Mammalian Nucleolytic Enzymes

Sierakowska, Halina; Shugar, David

doi:10.1016/s0079-6603(08)60470-5

Cited by 121 publications

(63 citation statements)

References 329 publications

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“…The major human ribonucleases, although part of the ribonuclease superfamily of related proteins, have been grouped into two broad classes [26] usually designated 'secretory' and 'non-secretory'. The former are most abundant in secretory organs and body fluids including pancreas, prostate, seminal fluid, milk, and saliva [27]; they are sometimes classed as 'pancreatic-type enzymes.…”

Section: Resultsmentioning

confidence: 99%

Ribonuclease activity and substrate preference of human eosinophil cationic protein (ECP)

Sorrentino

Glitz

1991

FEBS Letters

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The eosinophil cationic protein (ECP), a potent helminthotoxin with considerable ncurotoxic activity, was recently shown to also have ribonucleolytic activity. In this work the substrate preference of ECP ribonuclcase action was studied in detail. With singe-stranded RNA or synthetic polyribonucleotide substrates ECP showed significant but low activity, 70. to 200-fold less than that of bovine RNase A. ECP hydrolyzed .RNA more rapidly than it did any synthetic polynucleotide. Poly(U) was degraded more rapidly than poly(C), and poly(A) and double-stranded substrates were cxtrcmely resistant. &fined low molecular weight substrates in the form of the 16 dinucleoside phosphates (NpN') and uridine and cytidine 2', 3'-cyclic phosphates were tested, and none showed hydrolysis by ECP at a significant rate. The results link ECP ribonucleolytic activity to the 'non-secretory' liver-type enzymes rather than to the 'secretory' pancreatic-type RNases.

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Section: Resultsmentioning

confidence: 99%

Ribonuclease activity and substrate preference of human eosinophil cationic protein (ECP)

Sorrentino

Glitz

1991

FEBS Letters

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“…(3) noted the sequences similarities between ECP, EDN, and the amino acid sequence of HPR, and suggested that this group comprised a multigene family. HPR belongs to the secretory group of mammalian ribonucleases, which are characterized by alkaline pH optima and immunological crossreactivity (48), and have also been found in kidney, stomach, and saliva (49)(50)(51)(52)(53). This group is immunologically distinct from the neutral, nonsecretory ribonucleases, which have pH optima near 6.5, and have been found in spleen, lung, liver, and leukocytes (49,50,53,54).…”

Section: Resultsmentioning

confidence: 99%

Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.

Rosenberg

Ackerman

Tenen

1989

The Journal of Experimental Medicine

143

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The eosinophil cationic protein (ECP)' is one of several small, distinct argininerich proteins that have been isolated from the eosinophil's large specific granule. The molecular mass of human ECP has been estimated at 18-21 kD (1-3), depending on the degree of glycosylation (3). ECP has been shown to possess a wide variety of biological activities, including the ability to stimulate factor XII-dependent coagulation pathways (4), to neutralize the anticoagulant effects of heparin (5), and to inhibit lymphocyte proliferation induced by PHA or mixed lymphocyte reactions (6) . ECP is a potent cytotoxin; ECP-containing supernatants of activated eosinophils have been shown to be toxic to isolated myocardial cells in vitro (7), and both ECP and the eosinophil granule major basic protein (MBP) were found in the endothelial and endomyocardial lesions characteristic of the hypereosinophilic syndrome (8). Furthermore, ECP is also a potent helminthotoxin; destruction of schistosomula of Schistosoma mansont was reported at concentrations as low as 10' M (8-10-fold more active than MBP) (9, 10) . ECP has also been shown to kill trypomastigote and amastigote stages of Trypanosoma cruzi (11) . Both ECP and the related granule protein, eosinophil-derived neurotoxin (EDN), induce the neurotoxic effect known as the Gordon phenomenon (12)

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“…All six dependences showed individual features of pH dependencies. In contrast to all SLE abzymes, RNases Lupus 58 have only one pH optimum (6.8-7.5) for hydrolysis of poly(A) [104][105][106] (Figure 8D). …”

Section: Polyclonal Dnase and Rnase Abzymesmentioning

confidence: 99%

“…The substrate specificity of SLE IgGs with RNase activity, however, was unique within certain limits for Abs from every individual SLE patient [11]. In contrast to human RNases, SLE IgGs effectively hydrolyze the most resistant poly(A) substrate for all known human RNases [104][105][106][107][108][109]. SLE IgGs demonstrated a very slow hydrolysis of poly(C) [11], which is the best substrate for all mammalian RNases [104][105][106].…”

Section: Polyclonal Dnase and Rnase Abzymesmentioning

confidence: 99%

Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

Nevinsky¹

2017

Lupus

321

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Systemic lupus erythematosus (SLE) is known as a systemic polyethiologic diffuse autoimmune disease characterized by connective tissue disorganization and the paramount damage of skin and visceral capillaries. Usually, SLE symptoms include high fever, hair loss, mouth ulcers, chest pain, swollen lymph nodes, painful and swollen joints, increased fatigue, and appearance of red rash more often on the face. The exact reason of SLE appearance is not really clear. Detection of catalytic Abs (abzymes) was shown to be the earliest indicator of different AI disease development. Some abzymes are cytotoxic and can play a dangerous negative role in the pathogenesis of AI diseases. SLE is characterized by the appearance of abzymes with several different catalytic functions including hydrolysis of peptides and proteins, DNA, RNA, and oligosaccharides. In addition, monoclonal SLE abzymes are characterized by extraordinary diversity in the affinity to the substrates, physicochemical and catalytic characteristics, optimal conditions of catalysis, cytotoxicity, etc. Production of abzymes in SLE mice is associated with changes in the differentiation of hematopoietic stem cells of bone marrow, increase in lymphocyte proliferation, and significant suppression of cell apoptosis in different organs. In this chapter, abzymes with different catalytic activities in SLE are described.

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Mammalian Nucleolytic Enzymes

Cited by 121 publications

References 329 publications

Ribonuclease activity and substrate preference of human eosinophil cationic protein (ECP)

Ribonuclease activity and substrate preference of human eosinophil cationic protein (ECP)

Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.

Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

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