Identification and characterization of integrin-binding sialoprotein (IBSP) genes in reptile and amphibian

Shintani, Seikou; Kamakura, Naofumi; Kobata, Mitsuhiko; Toyosawa, Satoru; Onishi, Taku; Sato, Akie; Kawasaki, Kazuhiko; Weiss, Kenneth M.; Ooshima, Takashi

doi:10.1016/j.gene.2008.07.035

Cited by 11 publications

(9 citation statements)

References 27 publications

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“…Conversely, in SPP1 and IBSP, an intron was created in the last exon, splitting it into the current exons 6 and 7. In IBSP, the border between exon 6 and 7 might shift to the upstream region by reorganization of the exon-intron boundaries in the amniote lineage after the divergence from amphibians [42]. In chicken IBSP, two exons are absent compared to mammals: an exon at the 5 0 UTR and one exon through the fusion of the two-first exons that encode the signal peptide and N-terminal end of the mature IBSP peptide [43].…”

Section: Four Exons Encode Mepementioning

confidence: 99%

MEPE evolution in mammals reveals regions and residues of prime functional importance

Bardet¹,

Delgado²,

Sire

2009

Cell. Mol. Life Sci.

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In mammals, the matrix extracellular phosphoglycoprotein (MEPE) is known to activate osteogenesis and mineralization via a particular region called dentonin, and to inhibit mineralization via its ASARM (acidic serine-aspartate rich MEPE-associated motif) peptide that also plays a role in phosphatemia regulation. In order to understand MEPE evolution in mammals, and particularly that of its functional regions, we conducted an evolutionary analysis based on the study of selective pressures. Using 37 mammalian sequences we: (1) confirmed the presence of an additional coding exon in most placentals; (2) highlighted several conserved residues and regions that could have important functions; (3) found that dentonin function was recruited in a placental ancestor; and (4) revealed that ASARM function was present earlier, pushing the recruitment of MEPE deep into amniote origins. Our data indicate that MEPE was involved in various functions (bone and eggshell mineralization) prior to acquiring those currently known in placental mammals.

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Section: Four Exons Encode Mepementioning

confidence: 99%

MEPE evolution in mammals reveals regions and residues of prime functional importance

Bardet¹,

Delgado²,

Sire

2009

Cell. Mol. Life Sci.

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“…These proteins also contain integrinbinding RGD (Arginine-Glycine-Aspartate) sequences and highly acidic regions composed of (depending on the protein) poly-glutamate or poly-aspartate sequences. In BSP, the poly-glutamate sequences, which are highly conserved [16,17], are critical for hydroxyapatite (HA) nucleation activity based on in vitro studies [18]. The RGD sequence of BSP mediates cell attachment [19,20] but also has been demonstrated to promote osteoblastic cell differentiation and mineralization in vitro through cellular signaling pathways involving focal adhesion kinase and extracellular signal-regulated kinases [21].…”

Section: Introductionmentioning

confidence: 99%

Loss of bone sialoprotein leads to impaired endochondral bone development and mineralization

Holm

Aubin

Hunter

et al. 2015

Bone

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“…In a series of earlier studies on the evolution of molecules, we identified and characterized a number of orthologs in X. laevis involved in the formation of hard tissues (Toyosawa et al, '98;Shintani et al, 2003Shintani et al, , 2007Shintani et al, , 2008. X. laevis was chosen as it is commonly used for studies of developmental biology and genetics.…”

Section: Discussionmentioning

confidence: 99%

“…The DMP1 gene has been cloned and sequenced from tetrapods, including rat (George et al, ), mouse (MacDougall et al, ), cow (Hirst et al, ), human (Hirst et al, ), non‐eutherian mammals (Toyosawa et al, ), chicken (Toyosawa et al, ), crocodile (Toyosawa et al, ), and African clawed frog ( Xenopus tropicalis ; X. tropicalis ) (Kawasaki, ). Evolutionary analysis of the putative DMP1 amino acid sequences among amniotes suggested that the DMP1 gene evolved rapidly in comparison with other SIBLING genes such as IBSP (Shintani et al, ), and that it tolerates nonframe‐shifting insertion/deletions throughout the coding sequence. This suggests that the substitution rate at the DMP1 locus is very high, and that a higher number of non‐synonymous substitutions of amino acid residues have occurred than in other functional proteins (Toyosawa et al, ).…”

mentioning

confidence: 99%

Identification, characterization, and expression of dentin matrix protein 1 gene in Xenopus laevis

et al. 2013

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Dentin matrix protein 1 (DMP1) is an acidic extracellular matrix protein expressed mainly in bone and dentin, and is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family. The DMP1 gene, however, appears to evolve rapidly in comparison with other SIBLING genes, even though such functionally important molecules usually evolve more slowly than less important ones. The purpose of this study was to identify and characterize an ortholog of the DMP1 gene in an amphibian (Xenopus laevis; X. laevis) to clarify molecular evolutionary alterations in DMP1 associated with calcified tissues in tetrapods. Furthermore, we analyzed the mRNA expression of this gene to elucidate its functional change in bone and developing tooth germ in comparison with amniote DMP1s. The similarities of the deduced amino acid sequence of X. laevis DMP1 to that of the corresponding amniote proteins were low, although they did share several unique features specific to DMP1 and have similar properties. Expression of X. laevis DMP1 mRNA was predominant in osteocytes and odontoblasts, but only transiently observed in ameloblasts, as in amniotes. These results suggest that DMP1 has conserved several functions during tetrapod evolution. This indicates that continuity of biochemical properties has been more important in maintaining DMP1 functionality than that of the sequence of amino acid residues, which has undergone change over the course of molecular evolution.

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Identification and characterization of integrin-binding sialoprotein (IBSP) genes in reptile and amphibian

Cited by 11 publications

References 27 publications

MEPE evolution in mammals reveals regions and residues of prime functional importance

MEPE evolution in mammals reveals regions and residues of prime functional importance

Loss of bone sialoprotein leads to impaired endochondral bone development and mineralization

Identification, characterization, and expression of dentin matrix protein 1 gene in Xenopus laevis

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