Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.30.2 (endonuclease)
 18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An inherited type of amyloidosis was suspected in an individual of Italian descent who presented with vitreous opacities. Although no family history of amyloidosis was apparent, the patient's transthyretin gene was examined and found not to possess any of the known transthyretin mutations. Complete DNA sequencing revealed a substitution of adenine for thymine in the second base of codon 84 causing an amino acid change of asparagine for isoleucine. The mutation was confirmed by demonstrating the loss of an Sfa N1 restriction endonuclease site. Allele-specific DNA amplification by polymerase chain reaction also was used to confirm the mutation. Either of these tests can be used for diagnosis. Asparagine 84 represents the second mutation associated with amyloidosis to occur at codon 84.
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PMID:A new transthyretin mutation associated with amyloidotic vitreous opacities. Asparagine for isoleucine at position 84. 135 83

Familial amyloidotic polyneuropathy (FAP) is a dominantly inherited form of amyloidosis usually associated with an abnormal transthyretin (TTR), previously known as prealbumin. Several disease-related variants of the protein, each with a different amino acid substitution and correlating DNA point mutation, have been identified. The TTR gene from a patient suffering from this disorder was asymmetrically amplified and directly sequenced, revealing a cytosine for thymine substitution in the second base of codon 30 and the creation of a novel Cfo I restriction endonuclease site in exon 2. This mutation results in a previously undescribed substitution of an alanine for valine in the final TTR protein. Analysis of the amino acid mutation reveals it to be a hydrophilic substitution at a hydrophobic core position. Alanine at position 30 represents the second FAP-associated mutation at position 30 in TTR.
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PMID:Familial amyloidotic polyneuropathy: a new transthyretin position 30 mutation (alanine for valine) in a family of German descent. 154 14

Type I familial amyloid polyneuropathy (FAP) is an autosomal dominant hereditary generalized amyloidosis characterized by polyneuropathy and autonomic nerve failure. The main component of the amyloid fibril protein in this disorder has been shown to be a variant prealbumin with a single substitution of a methionine residue for valine at position 30. In the present study we have investigated 19 patients with FAP aged 31 to 67 and an asymptomatic family member using gene analysis with primer-directed enzymatic amplification (PCR) of DNA, isolation of plasma variant prealbumin and immunohistochemical identification of tissue amyloid protein. All patients and a symptom-free boy in the affected family had the mutant prealbumin gene showing abnormal DNA fragments by treatment with restriction endonuclease Bal I, and plasma variant prealbumin was also detected in all of them by reverse-phase high performance liquid chromatography. Rectum biopsies obtained from 9 patients showed amyloid deposits which were specifically immunostained by anti-human prealbumin antiserum. However, an asymptomatic carrier at the age of 16 showed no rectal amyloid deposition. Recent studies of FAP have disclosed that the expression of type I FAP is closely associated with the gene mutation of prealbumin. Accordingly, a simple and rapid method to detect this gene abnormality using PCR technique is considered to be very useful for diagnosis of type I FAP and can also provide valuable information for the genetic counselling of the family members at risk.
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PMID:[Diagnosis of familial amyloid polyneuropathy--gene analysis with primer-directed enzymatic amplification of DNA, isolation of plasma variant prealbumin and immunohistochemical identification of tissue amyloid protein]. 165 25

The autosomal dominant prealbumin amyloidoses are late-onset disorders characterized by varying degrees of peripheral neuropathy, nephropathy and cardiomyopathy. To date, seven different single amino acid mutations in the plasma protein prealbumin (transthyretin) have been found to be associated with amyloidosis and each is the result of a single nucleotide change in the prealbumin gene. By virtue of the restriction endonuclease sites created by the point mutations which give rise to the protein variants, direct DNA tests using Southern analysis have already been developed for detection of the Met-30, Ile-33, Ala-60, Tyr-77 and Ser-84 prealbumin genes. As an alternative to Southern analysis, we have amplified discrete regions of the prealbumin gene using polymerase chain reaction (PCR) and used restriction enzyme analysis of the PCR products to detect the Met-30, Ala-60, Tyr-77 and Ser-84 prealbumin genes after agarose gel electrophoresis and staining with ethidium bromide. In comparison to Southern analysis these alternative tests yield results much more quickly and avoid the use and handling of radioactively labeled probes.
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PMID:Hereditary amyloidosis: detection of variant prealbumin genes by restriction enzyme analysis of amplified genomic DNA sequences. 215 45

The results of an inventory of field cases of amyloid arthropathy in chickens and of routine post-mortem recordings over a two years period are described. Studies were also performed to evaluate the amyloidogenic potential of arthrotropic bacterial species (Staphylococcus aureus, Escherichia coli and Salmonella enteritidis) isolated from chickens as well as several Enterococcus faecalis isolates compared to the amyloidogenic E. faecalis isolate (previously isolated from amyloidotic joints). As chicken anemia virus was also isolated from amyloidotic joints of field cases, it was also screened for its amyloidogenic potential. In another experiment, Mycoplasma synoviae, inactivated E. faecalis isolate 6085.94, Freund's adjuvant and an arthrotropic reovirus field isolate were also screened for amyloidogenicity by intra-articular injection. These studies showed that the ability to elicit extensive amyloid arthropathy is reserved primarily to E. faecalis, but that this property is not common to every E. faecalis isolate. Intra-articular application of complete Freund's adjuvant led to the formation of extensive joint amyloid deposits. Of the other micro-organisms studied, S. aureus, S. enteritidis and E. coli were also able to cause joint amyloidosis, but in very small amounts. Inactivated E. faecalis, chicken anemia virus and reovirus did not cause amyloid arthropathy after intra-articular inoculation. This study is consistent with results of the analyses of previous field cases and of the induction of amyloid arthropathy in chickens, suggesting a considerable role for E. faecalis in this clinical-pathological entity. Finally, strain typing by analysis of chromosomal DNA restriction endonuclease digests by pulsed-field gel electrophoresis (PFGE) of amyloidogenic, non-amyloidogenic, amyloid-associated and other E. faecalis isolates from various origins showed that all amyloidogenic and amyloid-associated E. faecalis isolates had similar restriction digests, suggesting clonal spread.
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PMID:The role of various agents in chicken amyloid arthropathy. 1003 85

Although symmetrical polyarticular amyloidosis has been described extensively in brown layers, spontaneous unilateral amyloid arthropathy has not been described previously in chickens. Birds from nine flocks of broiler parent stock (PS) had unilateral lameness associated with severe swelling of the left hock joint and the caudal aspect of the metatarsus. Gross pathology was restricted to the left hock joint and the left digital flexor tendons in almost all cases, suggesting an association with administration of Marek's disease vaccine. Amyloid deposits were found in 83% (25/30) of affected joints by histological examination of Congo red stained sections. Systemic amyloidosis, involving mainly the liver and spleen, was found in 59% (10/17) of birds. Enterococcus faecalis was isolated from joints in 77% (23/30) of cases and Staphylococcus aureus was isolated from the joint in one case (1/30). Thirty-five E. faecalis isolates from joints, tendons and blood samples from birds in five affected PS flocks were compared using pulsed-field gel electrophoresis (PFGE) to separate genomic fragments after digestion with SmaI. All but one isolate had identical or closely related restriction endonuclease digestion (RED) patterns that were very similar to a known arthropathic and amyloidogenic E. faecalis isolate. A further 30 E. faecalis isolates from seven grandparent stock (GPS) flocks and two isolates from two unaffected PS flocks of the same genetic background were analysed by PFGE. Among these isolates, 11 originating from four GPS flocks had RED patterns identical to or closely related to the reference amyloid-inducing strain. Moreover, one E. faecalis isolate from amyloidotic joints of brown layers housed in California, USA was included in the analysis and appeared to be identical to the reference strain. This study showed that the E. faecalis isolates involved in these outbreaks of unilateral amyloid arthropathy in broiler breeders belonged to the same clone as that responsible for outbreaks in brown layers.
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PMID:Molecular epidemiology of unilateral amyloid arthropathy in broiler breeders associated with Enterococcus faecalis. 1242 90