signaling Technology), followed by HRP-conjugated secondary antibodies. All western blot images were acquired by Syngene (Chem Genius) and quantified by Syngene Gene Tools.…”

Section: Methodsmentioning

confidence: 99%

“…Elevated levels of SP-D at inflamed sites in the prostate manifested protection against bacterial infection (11, 12). Kankavi et al (13) observed differential expression of SP-D in glandular structures of inflamed malignant and non-malignant human prostate tissues. There was a significant correlation between decreased levels of SP-D and increased Gleason score, a grading system based on the histologic pattern of arrangement of carcinoma cells, and tumor volume.…”

Section: Introductionmentioning

confidence: 99%

Human SP-D Acts as an Innate Immune Surveillance Molecule Against Androgen-Responsive and Androgen-Resistant Prostate Cancer Cells

et al. 2019

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Surfactant Protein D (SP-D), a pattern recognition innate immune molecule, has been implicated in the immune surveillance against cancer. A recent report showed an association of decreased SP-D expression in human prostate adenocarcinoma with an increased Gleason score and severity. In the present study, the SP-D expression was evaluated in primary prostate epithelial cells (PrEC) and prostate cancer cell lines. LNCaP, an androgen dependent prostate cancer cell line, exhibited significantly lower mRNA and protein levels of SP-D than PrEC and the androgen independent cell lines (PC3 and DU145). A recombinant fragment of human SP-D, rfhSP-D, showed a dose and time dependent binding to prostate cancer cells via its carbohydrate recognition domain. This study, for the first time, provides evidence of significant and specific cell death of tumor cells in rfhSP-D treated explants as well as primary tumor cells isolated from tissue biopsies of metatstatic prostate cancer patients. Viability of PrEC was not altered by rfhSP-D. Treated LNCaP (p53 +/+ ) and PC3 (p53 −/− ) cells exhibited reduced cell viability in a dose and time dependent manner and were arrested in G2/M and G1/G0 phase of the cell cycle, respectively. rfhSP-D treated LNCaP cells showed a significant upregulation of p53 whereas a significant downregulation of pAkt was observed in both PC3 and LNCaP cell lines. The rfhSP-D-induced apoptosis signaling cascade involved upregulation of Bax:Bcl2 ratio, cytochrome c and cleaved products of caspase 7. The study concludes that rfhSP-D induces apoptosis in prostate tumor explants as well as in androgen dependent and independent prostate cancer cells via p53 and pAkt pathways.

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“…A monoclonal SP-D antibody showed the band at 43 kDa in sperm. The same group then followed with an in depth study to determine how surfactant proteins are altered in prostate adenocarcinomas (Kankavi et al, 2014). Protein expressions were tested by IHC and Western blots.…”

Section: Review Of the Localization And Known Functions Of Extra-pmentioning

confidence: 99%

Structure, genetics and function of the pulmonary associated surfactant proteins A and D: The extra-pulmonary role of these C type lectins

Vieira

Kung

Bhatti

2017

Annals of Anatomy - Anatomischer Anzeiger

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The collectins family encompasses several collagenous Ca2+-dependent defense lectins that are described as pathogen recognition molecules. They play an important role in both adaptive and innate immunity. Surfactant protein A and D are two of these proteins which were initially discovered in association with surfactant in the pulmonary system. The structure, immune and inflammatory functions, and genetic variations have been well described in relation to their roles, function and pathophysiology in the pulmonary system. Subsequently, these proteins have been discovered in a wide range of other organs and organ systems. The role of these proteins outside the pulmonary system is currently an active area of research. This review intends to provide a current overview of the genetics, structure and extra-pulmonary functions of the surfactant collectin proteins.

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Evidence of surfactant protein A and D expression decrement and their localizations in human prostate adenocarcinomas

Abstract: The development of prostate cancer may be related to decreased level of surfactant protein A and D.

Cited by 13 publications

References 27 publications

Expression and Localization of Lung Surfactant Proteins in Human Testis

Expression and Localization of Lung Surfactant Proteins in Human Testis

Human SP-D Acts as an Innate Immune Surveillance Molecule Against Androgen-Responsive and Androgen-Resistant Prostate Cancer Cells

Structure, genetics and function of the pulmonary associated surfactant proteins A and D: The extra-pulmonary role of these C type lectins

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