Coagulation Factor VIIa

Morrissey, James H.

doi:10.1016/b978-0-12-382219-2.00641-4

Cited by 2 publications

(2 citation statements)

References 91 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The release of proteases into skin may act directly on a pathogen (they can kill bacteria by cleaving their proteins) or may prevent pathogen invasion indirectly by modifying mucus consistency to increase the sloughing of mucus and thereby the removal of pathogens from the body surfaces [142]. Proteases also activate and enhance the production of other innate immune components present in fish mucus such as complement, immunoglobulins, or antibacterial peptides [132,140,143].…”

Section: Proteasesmentioning

confidence: 99%

An Overview of the Immunological Defenses in Fish Skin

2012

View full text Add to dashboard Cite

The vertebrate immune system is comprised of numerous distinct and interdependent components. Every component has its own inherent protective value, and the final combination of them is likely to be related to an animal's immunological history and evolutionary development. Vertebrate immune system consists of both systemic and mucosal immune compartments, but it is the mucosal immune system which protects the body from the first encounter of pathogens. According to anatomical location, the mucosa-associated lymphoid tissue, in teleost fish is subdivided into gut-, skin-, and gill-associated lymphoid tissue and most available studies focus on gut. The purpose of this paper is to summarise the current knowledge of the immunological defences present in skin mucosa as a very important part of the fish immune system, serving as an anatomical and physiological barrier against external hazards. Interest in defence mechanism of fish arises from a need to develop health management tools to support a growing finfish aquaculture industry, while at the same time addressing questions concerning origins and evolution of immunity in vertebrates. Increased knowledge of fish mucosal immune system will facilitate the development of novel vaccination strategies in fish.

show abstract

Section: Proteasesmentioning

confidence: 99%

An Overview of the Immunological Defenses in Fish Skin

2012

View full text Add to dashboard Cite

show abstract

“…The PA domain is an inserted domain in the peptidase S8 domain, which has been shown to play a role in collagen binding in some S8 proteases [27,32]. FN3 domain has been found in several proteases [33,34], whose function in proteases, however, has not been revealed. DUF11 domain is also present in peptidase brachyurin-T of the S1 family from Caldilinea aerophile based on InterProScan prediction (Figure 1).…”

Section: Aa2_1884 Is a Novel Multimodular Peptidase Of The S8 Familymentioning

confidence: 99%

A Novel Gelatinase from Marine Flocculibacter collagenilyticus SM1988: Characterization and Potential Application in Collagen Oligopeptide-Rich Hydrolysate Preparation

Cheng

Teng

et al. 2022

Marine Drugs

View full text Add to dashboard Cite

Although the S8 family in the MEROPS database contains many peptidases, only a few S8 peptidases have been applied in the preparation of bioactive oligopeptides. Bovine bone collagen is a good source for preparing collagen oligopeptides, but has been so far rarely applied in collagen peptide preparation. Here, we characterized a novel S8 gelatinase, Aa2_1884, from marine bacterium Flocculibacter collagenilyticus SM1988T, and evaluated its potential application in the preparation of collagen oligopeptides from bovine bone collagen. Aa2_1884 is a multimodular S8 peptidase with a distinct domain architecture from other reported peptidases. The recombinant Aa2_1884 over-expressed in Escherichia coli showed high activity toward gelatin and denatured collagens, but no activity toward natural collagens, indicating that Aa2_1884 is a gelatinase. To evaluate the potential of Aa2_1884 in the preparation of collagen oligopeptides from bovine bone collagen, three enzymatic hydrolysis parameters, hydrolysis temperature, hydrolysis time and enzyme-substrate ratio (E/S), were optimized by single factor experiments, and the optimal hydrolysis conditions were determined to be reaction at 60 ℃ for 3 h with an E/S of 400 U/g. Under these conditions, the hydrolysis efficiency of bovine bone collagen by Aa2_1884 reached 95.3%. The resultant hydrolysate contained 97.8% peptides, in which peptides with a molecular weight lower than 1000 Da and 500 Da accounted for 55.1% and 39.5%, respectively, indicating that the hydrolysate was rich in oligopeptides. These results indicate that Aa2_1884 likely has a promising potential application in the preparation of collagen oligopeptide-rich hydrolysate from bovine bone collagen, which may provide a feasible way for the high-value utilization of bovine bone collagen.

show abstract

Coagulation Factor VIIa

Cited by 2 publications

References 91 publications

An Overview of the Immunological Defenses in Fish Skin

An Overview of the Immunological Defenses in Fish Skin

A Novel Gelatinase from Marine Flocculibacter collagenilyticus SM1988: Characterization and Potential Application in Collagen Oligopeptide-Rich Hydrolysate Preparation

Contact Info

Product

Resources

About