An immune responsive complement factor D/adipsin and kallikrein-like serine protease (PoDAK) from the olive flounder Paralichthys olivaceus

Kong, Hee Jeong; Hong, Gyeong-Eun; Nam, Bo‐Hye; Kim, Young‐Ok; Kim, Woo Jin; Lee, Sang-Jun; Lee, Nam-Sil; Wan, Jeong; Cho, Hyun Kook; Cheong, JaeHun; Lee, Chang Hoon; Kim, Kyung-Kil

doi:10.1016/j.fsi.2009.06.022

Cited by 13 publications

(8 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The reconstructed phylogenetic tree in Figure S2 also demonstrates that the two piscine peptide sequences previously described as KLK-related [44] are totally unrelated to KLKs. Instead these proteins cluster with the known complement factor D/adipsin proteins [45], [46] (Figure S2).…”

Section: Resultsmentioning

confidence: 79%

Evolutionary History of Tissue Kallikreins

et al. 2010

View full text Add to dashboard Cite

The gene family of human kallikrein-related peptidases (KLKs) encodes proteins with diverse and pleiotropic functions in normal physiology as well as in disease states. Currently, the most widely known KLK is KLK3 or prostate-specific antigen (PSA) that has applications in clinical diagnosis and monitoring of prostate cancer. The KLK gene family encompasses the largest contiguous cluster of serine proteases in humans which is not interrupted by non-KLK genes. This exceptional and unique characteristic of KLKs makes them ideal for evolutionary studies aiming to infer the direction and timing of gene duplication events. Previous studies on the evolution of KLKs were restricted to mammals and the emergence of KLKs was suggested about 150 million years ago (mya). In order to elucidate the evolutionary history of KLKs, we performed comprehensive phylogenetic analyses of KLK homologous proteins in multiple genomes including those that have been completed recently. Interestingly, we were able to identify novel reptilian, avian and amphibian KLK members which allowed us to trace the emergence of KLKs 330 mya. We suggest that a series of duplication and mutation events gave rise to the KLK gene family. The prominent feature of the KLK family is that it consists of tandemly and uninterruptedly arrayed genes in all species under investigation. The chromosomal co-localization in a single cluster distinguishes KLKs from trypsin and other trypsin-like proteases which are spread in different genetic loci. All the defining features of the KLKs were further found to be conserved in the novel KLK protein sequences. The study of this unique family will further assist in selecting new model organisms for functional studies of proteolytic pathways involving KLKs.

show abstract

Section: Resultsmentioning

confidence: 79%

Evolutionary History of Tissue Kallikreins

et al. 2010

View full text Add to dashboard Cite

show abstract

“…Tissues were prepared as described previously [26]. After deparaffinization and rehydration, sections (4e5 mm) were washed for 5 min in 100% ethanol at room temperature and pretreated with proteinase K (10 mg/mL) for 30 min at 37 C. Prehybridization and hybridization were performed in DIG Easy Hyb solution (Roche).…”

Section: Localization Of Pobeclin-1 Mrna By In Situ Hybridization (Ish)mentioning

confidence: 99%

Molecular characterization of the autophagy-related gene Beclin-1 from the olive flounder (Paralichthys olivaceus)

Kong

Moon

Nam

et al. 2011

Fish & Shellfish Immunology

Self Cite

View full text Add to dashboard Cite

“…Dfs have been identified in teleost fish, such as Cyprinus carpio [ 30 ], Salvelinus fontinalis [ 31 ], Oncorhynchus mykiss [ 32 ], Paralichthys olivaceus [ 33 ], Ictalurus punctatus [ 34 ], Oryzias latipes [ 35 ], Oplegnathus fasciatus [ 36 ], Megalobrama amblycephala [ 37 ], and Carassius auratus [ 38 ], and structural information and the mRNA expression profiles during pathogen infection were revealed in these studies. Compared to Dfs in mammals, the structure of Dfs in teleost species is highly conserved, with a Tryp_SPc domain, three substrate binding sites, and three catalytic sites [ 25 , 39 ].…”

Section: Introductionmentioning

confidence: 99%

“…It has been reported that the mRNA expression level of Df in various teleost species is significantly changed after pathogen infection. For example, Df transcript levels are significantly increased in the kidney, liver, and spleen of P. olivaceus after viral hemorrhagic septicemia virus (VHSV) infection [ 33 ]. The expression profiles of Df in O. fasciatus show significant upregulation at 6 and 12 h after rock bream iridovirus (RBIV) infection [ 36 ].…”

Section: Introductionmentioning

confidence: 99%

Functional Identification of Complement Factor D and Analysis of Its Expression during GCRV Infection in Grass Carp (Ctenopharyngodon idella)

Ding

Xiao

Qin

et al. 2021

IJMS

View full text Add to dashboard Cite

Complement factor D (Df) is a serine protease well known for activating the alternative pathway (AP) in mammals by promoting the cleavage of complement component 3 (C3), thus becoming involved in innate defense. In teleost fish, however, the functional mechanisms of Df in the AP and against pathogen infection are far from clear. In the present study, we cloned and characterized the Df gene, CiDf, from grass carp (Ctenopharyngodon idella) and analyzed its function in promoting C3 cleavage and expression changes after grass carp reovirus (GCRV) infection. The open reading frame of CiDf was found to be 753 bp, encoding 250 amino acids with a molecular mass of 27.06 kDa. CiDf harbors a conserved Tryp_SPc domain, with three conserved residues representing the catalytic triad and three conserved binding sites in the substrate specificity pocket. Pairwise alignment showed that CiDf shares the highest identity (96%) and similarity (98%) with Df from Anabarilius grahami. Phylogenetic analysis indicated that CiDf and other fish Dfs formed a distinct evolutionary branch. Similar to most Dfs from other vertebrates, the CiDf gene structure is characterized by four introns and five exons. The incubation of recombinant CiDf protein with grass carp serum significantly increased the C3b content, demonstrating the conserved function of CiDf in the AP in promoting C3 cleavage, similar to Dfs in mammals. CiDf mRNA expression was widely detected in various tissues and levels were relatively higher in the liver, spleen, and intestine of grass carp. During GCRV infection over a 168-hour period, a high level of CiDf mRNA expression in the liver, spleen, and intestine was maintained at 144 and 168 h, suggesting AP activity at the late stage of GCRV infection. Collectively, the above results reveal the conserved structure and function of CiDf and its distinct expression patterns after GCRV infection, which provide a key basis for studying the roles of Df and AP during GCRV infection in the grass carp C. idella.

show abstract

An immune responsive complement factor D/adipsin and kallikrein-like serine protease (PoDAK) from the olive flounder Paralichthys olivaceus

Cited by 13 publications

References 38 publications

Evolutionary History of Tissue Kallikreins

Evolutionary History of Tissue Kallikreins

Molecular characterization of the autophagy-related gene Beclin-1 from the olive flounder (Paralichthys olivaceus)

Functional Identification of Complement Factor D and Analysis of Its Expression during GCRV Infection in Grass Carp (Ctenopharyngodon idella)

Contact Info

Product

Resources

About