Characterization of crustin antimicrobial proteins from Japanese spiny lobster Panulirus japonicus

Pisuttharachai, Duangjai; Fagutao, Fernand F.; Yasuike, Motoshige; Aono, Hiroyuki; Yano, Yutaka; Murakami, Keisuke; Kondo, Hidehiro; Aoki, Takashi; Hirono, Ikuo

doi:10.1016/j.dci.2009.05.006

Cited by 34 publications

(14 citation statements)

References 26 publications

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“…Production of AMPs can guarantee the innate immunity resistance against different pathogens. AMPs are majorly small cationic molecules and they are very favorable since their synthesis can be done with low metabolic cost and they have the capability to diffuse rapidly to the point of infection (Pisuttharachai et al, 2009). AMPs have a very wide scope in terms of their physiological roles, many of which are still to be determined.…”

Section: Antimicrobial Effectmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

131

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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Section: Antimicrobial Effectmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

131

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“…Likewise, another Type I crustin gene (designated DW176897) is expressed in regenerating limbs of the fiddler crab, Celuca pugilator (Durica et al, 2006). It is also noteworthy that transcripts of three crustin isoform genes have been identified in the heart, intestine, haemocytes, gills and hepatopancreas of planktonic phyllosoma (larval) stages of Panulirus japonicus, with a fourth isoform detected in nerves (Pisuttharachai et al, 2009). Interestingly, in humans, a gene, encoding a WFDSC-domain containing protein, namely WFDSC-2 (also known as human epididymis protein, HE4), is overexpressed in cancerous ovarian tissue (Hellström et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Unusual tissue distribution of carcinin, an antibacterial crustin, in the crab, Carcinus maenas, reveals its multi-functionality

Suleiman

Smith

Dyrynda

2017

Developmental & Comparative Immunology

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Crustins are whey acidic four-disulphide core (WFDSC) domain-containing proteins in decapods that are widely regarded as antimicrobial agents that contribute to host defence. Whilst there have been many analyses of crustin gene expression in tissues, few studies have been made of the distribution of the natural proteins. Here we report an immunostaining investigation of carcinin, a native crustin from Carcinus maenas, in the body organs. The results show that the protein is largely confined to the haemocytes with only a weak signal detected in the heart, hepatopancreas and midgut caecum where it is restricted to the outer surfaces. Importantly, carcinin was seen to be deposited by the haemocytes on these surfaces. Higher levels of staining were detected in the gonads with carcinin particularly abundant in the capsule of ovary as well as some oocytes. Conspicuous staining was further evident in the cuticle of the eyestalk peduncles. Ablation of the eyestalks resulted in a reduction of carcinin in the maturing ovary with the mature eggs rarely displaying a strong signal for the protein. Interestingly, the degree of carcinin also strongly increased in the healing peduncle, indicating that the protein may be associated with wounding, cell damage and/or tissue regeneration.

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“…Type II crustins have two flanked domains: one is cysteine-rich and similar to that of the Type I crustins and the other is a 50-60 residue glycinerich domain with a high representation of repeat VGGGLF motifs ( Figure 2) [17]. They are present in shrimp but are not confined to these decapods as similar proteins occur also in crayfish Pascifastacus leniusculus [18] and spiny lobster Panulirus japonicus [19]. A third group of crustins are the Type IIIs.…”

Section: Crustinsmentioning

confidence: 99%

“…These are named DWD proteins, but can be tentatively considered to be Type IV crustins, at least until additional information is forthcoming. The different crustin types are not mutually exclusive, as more than one crustin type may be co-expressed in a single species [18,19,26].…”

Section: Crustinsmentioning

confidence: 99%

Phylogeny of whey acidic protein (WAP) four-disulfide core proteins and their role in lower vertebrates and invertebrates

Smith

2011

Biochemical Society Transactions

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Proteins containing WAP (whey acidic protein) domains with a characteristic WFDC (WAP four-disulfide core) occur not only in mammals (including marsupials and monotremes) but also in birds, reptiles, amphibians and fish. In addition, they are present in numerous invertebrates, from cnidarians to urochordates. Many of those from non-mammalian groups are poorly understood with respect to function or phylogeny. Those well characterized so far are waprins from snakes, perlwapins from bivalves and crustins from decapod crustaceans. Waprins are venom proteins with a single WAP domain at the C-terminus. They display antimicrobial, rather than proteinase inhibitory, activities. Perlwapins, in contrast, possess three WAP domains at the C-terminus and are expressed in the shell nacre of abalones. They participate in shell formation by inhibiting the growth of calcium crystals in the shell. The crustin group is the largest of all WFDC-containing proteins in invertebrates with the vast majority being highly expressed in the haemocytes. Most have a single WAP domain at the C-terminus. The presence and type of the domains between the signal sequence and the C-terminus WAP domain separate the different crustin types. Most of the Type I and II crustins are antimicrobial towards Gram-positive bacteria, whereas the Type III crustins tend to display protease inhibition. Expression studies show that at least some crustins have other important biological effects, as levels change with physiological stress, wound repair, tissue regeneration or ecdysis. Thus WAP domains are widely distributed and highly conserved, serving in diverse physiological processes (proteinase inhibition, bacterial killing or inhibition of calcium transport).

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Characterization of crustin antimicrobial proteins from Japanese spiny lobster Panulirus japonicus

Cited by 34 publications

References 26 publications

Peptides: Production, bioactivity, functionality, and applications

Peptides: Production, bioactivity, functionality, and applications

Unusual tissue distribution of carcinin, an antibacterial crustin, in the crab, Carcinus maenas, reveals its multi-functionality

Phylogeny of whey acidic protein (WAP) four-disulfide core proteins and their role in lower vertebrates and invertebrates

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