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The Pharmacological Potential of Marine-Derived Peptides and Proteins

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A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (31 December 2018) | Viewed by 63547

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Special Issue Editors

Dr. Rim Nasri

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Guest Editor

Universite de Sfax, Lab Genie Enzymat & Microbiol, Ecole Natl Ingn Sfax, BP 1173-3038, Sfax, Tunisia
Interests: proteins; antioxidant activity; enzymes; biotechnology; biochemistry; chemical biology; protein purification; enzymatic assay; protein chemistry; enzymology; antioxidants; biopeptides

Dr. Mourad Jridi

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Guest Editor

Universite de Sfax, ENIS, Lab Genie Enzymat & Microbiol, Sfax, Tunisia
Interests: biotechnology; biostatistics; structural biology

Special Issue Information

Dear Colleagues,

The novel trend that invades the international market is the request for marine functional products by consumers. Indeed, marine organisms represent a valuable source of natural and new bioactive substances that provide body nutritional requirement and potential effects for promoting health. In particular, proteins and, naturally, peptides, extracted from different marine sources (macro- and microalgae, fish, mollusks, crustaceans and bivalves) and fishery waste, have attracted increasing attention owing to their pharmaceutical properties. Additionally, the development of marine fish-derived biologically-active peptides, using appropriate proteases, and under controlled conditions, has increased during the past decade due to their numerous and multifunctional bioactivites, including antioxidant, antimicrobial, anticancer, anti-aging, hypotensive, etc. Indeed, marine peptides have had their therapeutic potential assessed to prevent against several diseases, such as cancer, cardiovascular diseases, inflammation, diabetic complications, wound lesions, etc. Moreover, marine proteins are well known as functional and gelling agents used in pharmaceutical industries during drug encapsulation and delivery. Collagen and gelatin have also been utilized for various pharmaceutical applications, such as tissue engineering.

This Special Issue of Marine Drugs aims to present existing knowledge and recent research studies on bioactive marine proteins, naturally and marine-derived peptides, as well as their potential pharmaceutical applications.

Papers on related model systems, structural conformational studies, theoretical developments and new analytical techniques are welcome. All papers are required to focus primarily on at least one named biological marine bio-molecule. This naming should appear in the title, the abstract and the text of the paper. Crude extracts without purification are not acceptable for publication in this Special Issue.

Dr. Rim Nasri
Dr. Mourad Jridi
Guest Editors

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

marine resources
pharmaceutical effects
Marine-derived peptides
naturally peptides
marine proteins

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Research

19 pages, 3744 KiB

Open AccessArticle

Assessment of Cholesterol, Glycemia Control and Short- and Long-Term Antihypertensive Effects of Smooth Hound Viscera Peptides in High-Salt and Fructose Diet-Fed Wistar Rats

by Ola Abdelhedi, Hana Khemakhem, Rim Nasri, Mourad Jridi, Leticia Mora, Ikram Ben Amor, Kamel Jamoussi, Fidel Toldrá, Jalel Gargouri and Moncef Nasri

Mar. Drugs 2019, 17(4), 194; https://doi.org/10.3390/md17040194 - 27 Mar 2019

Cited by 15 | Viewed by 3107

Abstract

In this study, the antihypertensive activity of Purafect^®-smooth hound viscera protein hydrolysate (VPH) and its peptide fraction with molecular weight (MW) below 1 kDa (VPH-I) was investigated. In addition, the lipase inhibitory activity, as well the anticoagulant potential, in vitro, were assessed. The antihypertensive effects of VPH and VPH-I were studied during 24 h (short-term effect) and 30 days (long-term effect) using high-salt (18% NaCl) and -fructose (10%) diet (HSFD)-induced hypertension. Data showed that, 4 h post-administration of VPH and VPH-I (200 mg/kg BW), the systolic blood pressure of rats was reduced by about 6 and 9 mmHg, respectively. These effects were similar to that obtained with Captopril (~9 mmHg at t = 4 h). On the other hand, exposing the rats to daily to HSFD, coupled to the administration of viscera peptides, was found to attenuate hypertension. In addition, the proteins’ treatments were able to correct lipid and glycemic disorders, by reducing the total cholesterol and triglyceride contents and resorting to the plasma glucose level, compared to the HSFD group. Overall, the present findings demonstrated the preventive effect of VPH-peptides from hypertension complications, as a result of their biological properties. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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14 pages, 2761 KiB

Open AccessArticle

Wound Healing Potential of Spirulina Protein on CCD-986sk Cells

by Ping Liu, Jeong-Wook Choi, Min-Kyeong Lee, Youn-Hee Choi and Taek-Jeong Nam

Mar. Drugs 2019, 17(2), 130; https://doi.org/10.3390/md17020130 - 22 Feb 2019

Cited by 21 | Viewed by 6030

Abstract

Wound healing is a dynamic and complex process. The proliferation and migration of dermal fibroblasts are crucial for wound healing. Recent studies have indicated that the extracts from Spirulina platensis have a positive potential for wound healing. However, its underlying mechanism is not fully understood. Our previous study showed that spirulina crude protein (SPCP) promoted the viability of human dermal fibroblast cell line (CCD-986sk cells). In this study, we further investigated the wound healing effect and corresponding mechanisms of SPCP on CCD-986sk cells. Bromodeoxyuridine (BrdU) assay showed that SPCP promoted the proliferation of CCD-986sk cells. The wound healing assay showed that SPCP promoted the migration of CCD-986sk cells. Furthermore, cell cycle analysis demonstrated that SPCP promoted CCD-986sk cells to enter S and G₂/M phases from G₀/G₁ phase. Western blot results showed that SPCP significantly upregulated the expression of cyclin D1, cyclin E, cyclin-dependent kinase 2 (Cdk2), cyclin-dependent kinase 4 (Cdk4), and cyclin-dependent kinase 6 (Cdk6), as well as inhibited the expression of CDK inhibitors p21 and p27 in CCD-986sk cells. In the meanwhile, SPCP promoted the phosphorylation and activation of phosphoinositide 3-kinase (PI3K) and protein kinase B (Akt). However, the phosphorylation of Akt was significantly blocked by PI3K inhibitor (LY294002), which in turn reduced the SPCP-induced proliferation and migration of CCD-986sk cells. Therefore, the results presenting in this study suggested that SPCP can promote the proliferation and migration of CCD-986sk cells; the PI3K/Akt signaling pathway play a positive and important role in these processes. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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11 pages, 1276 KiB

Open AccessArticle

Anti-Inflammatory Activity of β-thymosin Peptide Derived from Pacific Oyster (Crassostrea gigas) on NO and PGE₂ Production by Down-Regulating NF-κB in LPS-Induced RAW264.7 Macrophage Cells

by Dukhyun Hwang, Min-jae Kang, Mi Jeong Jo, Yong Bae Seo, Nam Gyu Park and Gun-Do Kim

Mar. Drugs 2019, 17(2), 129; https://doi.org/10.3390/md17020129 - 21 Feb 2019

Cited by 69 | Viewed by 5878

Abstract

β-thymosin is known for having 43 amino acids, being water-soluble, having a light molecular weight and ubiquitous polypeptide. The biological activities of β-thymosin are diverse and include the promotion of wound healing, reduction of inflammation, differentiation of T cells and inhibition of apoptosis. Our previous studies showed that oyster β-thymosin originated from the mantle of the Pacific oyster, Crassostrea gigas and had antimicrobial activity. In this study, we investigated the anti-inflammatory effects of oyster β-thymosin in lipopolysaccharide (LPS)-induced RAW264.7 macrophage cells using human β-thymosin as a control. Oyster β-thymosin inhibited the nitric oxide (NO) production as much as human β-thymosin in LPS-induced RAW264.7 cells. It also showed that oyster β-thymosin suppressed the expression of prostaglandin E₂ (PGE₂), inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2). Moreover, oyster β-thymosin reduced inflammatory cytokines such as tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β) and interleukin-6 (IL-6). Oyster β-thymosin also suppressed the nuclear translocation of phosphorylated nuclear factor-κB (NF-κB) and degradation of inhibitory κB (IκB) in LPS-induced RAW264.7 cells. These results suggest that oyster β-thymosin, which is derived from the mantle of the Pacific oyster, has as much anti-inflammatory effects as human β-thymosin. Additionally, oyster β-thymosin suppressed NO production, PGE₂ production and inflammatory cytokines expression via NF-κB in LPS-induced RAW264.7 cells. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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21 pages, 3317 KiB

Open AccessArticle

Antioxidative Peptides from Proteolytic Hydrolysates of False Abalone (Volutharpa ampullacea perryi): Characterization, Identification, and Molecular Docking

by Shudong He, Yi Zhang, Hanju Sun, Ming Du, Jianlei Qiu, Mingming Tang, Xianbao Sun and Beiwei Zhu

Mar. Drugs 2019, 17(2), 116; https://doi.org/10.3390/md17020116 - 13 Feb 2019

Cited by 36 | Viewed by 5073

Abstract

Antioxidative peptides were produced from false abalone (Volutharpa ampullacea perryi) using enzymatic hydrolysis. Trypsin produced the most bioactive hydrolysates with the highest scavenging ABTS^+• free radicals compared to pepsin, alcalase, neutrase, and flavourzyme. The response surface methodology studies on trypsin hydrolysis indicated that the hydrolysis temperature, time, and pH were interacted with each other (p < 0.05), and the optimal conditions were hydrolysis at 51.8 °C for 4.1 h, pH 7.7 and the maximum predicted hydrolysis degree was 13.18% and ABTS^+• scavenging activity of 79.42%. The optimized hydrolysate was subjected to ultrafiltration fractionation, and the fraction with MW < 3 kDa showed the highest ABTS^+• scavenging activity. There were 193 peptide sequences identified from this peptide fraction and 133 of them were successfully docked onto human myeloperoxidase (MPO), an enzyme involved in forming reactive oxidants in vivo. The highest scored peptide, no. 39, consists of DTETGVPT. Its structure and molecular interactions with MPO active site were compared with previously characterized peptide hLF1-11. The interactions between peptide no. 39 and MPO include electrostatic charge, hydrogen bonds, and covalent bonds. The antioxidative peptide produced in this research may exert antioxidant activity in vivo due to its potential inhibition effect on MPO. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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14 pages, 2733 KiB

Open AccessArticle

Pyropia yezoensis Protein Prevents Dexamethasone-Induced Myotube Atrophy in C2C12 Myotubes

by Min-Kyeong Lee, Jeong-Wook Choi, Youn Hee Choi and Taek-Jeong Nam

Mar. Drugs 2018, 16(12), 497; https://doi.org/10.3390/md16120497 - 8 Dec 2018

Cited by 16 | Viewed by 5899

Abstract

Glucocorticoids (GCs), which are endocrine hormones released under stress conditions, can cause skeletal muscle atrophy. This study investigated whether Pyropia yezoensis crude protein (PYCP) inhibits synthetic GCs dexamethasone (DEX)-induced myotube atrophy associated with proteolytic systems. Mouse skeletal muscle C2C12 myotubes were treated with DEX in the presence or absence of PYCP. DEX exposure (100 μM) for 24 h significantly decreased myotube diameter and myogenin expression, which were all increased by treatment with 20 and 40 μg/mL PYCP. Additionally, PYCP significantly reduced the nuclear expression of the forkhead box transcription factors, FoxO1 and FoxO3a, and ubiquitin-proteasome pathway activation. Further mechanistic research revealed that PYCP inhibited the autophagy-lysosome pathway in DEX-induced C2C12 myotubes. These findings indicate that PYCP prevents DEX-induced myotube atrophy through the regulation of FoxO transcription factors, followed by the inhibition of the ubiquitin-proteasome and autophagy-lysosome pathways. Therefore, we suggest that inhibiting these two proteolytic processes with FoxO transcription factors is a promising strategy for preventing DEX-related myotube atrophy. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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20 pages, 9728 KiB

Open AccessArticle

Synthesis and Evaluation of Spumigin Analogues Library with Thrombin Inhibitory Activity

by Aleš Žula, Izabela Będziak, Danijel Kikelj and Janez Ilaš

Mar. Drugs 2018, 16(11), 413; https://doi.org/10.3390/md16110413 - 27 Oct 2018

Cited by 5 | Viewed by 3602

Abstract

Spumigins are marine natural products derived from cyanobacteria Nodularia spumigena, which mimics the structure of the d-Phe-Pro-Arg sequence and is crucial for binding to the active site of serine proteases thrombin and factor Xa. Biological evaluation of spumigins showed that spumigins with a (2S,4S)-4-methylproline central core represent potential lead compounds for the development of a new structural type of direct thrombin inhibitors. Herein, we represent synthesis and thrombin inhibitory activity of a focused library of spumigins analogues with indoline ring or l-proline as a central core. Novel compounds show additional insight into the structure and biological effects of spumigins. The most active analogue was found to be a derivative containing l-proline central core with low micromolar thrombin inhibitory activity. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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16 pages, 3249 KiB

Open AccessArticle

Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

by Fangmiao Yu, Zhuangwei Zhang, Liwang Luo, Junxiang Zhu, Fangfang Huang, Zuisu Yang, Yunping Tang and Guofang Ding

Mar. Drugs 2018, 16(11), 411; https://doi.org/10.3390/md16110411 - 27 Oct 2018

Cited by 45 | Viewed by 4888

Abstract

Marine-derived angiotensin-I converting enzyme (ACE) inhibitory peptides have shown potent ACE inhibitory activity with no side effects. In this study, we reported the discovery of a novel ACE-inhibitory peptide derived from trypsin hydrolysates of Cyclina sinensis (CSH). CSH was separated into four different molecular weight (MW) fractions by ultrafiltration. Fraction CSH-I showed the strongest ACE inhibitory activity. A peptide was purified by fast protein liquid chromatography (FPLC) and reversed-phase high-performance liquid chromatography (RP-HPLC) and its sequence was determined to be Trp-Pro-Met-Gly-Phe (WPMGF, 636.75 Da). The Lineweaver-Burk plot showed that WPMGF was a competitive inhibitor of ACE. WPMGF showed a significant degree of stability at varying temperatures, pH, and simulated gastrointestinal environment conditions. We investigated the interaction between this pentapeptide and ACE by means of a flexible molecular docking tool. The results revealed that effective interaction between WPMGF and ACE occurred mainly through hydrogen bonding, hydrophobic interactions, and coordination bonds between WPMGF and Zn(II). In conclusion, our study indicates that a purified extract derived from Cyclina sinensis or the WPMGF peptide could potentially be incorporated in antihypertensive functional foods or dietary supplements. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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21 pages, 3901 KiB

Open AccessArticle

Pyropia yezoensis Protein Supplementation Prevents Dexamethasone-Induced Muscle Atrophy in C57BL/6 Mice

by Min-Kyeong Lee, Jeong-Wook Choi, Youn Hee Choi and Taek-Jeong Nam

Mar. Drugs 2018, 16(9), 328; https://doi.org/10.3390/md16090328 - 11 Sep 2018

Cited by 7 | Viewed by 5846

Abstract

We investigated the protective effects of Pyropia yezoensis crude protein (PYCP) against dexamethasone (DEX)-induced myotube atrophy and its underlying mechanisms. DEX (3 mg/kg body weight, intraperitoneal injection) and PYCP (150 and 300 mg/kg body weight, oral) were administrated to mice for 18 days, and the effects of PYCP on DEX-induced muscle atrophy were evaluated. Body weight, calf thickness, and gastrocnemius and tibialis anterior muscle weight were significantly decreased by DEX administration (p < 0.05), while PYCP supplementation effectively prevented the DEX-induced decrease in body weight, calf thickness, and muscle weight. PYCP supplementation also attenuated the DEX-induced increase in serum glucose, creatine kinase, and lactate dehydrogenase levels. Additionally, PYCP supplementation reversed DEX-induced muscle atrophy via the regulation of the insulin-like growth factor-I/protein kinase B/rapamycin-sensitive mTOR complex I/forkhead box O signaling pathway. The mechanistic investigation revealed that PYCP inhibited the ubiquitin-proteasome and autophagy-lysosome pathways in DEX-administrated C57BL/6 mice. These findings demonstrated that PYCP increased protein synthesis and decreased protein breakdown to prevent muscle atrophy. Therefore, PYCP supplementation appears to be useful for preventing muscle atrophy. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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11 pages, 1905 KiB

Open AccessArticle

A Novel Peptide, Nicotinyl–Isoleucine–Valine–Histidine (NA–IVH), Promotes Antioxidant Gene Expression and Wound Healing in HaCaT Cells

by Dong Hwee Son, Dong Joo Yang, Ji Su Sun, Seul Ki Kim, Namju Kang, Jung Yun Kang, Yun-Hee Choi, Jeong Hun Lee, Sang Hyun Moh, Dong Min Shin and Ki Woo Kim

Mar. Drugs 2018, 16(8), 262; https://doi.org/10.3390/md16080262 - 1 Aug 2018

Cited by 16 | Viewed by 4660

Abstract

Nicotinamide (NA), a water-soluble vitamin B₃, has been shown to exert cellular-protective effects against reactive oxygen species (ROS). In order to improve the cellular-protective effects of NA, we synthesized a novel compound, nicotinyl–isoleucine–valine–histidine (NA–IVH), by combining NA with jellyfish peptides’ IVH. In the present study, we examined the cellular-protective effects of the novel synthetic nicotinyl-peptide, NA–IVH. We found that NA–IVH enhances the radical scavenging activity with a robust increase of the nuclear factor (erythroid-derived 2)-like factor (Nrf2) expression in human HaCaT keratinocytes. In addition, NA–IVH protected the cells from hydrogen peroxide (H₂O₂)-induced cell death. Interestingly, NA–IVH exhibited an improved wound-healing effect in a high glucose condition, possibly through the regulation of reactive oxygen species (ROS). Collectively, our results imply that a novel nicotinyl-peptide, NA–IVH, has a wound-healing effect in a hyperglycemic condition, possibly by modulating excessive ROS. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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13 pages, 14065 KiB

Open AccessArticle

Intraocular Penetration of a vNAR: In Vivo and In Vitro VEGF₁₆₅ Neutralization

by Tanya A. Camacho-Villegas, María Teresa Mata-González, Walter García-Ubbelohd, Linda Núñez-García, Carolina Elosua, Jorge F. Paniagua-Solis and Alexei F. Licea-Navarro

Mar. Drugs 2018, 16(4), 113; https://doi.org/10.3390/md16040113 - 31 Mar 2018

Cited by 28 | Viewed by 6324

Abstract

Variable new antigen receptor domain (vNAR) antibodies are novel, naturally occurring antibodies that can be isolated from naïve, immune or synthetic shark libraries. These molecules are very interesting to the biotechnology and pharmaceutical industries because of their unique characteristics related to size and tissue penetrability. There have been some approved anti-angiogenic therapies for ophthalmic conditions, not related to vNAR. This includes biologics and chimeric proteins that neutralize vascular endothelial growth factor (VEGF)₁₆₅, which are injected intravitreal, causing discomfort and increasing the possibility of infection. In this paper, we present a vNAR antibody against human recombinant VEGF₁₆₅ (rhVEGF₁₆₅) that was isolated from an immunized Heterodontus francisci shark. A vNAR called V13, neutralizes VEGF₁₆₅ cytokine starting at 75 μg/mL in an in vitro assay based on co-culture of normal human dermal fibroblasts (NHDFs) and green fluorescence protein (GFP)-labeled human umbilical vein endothelial cells (HUVECs) cells. In the oxygen-induced retinopathy model in C57BL/6:Hsd mice, we demonstrate an endothelial cell count decrease. Further, we demonstrate the intraocular penetration after topical administration of 0.1 μg/mL of vNAR V13 by its detection in aqueous humor in New Zealand rabbits with healthy eyes after 3 h of application. These findings demonstrate the potential of topical application of vNAR V13 as a possible new drug candidate for vascular eye diseases. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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18 pages, 4118 KiB

Open AccessArticle

Bioactive Peptides from Cartilage Protein Hydrolysate of Spotless Smoothhound and Their Antioxidant Activity In Vitro

by Jing Tao, Yu-Qin Zhao, Chang-Feng Chi and Bin Wang

Mar. Drugs 2018, 16(4), 100; https://doi.org/10.3390/md16040100 - 22 Mar 2018

Cited by 86 | Viewed by 7254

Abstract

In the experiment, crude proteins from spotless smoothhound (Mustelus griseus), cartilages were isolated by HCl-Guanidine buffer, and its hydrolysate was prepared using trypsin at pH 8.0, 40 °C with a total enzyme dose of 2.5%. Subsequently, three antioxidant peptides were purified from the hydrolysate using membrane ultrafiltration, anion-exchange chromatography, gel filtration chromatography, and reverse phase high-performance liquid chromatography. The amino acid sequences of isolated peptides were identified as Gly-Ala-Glu-Arg-Pro (MCPE-A); Gly-Glu-Arg-Glu-Ala-Asn-Val-Met (MCPE-B); and Ala-Glu-Val-Gly (MCPE-C) with molecular weights of 528.57, 905.00, and 374.40 Da, respectively, using protein amino acid sequence analyzer and mass spectrum. MCPE-A, MCPE-B and MCPE-C exhibited good scavenging activities on 2,2-diphenyl-1-picrylhydrazyl radicals (DPPH•) (EC₅₀ 3.73, 1.87, and 2.30 mg/mL, respectively), hydroxyl radicals (HO•) (EC₅₀ 0.25, 0.34, and 0.06 mg/mL, respectively), 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid radicals (ABTS⁺•) (EC₅₀ 0.10, 0.05, and 0.07 mg/mL, respectively) and superoxide anion radicals (

O_{2}^{-}

•) (EC₅₀ 0.09, 0.33, and 0.18 mg/mL, respectively). MCPE-B showed similar inhibiting ability on lipid peroxidation with butylated hydroxytoluene (BHT) in a linoleic acid model system. Furthermore, MCPE-A, MCPE-B, and MCPE-C could protect H₂O₂-induced HepG2 cells from oxidative stress by decreasing the content of malonaldehyde (MDA) and increasing the levels of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), and glutathione reductase (GSH-Rx). Glu, Gly, Met, and Pro in their sequences and low molecular weight could be attributed to the antioxidant activities of three isolated peptides. These results suggested that GAERP (MCPE-A), GEREANVM (MCPE-B), and AEVG (MCPE-C) from cartilage protein hydrolysate of spotless smoothhound might serve as potential antioxidants and be used in the pharmaceutical and health food industries. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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14 pages, 2439 KiB

Open AccessArticle

Phycoerythrin Peptide from Pyropia yezoensis Alleviates Endoplasmic Reticulum Stress Caused by Perfluorooctane Sulfonate-Induced Calcium Dysregulation

by Jeong Hwan Oh, Eun-Young Kim and Taek-Jeong Nam

Mar. Drugs 2018, 16(2), 44; https://doi.org/10.3390/md16020044 - 26 Jan 2018

Cited by 11 | Viewed by 4002

Abstract

Perfluorooctane sulfonate (PFOS), a stable fluorosurfactant, causes endoplasmic reticulum (ER) stress in the brain. This study was designed to investigate whether a phycoerythrin-derived peptide of Pyropia yezoensis (PYP) reduces PFOS-induced ER stress associated with calcium dysregulation. The protective effects of PYP were determined by cell viability, immunoblotting for ER stress response protein glucose-regulated protein 78 (GRP78) and calcium-dependent protein kinases in rat frontal cortical neurons. PFOS-induced decrease in cell viability was attenuated by PYP pretreatment (1 µg/mL) for 24 h, which was downregulated by inhibiting tropomyosin-receptor kinase B (TrkB). PYP pretreatment downregulated the increase in intracellular calcium levels and phosphorylation of calcium/calmodulin-dependent protein kinase II and c-Jun N-terminal kinase which are associated with a PFOS-induced increase in GRP78. The PFOS-induced increase in GRP78 was downregulated via activation of TrkB receptor-linked extracellular signal-regulated kinases 1/2 (ERK1/2) by PYP pretreatment. Moreover, PYP microinjections (1 µg/kg, 0.54 nmol) attenuated the GRP78 expression in rat prefrontal cortex caused by PFOS (10 mg/kg) exposure for 2 weeks. These findings demonstrate that PYP enhances frontal cortical neuron viability via activation of TrkB receptor-ERK1/2 signaling and attenuation of ER stress in rat prefrontal cortex against PFOS exposure, suggesting that PYP might prevent neuronal dysfunctions caused by PFOS-induced ER stress. Full article

(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)

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