Amino acid sequence of sialic acid binding lectin from frog (Rana catesbeiana) eggs

Titani, Koiti; Takio, Koji; Kuwada, Manabu; Nitta, Kazuo; Sakakibara, Fusao; Kawauchi, Hiroaki; Takayanagi, Giichi; Hakomori, Sen‐itiroh

doi:10.1021/bi00382a018

Cited by 76 publications

(52 citation statements)

References 21 publications

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“…Although it is tempting to consider the possibility of a similar physiologic function for the Rana ribonucleases, this interpretation would be decidedly premature, and it is difficult to envision this sort of role for the proteins that are localized in the oocyte. However, it is worthwhile to note that several of the Rana ribonucleases were initially isolated as carbohydrate-binding proteins (Titani et al 1987;Kamiya et al 1990); we can consider the possibility that these "bifunctional" ribonuclease-lectins function in some way similarly to the combined efforts of the eosinophil-associated ribonucleases and the eosinophil-specific galectin, the CharcotLeyden crystal protein (Leonidas et al 1995;Dyer and Rosenberg 1996).…”

Section: Discussionmentioning

confidence: 99%

“…Several of these sequences were also identified by PCR amplification but not reported in the studies performed by Liao et al (2000). The amino terminal "Q" of these novel sequences has been inferred based on similarity to the amino acid sequence of rc-RNase (rc-RN), whose terminus was determined directly via protein sequencing (Titani et al 1987); the 22 amino acid signal sequences encoded by the full length cDNAs are not shown. Four of the five novel sequences include eight cysteines (Fig.…”

Section: Identification Of Novel Ribonucleasementioning

confidence: 99%

“…Although the cysteine structure and N-terminus of onconase (rp-onc) differ from those of the mammalian ribonucleases, the catalytic histidines and lysine and enzymatic activity are maintained. Three additional proteins identified in oocytes and liver from the bullfrogs Rana catesbeiana (rc-RNase and rc-L1) and Rana japonica (rj-lec from oocytes), were introduced as members of this new group of ribonucleases (Titani et al 1987;Nitta et al 1989;Kamiya et al 1990). Liao et al (Huang et al 1998) were the first to isolate a cDNA encoding a Rana ribonuclease (rc-RNase), and found mRNA expression in the liver rather than in oocytes where the protein is ultimately localized.…”

Section: Introductionmentioning

confidence: 99%

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Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

et al. 2001

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Abstract. We present sequences of five novel RNase A superfamily ribonuclease genes of the bullfrog, Rana catesbeiana. All five genes encode ribonucleases that are similar to Onconase, a cytotoxic ribonuclease isolated from oocytes of R. pipiens. With amino acid sequence data from 14 ribonucleases from three Rana species (R. catesbeiana, R. japonica, and R. pipiens), we have constructed bootstrap-supported phylogenetic trees that reorganize these ribonucleases into five distinct lineagesthe pancreatic ribonucleases (RNases 1), the eosinophilassociated ribonucleases (RNases 2, 3, and 6), the ribonucleases 4, the angiogenins (RNases 5) and the Rana ribonucleases-with the Rana ribonucleases no more closely related to the angiogenins than they are to any of the other ribonuclease lineages shown. Further phylogenetic analysis suggests the division of the Rana ribonucleases into two subclusters (A and B), with positive (Darwinian) selection (d N /d S > 1.0) and an elevated rate of radical nonsynonymous substitution (d R ) contributing to the rapid diversification of ribonucleases within each cluster. This pattern of evolution-rapid diversification via positive selection among sequences of a multigene cluster-bears striking resemblance to what we have described for the eosinophil-associated ribonuclease genes of the rodent Mus musculus, a finding that may have implications with respect the physiologic function of this unique family of proteins.

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Section: Discussionmentioning

confidence: 99%

Section: Identification Of Novel Ribonucleasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

et al. 2001

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“…The anti-proliferative activity of RNase Hel was measured with human leukemia cells (HL-60, Health Science Research Resources Bank, Osaka, Japan) according to the method described by Titani et al 2) and Kobayashi et al…”

Section: Effect Of Rnase He1 On the Proliferation Of Human Leukemia Cmentioning

confidence: 99%

Mutagenesis of the Novel <i>Hericium erinaceus</i> Ribonuclease, RNase He1, Reveals Critical Responsible Residues for Enzyme Stability and Activity

Kobayashi

Motoyoshi

Itagaki

et al. 2014

Biological & Pharmaceutical Bulletin

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Here, we determined the sequence of a cDNA encoding a guanylic acid-specific ribonuclease (RNase He1) from Hericium erinaceus that exhibits high sequence identity (59%) with RNase Po1, an enzyme with anticancer activity and which is found in Pleurotus ostreatus. RNase He1 and RNase Po1 have similar structures and heat stabilities; hence, RNase He1 may also have potential as an anti-cancer agent. Therefore, we initiated structure-function studies to further characterize the enzyme. Based on the RNase Po1 structure, RNase He1 is predicted to form 3 disulfide bonds involving Cys7-Cys98, Cys5-Cys83, and Cys47-Cys81 linkages. The Cys5Ala mutant exhibited no RNase activity, whereas the Cys81Ala mutant retained RNase activity, but had reduced heat stability. Therefore, the Cys5-Cys83 bond in RNase He1 is essential for the structure of the RNase active site region. Similarly, the Cys47-Cys81 bond helps maintain the conformational stability of the active site region, and may contribute to the greater heat stability of RNase He1.

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“…The ; RNase RC, RNase from bullfrog liver 7) ; onconase, RNase from leopard frog oocyte 8) ; jSBL, sialic acid binding lectin from Japanese frog oocyte 9) ; cSBL, sialic acid binding lectin from bullfrog oocyte. 10) Amino acid residues essential for catalysis are denoted by white letters, and half-cystine residues are by white letters on a black background. Figures at the top and bottom of the matrix are RNase A and cSBL numbering, respectively.…”

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confidence: 99%

Effect of Modification of the Carboxyl Groups of the Sialic Acid Binding Lectin from Bullfrog (Rana catesbeiana) Oocyte on Anti-tumor Activity.

Iwama

Ogawa

Sasaki

et al. 2001

Biological & Pharmaceutical Bulletin

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The sialic acid binding lectin from Rana catesbeiana oocyte (cSBL) is known to have anti-tumor activity.2) cSBL is a multifunctional protein which has pyrimidine base specific ribonuclease activity. 3,4) In respect to RNase, cSBL belongs to the RNase A family, and is a very heat stable enzyme. It remained 100% active after heating at 100°C. 3,5) Four RNases belonging to the RNase A family have been isolated from Rana family frogs to date. Their primary structures are shown in Fig. 1. They have anti-tumor activity, except for that from bullfrog liver. 11)They are a simple protein and constituted from 104 to 111 amino acid residues. The anti-tumor activity of one of them, onconase, obtained from Rana pipiens, has been studied in detail, and is on its way to application as an anti-tumor drug, now in phase III clinical trials. 12,13) On the other hand, the anti-tumor activity of cSBL has been reported by Nitta et al.2) Although the mechanism of the anti-tumor activity of cSBL is not fully elucidated to date, the first step of the action was different from that of onconase. That is, the interaction of cSBL with sialoglycoprotein on the surface of tumor cells is thought to be essential for cSBL action. The interaction enhances the internalization of cSBL into the tumor cells. However, in contrast to cSBL, for onconase, the contribution of sialic acid to the action has not been identified to date.Nitta et al. showed that the chemical modification of cSBL with a water-soluble carbodiimide (EDC) in the presence of glycine methylester increased the anti-tumor activity. The The sialic acid binding lectin from bullfrog Rana catesbeiana oocyte (cSBL) is known to have anti-tumor activity. In order to investigate the relationship between the net charge of cSBL and its anti-tumor effect, cSBL was modified with a water-soluble carbodiimide (EDC) in the presence of three kinds of nucleophiles, taurine, glycine methylester and ethylenediamine. cSBL having four carboxyl groups was partially modified (ca. 2 residues). The anti-tumor activity of modified cSBLs was in the order of ethylenediamine-modified cSBLϾglycine methylestermodified cSBLϾtaurine modified cSBLмnative cSBL. The results suggested that anti-tumor activity seems to increase with the increase in positive net charge, possibly enhancing the interaction of cSBL with sialoglycoprotein on the surface of tumor cells. The ribonuclease activity of ethylenediamine-modified cSBL decreased with the progress of the reaction, but the number of internalized molecules in the tumor cell increased. Thus, for antitumor activity, a higher incorporation of cSBL with reasonable RNase activity seems to be more important than total RNase activity.

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Amino acid sequence of sialic acid binding lectin from frog (Rana catesbeiana) eggs

Cited by 76 publications

References 21 publications

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

Mutagenesis of the Novel <i>Hericium erinaceus</i> Ribonuclease, RNase He1, Reveals Critical Responsible Residues for Enzyme Stability and Activity

Effect of Modification of the Carboxyl Groups of the Sialic Acid Binding Lectin from Bullfrog (Rana catesbeiana) Oocyte on Anti-tumor Activity.

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