Acute oral toxicity study on Wistar rats fed microalgal protein hydrolysates from Bellerochea malleus.

Protein hydrolysates and bioactive peptides from various protein sources have demonstrated their effectiveness for the prevention of illness and the improvement of symptoms from several diseases. In particular, the use of microalgae to generate bioactive peptides has received a growing interest because of their potential to be cultivated on non-arable land and high nutritional value. However, scant research is available on the toxicity of peptide-based preparations. The present study aims to evaluate the toxicity of microalgal protein hydrolysates (MPH) from one marine species of microalgae (Bellerochea malleus) to determine the feasibility of their use for functional food applications. Results showed that the oral administration of MPH at three doses (D1, 100 mg kg-1 BW; D2, 400 mg kg-1 BW; and D3, 2000 mg kg-1 BW) to male Wistar rats did not induce any adverse effects or mortality up to13 days of treatment. Data analysis of relative organ weights and biochemical and hematological parameters did not show any significant differences between control and treated groups at the three doses investigated. Data from histopathological observations did not reveal any signs of major toxicity at the doses D1 and D2. However, mild signs of inflammation and necrosis were observed in the kidney of rats fed MPH at D3. All together, these results reveal the overall safety of MPH and provide new evidence for advocating their use for functional food or nutraceutical applications.

The same genetic defect in three Tunisian families with Bernard Soulier syndrome: a probable founder Stop mutation in GPIbß.

GPIbα, GPIbß, and GPIX are three candidate genes for a rare genetic bleeding disorder named Bernard Soulier syndrome (BSS). These genes are unique in the genome and encode for glycoprotein subunits of the GPIb-IX complex. Quantitative or qualitative deficiency in this complex is often associated with BSS. Here, we report the novel variant of BSS in which Ser23 of GPIbß is substituted by a Stop codon causing a premature termination of translation, recently described in one family. This genetic defect is revealed in three unrelated BSS patients. The pedigree was determined for two families (F1 and F2) and revealed the homozygosity of the mutation in the two patients and its heterozygosity in parents. In the third family, the patient DNA was heterozygote with the same Ser23 Stop mutation in addition to two missense heterozygote mutations (Asp 51 Gly) and (Ala 55 to Pro). We studied the effect of the Ser23 Stop mutation on the expression of the complex. Our findings confirm that the identified GPIbß mutation is responsible for the BSS phenotype and hampers the GPIb-IX complex to form on the platelets' surface. Regarding the scarcity of the BSS syndrome, the occurrence of the same mutation in three unrelated families would suggest a BSS founder mutation in Tunisia.