Background: Mucins have vital pathophysiological role in gastrointestinal tract (GIT) of avian and other species. However, despite this very little is known about the types of mucins expressed in quail GIT. Hence in this study we examined the expression pattern of mucins (MUC1, and MUC4) in the GIT of the Iraqi Common Quail (Coturnix Coturnix) and performed the network and structural analysis of all reported types of mucins in various breeds of quails. Materials and methods: This study protocol was approved by the animal ethics research committee of the College of Veterinary Medicine, University of Al-Qadisiyah, Iraq. Fresh samples of small and large intestines were used for histological and gene expression analysis of MUC1, and MUC4. Network and structural analysis of all reported types of mucins in quails was performed using the STRING Database, Chimera software and PrankWeb-Ligand Binding Site Prediction tool. Results: The histological analysis using Alcian blue and PAS stains indicated that most mucins in the intestines of quails were of the acidic mucin type, with minimal prevalence of neutral mucins. The expression of acidic mucins was relatively higher in the duodenum, ileum, caecum, and colon, while the jejunum showed a relatively higher expression of neutral mucins. Gene expression analysis revealed higher expression levels of MUC1 and MUC4 mRNA in the jejunum and colon, with its least expression in the duodenum and ilium. Network analysis indicated predominantly mucin-mucin interactions, with MUC 1, 15, 16 and 24 showing preferential homologous networks while the MUC 2, 4, 5 and 6 showed heterologous networks. Detailed evaluation of intermolecular hydrogen bond formation highlighted the interactions between specific mucin combinations, with certain combinations showing higher affinity, such as MUC5A-MUC6, MUC5A-MUC5B, and MUC5B-MUC6. In contrast, MUC15, MUC16, and MUC24 exhibited limited interactions with other mucin types. Binding site analysis indicated that MUC5B and MUC6 had the most number of binding sites with high probability scores, while MUC2, MUC4, and MUC5A showed lower probability scores despite having more binding sites. In contrast MUC 1, 15, and 16 had very few binding sites (<3 binding sites) all with very low probability scores. Conclusion: The findings of this study provide valuable insights into the composition, expression, network interactions, and binding sites of mucins in the quails, contributing to the understanding of mucin-related processes in gastrointestinal physiology and potential implications for gastrointestinal diseases.
The current study aimed to detect specific types of ADAM proteins in the bovine sperm. Histology study of tissue of male reproduction was involved with testis, head, body, and the tail of the epididymis. Results showed that the testis composed of the parenchyma of testis contained the seminiferous tubules which are surrounded by two layers externally tunica vaginalis and internally tunica albuginea. PAS was positive in the seminiferous tubules of testis and lumen, epithelium of the head, and body of epididymis, Whereas Alcian blue was very low intensity stains with sections and contents of the head, body and tail of the epididymis. Fresh ejaculated bovine sperms were collected and separated from seminal plasma, and proteins of sperm were extracted and run on an electrophoresis gel. Then, the bands of proteins have been stained with coomassie stain, after that, the pieces of proteins were cut and separated from gels and amino acids were extracted after the digestion of proteins, and uploaded to a mass spectrometry machine. Our data was profiled and analysed and detected characterised ADAM proteins included: ADAM1, ADAM2, ADAM3A, ADAM10 and ADAM32, and uncharacterized ADAM proteins included: ADAM1B, ADAM7, ADAM9, ADAM12, ADAM15, ADAM17.
Background and Aim: Angiotensin-converting enzyme 2 (ACE2) is expressed and plays functional and physiological roles in different tissues of the body. This study aimed to distinguish the levels of expression of ACE2 in the lung tissue at different ages of rats. Materials and Methods: In this study, 18 male rats were used and divided into three groups according to age. Real-time quantitative polymerase chain reaction (RT-qPCR) was conducted to determine the levels of the quantification of eosinophil cationic protein mRNA transcript. In addition, tissue specimens of the lung were stained with routine hematoxylin and eosin stains. Results: This study confirmed that RT-qPCR amplification plots of ACE2 gene exhibited clearly expression of the lung tissue of rats in the different groups and there are strong different threshold cycles numbers according to the age at 2 weeks, 2 months, and 6-8 months. Consequently, the expression of ACE2 was completely different between groups depending on the age of the rats. The RT-qPCR results showed that the older animal group (age of 6-8 months) had a significantly higher expression of ACE2 than the other animal groups (ages of 2 weeks and 2 months). In the same way, the second group (age of 2 months) had a significantly higher expression of ACE2 than the first group (age of 2 weeks). This study confirmed that the ACE2 expression is influenced by the age of rats. Conclusion: This study concluded that the expression of the ACE2 receptor of coronavirus disease 2019 would be different according to the age of rats, and this result suggested that expression of ACE2 in lung tissue could determine infection and pathogenesis of COVID-19 during different ages of rats or some individual differences.
This study has been designed to analyse the secreted and soluble proteins in bovine seminal plasma by mass spectrometry. The majority of these proteins are produced by accessory glands, and partially by testis, epididymis, ductus deferens and vas deferens of male reproductive tract. Seminal plasma of bovine was collected freshly and isolated after centrifuged and removed the sperm. Non boiled and boiled seminal plasma lysate were run to identify and detect the total proteins, as well as the individual single member of ADAMs protein is determined. The non-boiled lysate of seminal plasma was displayed diversity of proteins more than boiled sample lysate of seminal plasma. However, boiled and non-boiled seminal plasma have distinguished several types of ADAMs protein which are included: ADAM10, ADAM9, ADAM7, ADAM15 in non-boiled samples, while boiled lysate of bovine seminal plasma was displayed ADAM10, ADAM9, ADAM28, and ADAM22. Our finding concluded that bovine seminal plasma is very rich in different types of soluble, cleaved and shed proteins such ADAMs protein which could potentially have a biological and physiological role in protection and interactions of sperm during motility inside female reproductive tract, as it might support it to fertilise the ovum. This protection might be via immunosuppression behaviour or by block specific receptors in female reproductive tract for enhancing sperm motility, and avoid sperm the singling response of immunity.
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