Cathepsin L gene organization in crustaceans

Macrobrachium rosenbergii mannose binding lectin: Synthesis of MrMBL-N20 and MrMBL-C16 peptides and their antimicrobial characterization, bioinformatics and relative gene expression analysis

“…Hoess et al [57], Le Boulay et al [58] and Rao and Yang [59] stated that the signal sequence in crustaceans is largely involved in secretary process that carries mature proteins outside the cell. It is interesting to note that, some MBL from vertebrates and invertebrates either have a short signal sequence or none [60e62].…”

Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata

“…The active Cys site of CpCL gene was also located in exon 4, but His and Asn sites were found in exon 6. The genomic organization of cathepsin L from Metapenaeus ensis [18], Neobenedenia melleni [16], Caenorhabditis elegans [39], Dictyocaulus viviparous [40], and Penaeus vannamei [41] were consisted of 0,3, 13, 9, and 5 introns, respectively. The gene structure of cathepsin L and the location of the active Cys, His and Asn sites in the gene were distinguishing among various organisms.…”

Aspartic Cathepsin D Endopeptidase Contributes to Extracellular Digestion in Clawed Lobsters Homarus americanus and Homarus gammarus

“…In the digestive tract of decapods, serine proteinases, such as trypsin and chymotrypsin (Galgani et al 1985;Hernández-Cortés et al 1999;Hernández-Cortés et al 1997); cysteine proteinases, such as cathepsin L and cathepsin B (Aoki et al 2004;Le Boulay et al 1998;Teschke and Saborowski 2005); and metallo-proteinses, such as astacin (Titani et al 1987;Zwilling and Stöcker 1997) were studied most intensively, while aspartic proteinases remained unnoticed. In clawed lobsters (Homaridae), digestive proteolytic enzymes have been reported since the early 1970s (Brockerhoff et al 1970;Hoyle 1973), and, unlike other decapods, these proteinases show highest activity at acid pH (Baker and Gibson 1977;Glass and Stark 1994).…”