Long-Term Dietary Fish Meal Substitution with the Black Soldier Fly Larval Meal Modifies the Caecal Microbiota and Microbial Pathway in Laying Hens.

Feeding laying hens with black soldier fly larval (BSFL) meal improves their performance. However, the beneficial mechanism of BSFL meals in improving the performance of laying hens remains unclear. This study investigated the effects of the BSFL diet on liver metabolism, gut physiology, and gut microbiota in laying hens.

Egg quality and laying performance of Julia laying hens fed with black soldier fly (Hermetia illucens) larvae meal as a long-term substitute for fish meal.

The use of insects in animal feed appears to be an efficient approach that contributes to solving the environmental issues related to leftover disposal; however, it has not been approved in some countries due to concerns about pathogenic infections. This study aimed to evaluate the feasibility of long-term substitution of fish meal in poultry feed with organic defatted black soldier fly larvae (BSFL) meal prepared from BSFL raised on leftovers. The 87 Julia laying hens (178-day-old) were allotted in a completely randomized design with three treatments (29 layers in each treatment).

Evaluation of Black Soldier Fly () Larvae and Pre-Pupae Raised on Household Organic Waste, as Potential Ingredients for Poultry Feed.

Black soldier fly (BSF) larvae and pre-pupae could be satisfactorily raised on household organic waste and used as poultry feed, offering a potential sustainable way to recycle untapped resources of waste. The present study was conducted to determine if whole (non-defatted) BSF larvae and pre-pupae raised on experimental household waste could substitute soybean meal and oil as ingredients for laying hen diets. While no significant differences in feed intake and the egg-laying rate of hens were observed throughout the experiment, egg weight and eggshell thickness were greater in the pre-pupae-fed group than in the other groups.

The effects of administering lactic acid bacteria sealed in a capsule on the intestinal bacterial flora of cattle.

We examined the effects of encapsulated lactic acid bacteria administrated orally to lactating cattle on the intestinal flora. A dose of 3 X 10¹¹ colony forming unit (cfu) of freeze-dried Lactobacillus coryniformis subsp. torquens (JCM1099) encapsulated in an enteric capsule capable of bypassing the rumen was administered for seven days.

Development of three-layered rumen escapable capsules for cattle.

A new rumen escapable tool is presented for cattle in prospect of developing medical treatment or supplementing trace elements for disease prevention. This tool consists of a three-layered capsule that dissolves in the lower digestive tract, but not in the rumen. The capsule was manufactured by capsule-forming techniques through the use of liquid surface tension.

Excretion rates of indigestible plastic balls of different specific gravities and diameters in dairy cattle.

We used plastic balls to investigate how their specific gravity and diameter affect excretion rate and rumination in dairy cattle, to develop a capsule that can be used for reaching the lower gastrointestinal tract without physical breakdown and/or degradation in the rumen. Twelve types of indigestible plastic balls composed of a combination of four specific gravities (0.95, 1.

Granzyme A and thrombin differentially promote the release of interleukin-8 from alveolar epithelial A549 cells.

Some of extracellular serine proteases with trypsin-like specificity of cleavage have been known to increase the release of inflammatory mediators from various cell types. For instance, two well-known trypsin-like serine proteases circulating in blood, granzyme A (GrA) and thrombin, have been found to promote interleukin (IL)-8 release from an alveolar epithelial A549 cell line. However, the mechanisms by which the proteases promote IL-8 release from the cells are not fully understood.

Carrageenan inhibits granzyme A-induced detachment of and interleukin-8 release from alveolar epithelial A549 cells.

Granzyme A (GrA) is a lymphocyte serine protease that is believed to enter virus-infected cells and growing tumors and induce apoptosis. We found recently that recombinant rat GrA (rGrA) promotes detachment of and interleukin (IL)-8 release from alveolar epithelial A549 cells and suggested that this protease is involved in the pathogenesis of certain inflammatory lung diseases. In the present study, we found that lambda-carrageenan (a sulfated oligosaccharide constituting the cell walls of seaweeds) potently inhibits rGrA-induced detachment and IL-8 release of A549 cells.

A lymphocyte serine protease granzyme A causes detachment of a small-intestinal epithelial cell line (IEC-6).

Granzyme A (GzmA) is a serine protease (trypsin-like specificity) produced in cytotoxic lymphocytes. This enzyme is believed to enter virus-infected cells and growing tumors and induce apoptosis, but the roles of GzmA expressed in lymphocytes scattered through the epithelial layer of the normal small intestine are unknown. In the present study, recombinant rat GzmA (rGzmA) was found to cause morphological changes and detachment of a non-transformed rat small-intestinal epithelial cell line IEC-6, although the rGzmA-treated cells detached as aggregates with no changes characteristic of apoptosis.

Granzyme A causes detachment of alveolar epithelial A549 cells accompanied by promotion of interleukin-8 release.

Granzyme A (GrA) is a serine protease produced in cytotoxic lymphocytes, lung epithelial cells (alveolar type-II cells), and alveolar macrophages. In the present study, recombinant rat GrA (rGrA) was found to cause rounding and detachment of an alveolar type-II epithelial cell line, A549. Also, rGrA stimulated release of a neutrophil chemoattractant, interleukin-8, from the cells, via a mechanism involving microtubule disruption, probably resulting from reduction of cell adhesion to culture dishes.

A role of a lymphocyte tryptase, granzyme A, in experimental ulcerative colitis.

In the large-intestinal mucosae of rats orally administered dextran sulfate sodium, which induces an enteritis resembling ulcerative colitis (UC), the activity for granzyme A, a lymphocyte tryptase, increased at an earlier stage than that at which UC markers (growth-regulated gene product/cytokine-induced neutrophil chemoattractant-1 and caspase-3) increased. This suggests involvement of the enzyme in the exacerbation and perpetuation of enteritis.

Sulfated polysaccharides derived from dietary seaweeds increase the esterase activity of a lymphocyte tryptase, granzyme A.

Intake of sulfated polysaccharides, such as fucoidan or lambda-carrageenan extracted from seaweeds, has been shown to enhance immune responses, resulting in inhibition of tumor growth. However, little is known about the mechanisms by which these sulfated compounds mediate the enhancement. In the present study, we examined the effect of sulfated polysaccharides from seaweeds on esterase activity of a lymphocyte tryptase, granzyme A (GzmA), which is believed to induce the production of cytokines in a variety of cells.

Evidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytes.

MT-SP1 (membrane-type serine protease 1)/matriptase is an epithelial-derived integral membrane enzyme. The purpose of the present study was to examine whether the enzyme exists on the basolateral side of simple columnar epithelial cells, such as enterocytes, of normal adult animals. Using COS-1 monkey kidney cells transiently transfected with rat MT-SP1/matriptase expression plasmids, we found that the enzyme is post-translationally processed by the cleavage between Gly149 and Ser150, that a portion of the C-terminal part (Ser150-Val855) remains in the cells by association with the NTF (N-terminal fragment) (Met1-Gly149), while the other portions are released into the medium and that the release is increased on activation by co-expression with hepatocyte growth factor activator inhibitor type-1.

Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: a novel role of the inhibitor as an anti-granzyme A.

Pancreatic secretory trypsin inhibitor (PSTI) is a potent trypsin inhibitor that is mainly found in pancreatic juice. PSTI has been shown to bind specifically to a protein, distinct from trypsin, on the surface of dispersed cells obtained from tissues such as small intestine. In the present study, we affinity-purified the binding protein from the 2% (w/v) Triton X-100-soluble fraction of dispersed rat small-intestinal cells using recombinant rat PSTI.