Serum Carnosinase Deficiency: A Non‐disabling Phenotype?

Cohen, Morris J.; Pl, Hartlage; Krawiecki, Nicolas; Ra, Roesel; Al, Carter; Hommes, F. A.

doi:10.1111/j.1365-2788.1985.tb00364.x

Cited by 9 publications

(8 citation statements)

References 19 publications

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“…Alterations of serum carnosinase expression and activity have been shown to be associated with neurological diseases including multiple sclerosis and Parkinson’s disease 54 . Although carnosinase deficiency has been reported in patients with ID and DD 55 – 57 , the overexpression of CNDP1 from copy number gain as seen in our patient has never, to our knowledge, been previously reported. Additionally, carnosinase is an enzyme whose alterations is likely to be recessively inherited, so CNDP1 gene duplication may not affect the carnosinase function.…”

Section: Discussioncontrasting

confidence: 48%

Chromosomal microarray analysis in a cohort of underrepresented population identifies SERINC2 as a novel candidate gene for autism spectrum disorder

Hnoonual

Thammachote

Tim‐Aroon

et al. 2017

Sci Rep

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Chromosomal microarray (CMA) is now recognized as the first-tier genetic test for detection of copy number variations (CNVs) in patients with autism spectrum disorder (ASD). The aims of this study were to identify known and novel ASD associated-CNVs and to evaluate the diagnostic yield of CMA in Thai patients with ASD. The Infinium CytoSNP-850K BeadChip was used to detect CNVs in 114 Thai patients comprised of 68 retrospective ASD patients (group 1) with the use of CMA as a second line test and 46 prospective ASD and developmental delay patients (group 2) with the use of CMA as the first-tier test. We identified 7 (6.1%) pathogenic CNVs and 22 (19.3%) variants of uncertain clinical significance (VOUS). A total of 29 patients with pathogenic CNVs and VOUS were found in 22% (15/68) and 30.4% (14/46) of the patients in groups 1 and 2, respectively. The difference in detected CNV frequencies between the 2 groups was not statistically significant (Chi square = 1.02, df = 1, P = 0.31). In addition, we propose one novel ASD candidate gene, SERINC2, which warrants further investigation. Our findings provide supportive evidence that CMA studies using population-specific reference databases in underrepresented populations are useful for identification of novel candidate genes.

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Section: Discussioncontrasting

confidence: 48%

Chromosomal microarray analysis in a cohort of underrepresented population identifies SERINC2 as a novel candidate gene for autism spectrum disorder

Hnoonual

Thammachote

Tim‐Aroon

et al. 2017

Sci Rep

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“…So, serum carnosinase probably did not evolve to avoid high serum carnosine concentrations, even though it may help in the digestion of HCD and the availability of ␤-alanine and L-histidine in meat-eating early hominids. Second, the findings of dietary interventions in carnosinase deficiency patients do not support the idea that high carnosine concentrations in itself would be causing the mental retardation and other clinical signs (88). Finally, it would be somewhat strange that we would develop a system with the aim to avoid the high presence of a molecule like carnosine that has low toxicity and has been documented to have health-promoting effects in rodents (who lack serum carnosinase activity).…”

Section: The Human Serum Carnosinase Paradoxmentioning

confidence: 96%

“…Reported symptoms of patients with serum carnosinase deficiency are mental retardation, hypotonia, myoclonic seizures, and spasticity, which usually manifest in the first year of life (298,377,392). However, it appears that the severity of symptoms is not related to the residual activity of serum carnosinase (88), and serum carnosinase deficiency can occur in the absence of neurological symptoms. Dietary meat restriction will partially reduce carnosinemia, but will not relieve clinical symptoms.…”

Section: B Serum Carnosinase Deficiency and Homocarnosinosismentioning

confidence: 99%

Physiology and Pathophysiology of Carnosine

Boldyrev

Aldini

Derave

2013

Physiological Reviews

902

1,023

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Carnosine (β-alanyl-l-histidine) was discovered in 1900 as an abundant non-protein nitrogen-containing compound of meat. The dipeptide is not only found in skeletal muscle, but also in other excitable tissues. Most animals, except humans, also possess a methylated variant of carnosine, either anserine or ophidine/balenine, collectively called the histidine-containing dipeptides. This review aims to decipher the physiological roles of carnosine, based on its biochemical properties. The latter include pH-buffering, metal-ion chelation, and antioxidant capacity as well as the capacity to protect against formation of advanced glycation and lipoxidation end-products. For these reasons, the therapeutic potential of carnosine supplementation has been tested in numerous diseases in which ischemic or oxidative stress are involved. For several pathologies, such as diabetes and its complications, ocular disease, aging, and neurological disorders, promising preclinical and clinical results have been obtained. Also the pathophysiological relevance of serum carnosinase, the enzyme actively degrading carnosine into l-histidine and β-alanine, is discussed. The carnosine system has evolved as a pluripotent solution to a number of homeostatic challenges. l-Histidine, and more specifically its imidazole moiety, appears to be the prime bioactive component, whereas β-alanine is mainly regulating the synthesis of the dipeptide. This paper summarizes a century of scientific exploration on the (patho)physiological role of carnosine and related compounds. However, far more experiments in the fields of physiology and related disciplines (biology, pharmacology, genetics, molecular biology, etc.) are required to gain a full understanding of the function and applications of this intriguing molecule.

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“…Homocarnosinosis (EC 236130), which was considered as a distinct disorder, may be a severe serum carnosinase deficiency, since the presence of the enzyme homocarnosinase was not shown in human tissues [109]. The phenotype of SCD patients is very variable and it was suggested that the enzyme deficiency is not pivotal to the neurological dysfunction [108,110].…”

Section: Id In Scdmentioning

confidence: 99%

Carnosine and Related Peptides: Therapeutic Potential in Age-Related Disorders

Cararo¹,

Streck²,

Schuck³

et al. 2015

Aging and disease

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Imidazole dipeptides (ID), such as carnosine (β-alanyl-L-histidine), are compounds widely distributed in excitable tissues of vertebrates. ID are also endowed of several biochemical properties in biological tissues, including antioxidant, bivalent metal ion chelating, proton buffering, and carbonyl scavenger activities. Furthermore, remarkable biological effects have been assigned to such compounds in age-related human disorders and in patients whose activity of serum carnosinase is deficient or undetectable. Nevertheless, the precise biological role of ID is still to be unraveled. In the present review we shall discuss some evidences from clinical and basic studies for the utilization of ID as a drug therapy for age-related human disorders.

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Serum Carnosinase Deficiency: A Non‐disabling Phenotype?

Cited by 9 publications

References 19 publications

Chromosomal microarray analysis in a cohort of underrepresented population identifies SERINC2 as a novel candidate gene for autism spectrum disorder

Chromosomal microarray analysis in a cohort of underrepresented population identifies SERINC2 as a novel candidate gene for autism spectrum disorder

Physiology and Pathophysiology of Carnosine

Carnosine and Related Peptides: Therapeutic Potential in Age-Related Disorders

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