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Structual Comparison of Dermatopontin Amino Acid Sequences

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Structual Comparison of Dermatopontin Amino Acid Sequences Biologia 65/5: 874—879, 2010 Section Zoology DOI: 10.2478/s11756-010-0098-3 Structual comparison of dermatopontin amino acid sequences Takumi Takeuchi Department of Urology, Kanto Rosai Hospital, 1-1 Kizukisumiyoshi Nakahara-ku, 211-8510, Kawasaki, Japan; e-mail: [email protected] Abstract: Dermatopontin is a tyrosine-rich acidic extracellular matrix protein of 22 kD with possible functions in cell- matrix interactions and matrix assembly. Database of GenBank+EMBL+DDBJ sequences from Nucleotide, Gene, and Expressed Sequence Tag (EST) Divisions was searched with a keyword “dermatopontin” or mouse dermatopontin amino acid sequence. In addition to five mammals previously described, five mammalian, two bird, one fish dermatopontin genes were detected in vertebrates. Additionally, a goat EST was also shown as goat dermatopontin missing 5’-end of the coding region. Moreover, a mRNA sequence of rhesus monkey dermatopontin was identified, but the deduced amino acid sequence was terminated abruptly due to a nonsense codon. For three 6–residue repeat regions (D-R-E/Q-W-X-F/Y) that may function as part of a glycosaminoglycan binding site, the first repeat sequence is D-R-Q-W-N-Y in all mammals while Glutamine is substituted for Leucine in birds. The second and the third repeats are conserved in all vertebrates. The N-Y-D sequence, the consensus in many amine oxidases, is conserved in mammals except rodents. Asparagine is substituted for Threonine in birds. The tetrapeptide R-G-A-T sequence possibly recognizing the integrin family is conserved in mammals and birds, but Alanine was substituted for Glutamine in zebrafish resulting in loss of activity. In conclusion, functionally significant amino acid sequences in vertebrate dermatopontins are conserved in mammals, while they are not necessarily identified in birds and fish. The original function of vertebrate dermatopontins may be glycosaminoglycan binding and functions as a ligand for integrin and an amine oxidase may be gained in the process of evolution. Key words: dermatopontin; amino acid; vertebrate; invertebrate Introduction There has been controversy as to whether der- matopontin enhances or suppresses the proliferation of Dermatopontin is a tyrosine-rich acidic extracellular cells and the accumulation of the extracellular matrices. matrix protein of 22 kD with possible functions in Dermatopontin enhanced the growth-inhibitory activ- cell-matrix interactions and matrix assembly (Superti- ity of TGF-beta on mink lung epithelial cells through Furga et al. 1993; Neame et al. 1989; Forbes et al. its interaction with decorin in the microenvironment of 1994). Human dermatopontin has 96% identity to the the extracellular matrix in vivo (Okamoto et al. 1999). bovine sequence and its expression is not limited to Leiomyomas and keloids demonstrated reduced levels of the connective tissue, as Northern blots show specific dermatopontin (Catherino et al. 2004) and microarray mRNAs in cultured fibroblasts, the muscle, heart, pan- analysis showed the down-regulation of dermatopon- creas, and lung (Superti-Furga et al. 1993). The pro- tin in leiomyoma compared with myometrium (Tsib- tein was proved to associate with decorin and a modi- ris et al. 2002). The decreased expression of dermato- fied decorin with carboxymethylated cysteinyl residues, pontin is associated with the pathogenesis of fibrosis but not to assemble to hyaluronate or dermatan sulfate in hypertrophic scar and systemic sclerosis (Kuroda chains (Okamoto et al. 1996). There are reports indi- et al. 1999). Additionally, stably transfected BALB/c cating that dermatopontin is induced with the stimula- 3T3 cells expressing mouse dermatopontin showed ap- tion of nuclear steroid receptors via their binding sites proximately 50% inhibition of cell proliferation (Tzen in the dermatopontin promoter region. Dermatopontin & Huang 2004). was identified in the uterus of a pregnant mouse and Conversely, dermatopontin knockout mice did not its expression was markedly up-regulated in ovariec- exhibit any obvious anatomical abnormality, but showed tomized uteri following progesterone administration. In a significant decrease in the relative thickness of the silico analysis revealed progesterone receptor binding dermis compared with wild-type mice and 40% lower sites in the dermatopontin promoter region (Kim & skin collagen content, indicating that dermatopontin Cheon 2006). Dermatopontin is also shown to be a plays a critical role in the elasticity of skin and colla- downstream target of Vitamine D receptor in the differ- gen accumulation attributed to collagen fibrillogenesis entiation of multipotential stromal cells into osteoblasts in vivo (Takeda et al. 2002). Corneas of dermatopon- (Pochampally et al. 2007). tin knockout mice showed a 24% reduction in stromal c 2010 Institute of Zoology, Slovak Academy of Sciences Structual comparison of dermatopontin 875 thickness with significant disruption of fibril spacing Table 1. GenBank Accession numbers of dermatopontin nu- within the posterior lamellae (Cooper et al. 2006). The cleotides. infarct zone of experimentally induced myocardial in- Species Accession number farction in rats showed the increased expression of der- matopontin mRNA in macrophages and spindle-shaped Human NM 001937 mesenchymal cells (Takemoto et al. 2002). The overex- Chimpanzee XM 524956 Rhesus monkey XR 011309 pressed proteins identified by a quantitative proteomic Bovine NM 001045903 approach in the chemoresistant ovarian cancer tissue Sheep DY517155 included dermatopontin (Pan et al. 2009). Dog XM 547476 In invertebrates, Biomphalaria glabrata (Say, 1818) Rat NM 001105965 Mouse NM 019759 shell matrix protein of 19.6 kDa, isolated and sequenced Porcine AY610423 as 148 amino acids, showed 32% sequence identity Horse XM 001494376 to mammalian dermatopontin sequences and 34–37% Goat EV436401 identity to invertebrate dermatopontins with the pres- Platypus XM 001514028 Chicken XM 001231675 ence of a single N-glycosylation consensus sequence Zebrafinch XM 002193636 (Marxen et al. 2003) An active cytotoxin of 18 kDa Zebrafish NM 001030085 (MCTx-1), isolated from nematocysts of Millepora sp. Haliotis discus discus EF103386 Aka Island (Fire corals) and lethal in crayfish, was de- Biomphalaria glabrata DQ113395 Limulus polyphemus M96983 duced as a novel dermatopontin (Iguchi et al. 2008). Suberites domuncula AJ299722 We have previously shown that dermatopontin Millepora sp. Aka Island AB299385 mRNA is differentially expressed in hormone-refractory but not in hormone-sensitive mouse mammary cancer (Shionogi-carcinoma) (Takeuchi et al. 2000). We have also reported that transfectants of mouse dermatopon- Results tin cDNA into PC3 human prostate cancer cells en- hanced tumor growth following subcutaneous implan- In addition to five mammals previously summarized tation in nude mice and in mouse dermatopontin trans- (Okamoto & Fujiwara 2006), five mammalian (chim- genic mice under the control of the rat probasin pro- panzee, sheep, dog, horse, platypus), two bird (chicken, moter, the prostatic dorsal lobes showed prostate in- zebrafinch), one fish (zebrafish) dermatopontin genes traepithelial neoplasia (Takeuchi et al. 2006). This may with complete coding regions were detected with a key- suggest that dermatopontin may be involved in the word “dermatopontin” in vertebrates. Additionally, a pathogenesis and growth of the prostate cancer. goat EST was also detected by a homology with amino In a review published in 2006 (Okamoto & Fuji- acid sequence of mouse dermatopontin and shown by wara 2006) it is stated that dermatopontin was identi- a multiple alignment analysis as goat dermatopontin fied in five mammals (bovine, porcine, human, mouse, missing 5’-end of the coding region. Moreover, a mRNA and rat) and 16 invertebrates (horseshoe crab, marine sequence of rhesus monkey dermatopontin was identi- sponges, freshwater snails). With a growing number of fied, but the deduced amino acid sequence seems ter- accumulated DNA and amino acid data, it is meaning- minated abruptly in the midway compared with other ful to delineate now in what species dermatopontin is mammalian dermatopontins due to a nonsense codon actually identified and compare those sequences to as- (TGA). GenBank Accession numbers of vertebrate and sess homology among themselves. invertebrate dermatopontins are listed in Table 1. In invertebrates, dermatopontin genes were de- tected in freshwater snails Biomphalaria glabrata,ma- rine sponges Suberites domuncula (Olivi, 1792), horse- Material and methods shoe crab Limulus polyphemus L., 1758 as summa- rized previously (Okamoto & Fujiwara 2006). There- Database of GenBank+EMBL+DDBJ sequences from Nu- cleotide or Gene Divisions was searched with a keyword after, Iguchi et al. (2008) reported Millepora sp. Aka “dermatopontin” and database of those sequences from EST Island (Fire coral) dertmatopontin and in this study, (expressed sequence tag) Divisions was searched with mouse disc abalone Haliotis discus discus dermatopontin was dermatopontin amino acid sequence using tblastn2.2.21 identified. Multiple alignments of dermatopontin amino program. Translation into an amino acid sequence from acids are shown in Fig. 1 (vertebrates and inverte- a nucleotide sequence was done with the ApE software brates) and Fig. 2 (only invertebrates). Phylogenic tree (http://www.biology.utah.edu/jorgensen/wayned/ape/) created using dermatopontin mRNA sequences is shown when necessary. Multiple amino acid sequence alignments in Fig. 3. Existence of functional amino acid sequences
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