Preparation of recombinant rat eosinophil-associated ribonuclease-1 and -2 and analysis of their biological activities

Ishihara, Kenji; Asai, Kanako; Nakajima, Masahiro; Mue, Suetsugu; Ohuchi, Kazuo

doi:10.1016/s0925-4439(03)00077-2

Cited by 13 publications

(9 citation statements)

References 43 publications

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“…The bactericidal activity of Ss‐RNases was found to be retained when their ribonucleolytic activity was destroyed, as previously described for other bactericidal RNases, such as human RNase 3 and RNase 7, and chicken RNase A‐2 [11,13,29]. A similar result has been reported for rat eosinophils Ear‐1 and Ear‐2 [30], but in those experiments only about 50% of the ribonucleolytic activity was destroyed, and many details of the experiments were not provided.…”

Section: Discussionsupporting

confidence: 80%

Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon

et al. 2008

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The importance of fish in vertebrate evolution has been better recognized in recent years after the intense work carried out on fish genomics. The recent discovery that fish genomes comprise homologs of ribonucleases, studied before only in tetrapods, and the isolation of ribonucleases from zebrafish have suggested an experimental model for studying fish and vertebrate evolution. Thus, the cDNAs encoding the RNases from the Atlantic salmon were expressed, and the recombinant RNases (Ss-RNase-1 and Ss-RNase-2) were isolated and characterized as both proteins and for their biological activities. Salmon RNases are less active than RNase A in degrading RNA, but are both sensitive to the action of the human cytosolic RNase inhibitor. The two enzymes possess both angiogenic and bactericidal activities. However, catalytically inactivated Ss-RNases do not exert any angiogenic activity, but preserve their full bactericidal activity, which is surprisingly preserved even when the enzyme proteins are fully denatured. Analyses of the conformational stability of the two RNases has revealed that they are as stable as typical RNases of the superfamily, and Ss-RNase-2, the most active as an enzyme, is also the most resistant to thermal and chemical denaturation. The implications of these findings in terms of the evolution of early RNases, in particular of the physiological significance of the angiogenic and bactericidal activities of fish RNases, are analyzed and discussed

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Section: Discussionsupporting

confidence: 80%

Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon

et al. 2008

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“…The pI of RNASE9 is lower than that of any other mammalian RNASEs. A basic pI RAT RNase9 IN EPIDIDYMIS is believed to be important for RNase activity, conferring the affinity of the enzyme to its negatively charged RNA substrate [26][27][28][29]. Therefore, RNase9 may not function as a typical RNase.…”

Section: Discussionmentioning

confidence: 99%

RNase9, an Androgen-Dependent Member of the RNase A Family, Is Specifically Expressed in the Rat Epididymis1

Zhu

Liu

Zhang

et al. 2007

Biology of Reproduction

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Members of the RNase superfamily participate in a diverse array of biological processes, including RNA degradation, antipathogen activities, angiogenesis, and digestion. In the present study, we cloned the rat RNase9 gene by in silico methods and genome walking based on homology to the Macaca mulatta (rhesus monkey) epididymal RNase9. The gene is located on chromosome 15p14, spanning two exons, and is clustered with other members of the RNase A superfamily. It contains 1279 bp and encodes 182 amino acids, including a 24-amino acid signal peptide, and it has unique features known from other RNases. Unlike those other members, the rat RNase9 mRNA was specifically expressed in the epididymis, especially in the caput and corpus, and exhibited an androgen-dependent expression pattern but was downregulated in an epididymitis animal model. The RNASE9 was expressed in a principal cell-specific pattern. Interestingly, most of the principal cells in the caput expressed the RNASE9; however, in the distal caput, the principal cells showed a checkerboard-like pattern of immunoreactivity. We also observed that the RNASE9 was bound on the acrosomal domain of sperm. Its potential roles in sperm maturation are discussed.

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“…Rat EAR-1 and EAR-2 have been shown to inhibit the growth of E. coli and S. aureus at concentrations as low as 0.3 mM. 81 Antiviral activity has also been reported for the EARs. Moreau and colleagues demonstrated that recombinant EAR-2 reduces the infectivity of pneumonia virus of mice (PVM) in cultured respiratory epithelial cells.…”

Section: Eosinophil-associated Ribonucleasesmentioning

confidence: 99%

The mammalian secreted RNases: Mechanisms of action in host defence

et al. 2012

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The mammalian ribonucleaseA family comprises a large group of structurally similar proteins which are secreted by a range of tissues and immune cells. Their physiological role is unclear. It has been suggested that some of these RNases contribute to host defence, notably eosinophil-derived neurotoxin, eosinophil cationic protein, eosinophil-associated RNases, RNase4, angiogenin (RNase5), RNase7, RNase8 and bovine seminal RNase. This review summarises data supporting the involvement of these proteins in host defence, focusing on their antimicrobial, cytotoxic and immunomodulatory activities. The extent to which the data support possible mechanisms of action for these proteins is discussed. This compilation of findings and current hypotheses on the physiological role of these RNases will provide a stimulus for further research and development of ideas on the contribution of the RNases to host defence.

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Preparation of recombinant rat eosinophil-associated ribonuclease-1 and -2 and analysis of their biological activities

Cited by 13 publications

References 43 publications

Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon

Ribonucleases with angiogenic and bactericidal activities from the Atlantic salmon

RNase9, an Androgen-Dependent Member of the RNase A Family, Is Specifically Expressed in the Rat Epididymis1

The mammalian secreted RNases: Mechanisms of action in host defence

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