Dataset Information

Kidney therapeutic potential of peptides derived from the bromelain hydrolysis of green peas protein.

ABSTRACT:

Objectives

Kidney disease is a global health problem that needs a solution to its therapy. In the previous study, we found that protein hydrolysate of green peas origin of Indonesia hydrolysed by bromelain (PHGPB) showed improve kidney function in cisplatin-induced nephropathy rats. In this study, we investigated the effect of PHGPB to obtain effective dose that exerts a therapeutic effect on chronic kidney disease (CKD) based on reducing urea and creatinine levels and to elucidate its mechanism of action.

Materials and methods

Two sets of experiments were conducted: (1) characteristics and proteomic profile of PHGPB, (2) in vivo test of PHGPB in gentamycin-induced Wistar rats, including urea and creatinine measurements, activities of antioxidant and kidney-related peptides (ANP, COX-1, and renin).

Results

PHGPB showed three bands under 10 kDa using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and contained 10 identified proteins using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Significant differences in urea and creatinine levels were found between all PHGPB treatments and positive controls (P<0.01). The lowest levels of urea and creatinine that were validated by high super oxide dismutase (SOD) activity and atrial natriuretic peptide (ANP) level were obtained in the 200 mg/day PHGPB treatment. However, the mean renin level was high and cyclooxygenase-1 (COX-1) level did not exceed positive and negative control levels.

Conclusion

PHGPB at dose 200 mg/kgBW shows a potential CKD therapeutic effect that is dose-dependent. Higher PHGPB dose corresponds to better effect on kidney function by increasing antioxidant activity and ANP levels in gentamycin-induced Wistar rats.

SUBMITTER: Hidayat M

PROVIDER: S-EPMC6880536 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Kidney therapeutic potential of peptides derived from the bromelain hydrolysis of green peas protein.

Hidayat Meilinah M Prahastuti Sijani S Riany Destiya Ulfah DU Soemardji Andreanus Andaja AA Suliska Nova N Garmana Afrilia Nuryanti AN Assiddiq Bobby F BF Hasan Khomaini K

Iranian journal of basic medical sciences 20190901 9

<h4>Objectives</h4>Kidney disease is a global health problem that needs a solution to its therapy. In the previous study, we found that protein hydrolysate of green peas origin of Indonesia hydrolysed by bromelain (PHGPB) showed improve kidney function in cisplatin-induced nephropathy rats. In this study, we investigated the effect of PHGPB to obtain effective dose that exerts a therapeutic effect on chronic kidney disease (CKD) based on reducing urea and creatinine levels and to elucidate its m ...[more]

PMID: 31807245

Similar Datasets

Project description:IntroductionThis study investigated the tryptic hydrolysis of β-lactoglobulin (BLG) for 30, 60, 90, and 120 min at 1/200 E/S (enzyme/substrate ratio, w/w) to prepare potentially anticarcinogenic peptides.MethodsThe properties of hydrolysates were characterized, including degree of hydrolysis, free amino acids, SDS-PAGE, FTIR, and antioxidant activity employing DPPH-assay, β-carotene/linoleic acid, and FRAP assay.ResultsBLG tryptic hydrolysate produced after 60 min hydrolysis recorded the highest antioxidant activity, and LCMS analysis revealed 162 peptides of molecular masses ranging from 800 to 5671Da, most of them are of hydrophobic nature. Within the low-MW peptide group (24 peptides), there were nine hydrophobic basic (HB) and seven hydrophobic acidic (HA), representing 38% and 29%, respectively. The HB peptides may be responsible for the considerable biological activity of the hydrolysate. With dominant basic character supporting the carcinogenic activity of this hydrolysate. The in vitro anticancer activity against Mcf-7, Caco-2, and A-549 human cancer cell lines proliferation by MTT assay recorded IC50% at 42.8, 76.92, and 45.93 μg/mL, respectively. Treating each cell line with IC50% of the hydrolysate for 24 h increased the apoptosis by enhancing the expression of caspase-9 by 5.66, 7.97, and 3.28 folds over the untreated control and inhibited angiogenesis by reducing VEGFR-2 expression by about 56, 76, and 70%, respectively, indicating strong anticancer and antiangiogenic actions on human cancer cells. BLG tryptic hydrolysate may serve as a natural anticarcinogenic agent. The results of this study demonstrated that BLG hydrolysates have direct anticancer and antiangiogenic effects on human cancer cells. The chemical composition and characteristics of the BLG tryptic hydrolysate influence these biological and anticancer activities. The tryptic hydrolysates were generally effective against the three cancer cell lines studied (Mcf-7, Caco-2, and A-549). This effectiveness was assessed by measuring cell proliferation using the MTT assay and by evaluating their impact on angiogenesis through inhibition of VEGFR-2 activity.DiscussionFuture studies may focus on enhancing the anticarcinogenic effectiveness of the peptides by isolating and evaluating the most prominent individual peptide and varying the treatment conditions.

Project description:Kidney disease is prevalent in diabetes. Urinary exosomes (uE) from animal models and patients with Diabetic nephropathy (DN) showed increased levels of miRs with reno-protective potential. We examined whether urinary loss of such miRs is associated with their reduced renal levels in DN patients. We also tested whether injecting uE can leverage kidney disease in rats. In this study (study-1) we performed microarray profiling of miRNA in uE and renal tissues in DN patients and subjects with diabetes without DN (controls). In study-2, diabetes was induced in Wistar rats by Streptozotocin (i.p. 50 mg/kg of body weight). Urinary exosomes were collected at 6th, 7th and 8th weeks, and injected back into the rats (100ug/biweekly, uE-treated n=7) via tail vein on weeks 9 and 10. Equal volume of vehicle was injected in controls (vehicle, n=7). uE from the human and rat showed the presence of exosome-specific proteins by immunoblotting. Microarray profiling revealed a set of 15 miRs having high levels in the uE, while lower in renal biopsies, from DN, compared to controls (n=5-9/group). Bioinformatic analysis also confirmed the Renoprotective potential of these miRs. Taqman qPCR confirmed the opposite regulation of miR-200c-3p and miR-24-3p in paired uE and renal biopsy samples from DN patients (n=15), relative to non-DN controls. A rise in 28 miRs levels, including miR-200c-3p, miR-24-3p, miR-30a-3p and miR-23a-3p were observed in the uE of DN rats, collected between 6th-8th weeks, relative to baseline (before diabetes induction). uE- treated DN rats had significantly reduced urine albumin-to-creatinine ratio, attenuated renal pathology, and lower miR-24-3p target fibrotic/inflammatory genes (TGF-beta, and Collagen IV), relative to vehicle treated DN rats. In uE treated rats, the renal expression of miR-24-3p, miR-30a-3p, let-7a-5p and miR-23a-3p was increased, relative to vehicle control. Patients with diabetic nephropathy had reduced renal levels, while higher uE abundance of miRs with reno-protective potential. Reverting the urinary loss of miRs by injecting uE attenuated renal pathology in diabetic rats.

Project description:BackgroundThe demonstration of chaperone-like activity in peptides (mini-chaperones) derived from α-crystallin's chaperone region has generated significant interest in exploring the therapeutic potential of peptide chaperones in diseases of protein aggregation. Recent studies in experimental animals show that mini-chaperones could reach intended targets and alter the disease phenotype. Although mini-chaperones show potential benefits against protein aggregation diseases, they do tend to form aggregates on storage. There is thus a need to fine-tune peptide chaperones to increase their solubility, pharmacokinetics, and biological efficacy.Scope of reviewThis review summarizes the properties and the potential therapeutic roles of mini-chaperones in protein aggregation diseases and highlights some of the refinements needed to increase the stability and biological efficacy of mini-chaperones while maintaining or enhancing their chaperone-like activity against precipitation of unfolding proteins.Major conclusionsMini-chaperones suppress the aggregation of proteins, block amyloid fibril formation, stabilize mutant proteins, sequester metal ions, and exhibit antiapoptotic properties. Much work must be done to fine-tune mini-chaperones and increase their stability and biological efficacy. Peptide chaperones could have a great therapeutic value in diseases associated with protein aggregation and apoptosis.General significanceAccumulation of misfolded proteins is a primary cause for many age-related diseases, including cataract, macular degeneration, and various neurological diseases. Stabilization of native proteins is a logical therapeutic approach for such diseases. Mini-chaperones, with their inherent antiaggregation and antiapoptotic properties, may represent an effective therapeutic molecule to prevent the cascade of protein conformational disorders. Future studies will further uncover the therapeutic potential of mini-chaperones. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease.

Dataset Information

Kidney therapeutic potential of peptides derived from the bromelain hydrolysis of green peas protein.

Objectives

Materials and methods

Results

Conclusion

Publications

Kidney therapeutic potential of peptides derived from the bromelain hydrolysis of green peas protein.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets