Search Results (3)

The second stomach compartment (C2) of the dromedary camel (Camelus dromedarius) plays an important role in digestion. However, detailed morphological and histochemical data remain limited. This study aimed to investigate the gross anatomy, histological organization, histometric features, and histochemical distribution of muco-substances in C2. The study was conducted on twenty dromedary camels, including fetuses and adults. Gross anatomical observations were performed on eight fresh and fixed specimens, while histological, histometric, and histochemical analyses were carried out on samples from twelve adult camels using routine and special staining techniques to identify neutral and acidic mucins. C2 was the smallest gastric compartment, located on the right side of the abdominal cavity and partially continuous with C1. Its mucosa formed chambered zones supported by prominent longitudinal muscular bands. Histologically, C2 comprised glandular and non-glandular regions. The glandular mucosa contained gastric pits and branched tubular glands with mucous, chief, and parietal cells, whereas the non-glandular region was lined by keratinized stratified squamous epithelium. Submucosal lymphoid aggregations were observed near the C2–C3 junction. Histometric analysis revealed a markedly developed tunica muscularis. Strong PAS and Alcian blue reactions indicated abundant neutral and acidic mucins. These findings demonstrate that C2 is a structurally specialized compartment supporting digestion, mucosal immune defense, and adaptation to arid environments, clearly distinguishing it from the reticulum of true ruminants. Full article

This study aims to reveal the synergistic degradation and conversion of lignocellulose by spatially distributed gastric microorganisms, facilitating efficient anaerobic fermentation of plant biomass. Contents from camel stomach compartments, feces, and plant biomass were collected for analyses of total carbon, total nitrogen, lignocellulose, FTIR, and XRD. Portions were cultured in vitro to measure gaseous products, organic acids, and ammonia nitrogen, combined with high-throughput sequencing for microbial community analysis. The results indicate a compartment-specific degradation pattern of protein, cellulose, hemicellulose, and lignin across stomach compartments, driven by distinct pH environments: cellulose in the rumen (pH 7.71), hemicellulose and protein in the reticulum (pH 7.78), and lignin in the abomasum (pH 3.72). Synergistic interactions among key degraders in the reticulum, including Rikenellaceae_RC9_gut_group (15.9%), Cyllamyces (5.1%), Prevotella (7.4%), and Methanobrevibacter (39.6%), enhanced production of reducing sugars, organic acids, and ammonia nitrogen, with CO₂, CH₄, and NH₃ yields being 1.3, 3.1, and 2.0 times those in the rumen. These findings reveal an efficient sequential bioconversion system, highlighting the reticulum as a key region with a stable microbial network, and offer a biomimetic basis for expanding enzyme resources and designing staged anaerobic bioreactors, thereby contributing to sustainable bioenergy development and conversion of lignocellulosic resources. Full article

Acid lipase belongs to a family of enzymes that is mainly present in lysosomes of different organs and the stomach. It is characterized by its capacity to withstand acidic conditions while maintaining high lipolytic activity. We cloned for the first time the full coding sequence of camel’s lysosomal acid lipase, cLIPA using RT-PCR technique (Genbank accession numbers JF803951 and AEG75815, for the nucleotide and aminoacid sequences respectively). The cDNA sequencing revealed an open reading frame of 1,197 nucleotides that encodes a protein of 399 aminoacids which was similar to that from other related mammalian species. Bioinformatic analysis was used to determine the aminoacid sequence, 3D structure and phylogeny of cLIPA. Bioinformatics analysis suggested the molecular weight of the translated protein to be 45.57 kDa, which could be decreased to 43.16 kDa after the removal of a signal peptide comprising the first 21 aminoacids. The deduced cLIPA sequences exhibited high identity with Equus caballus (86%), Numascus leucogenys (85%), Homo sapiens (84%), Sus scrofa (84%), Bos taurus (82%) and Ovis aries (81%). cLIPA shows high aminoacid sequence identity with human and dog-gastric lipases (58%, and 59% respectively) which makes it relevant to build a 3D structure model for cLIPA. The comparison confirms the presence of the catalytic triad and the oxyanion hole in cLIPA. Phylogenetic analysis revealed that camel cLIPA is grouped with monkey, human, pig, cow and goat. The level of expression of cLIPA in five camel tissues was examined using Real Time-PCR. The highest level of cLIPA transcript was found in the camel testis (162%), followed by spleen (129%), liver (100%), kidney (20.5%) and lung (17.4%). Full article