Some Aspects of Biotin Binding to Protein Catalyzed by Biotin-Deficient Chicken Liver Preparations

Pn, Achuta Murthy; Sp, Mistry; Fa, Kummerow

doi:10.3181/00379727-145-37852

Cited by 10 publications

(8 citation statements)

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“…Indeed, in holocarboxylase synthetase deficiency neurologic symptoms are not prominent and usually occur concomitantly with acute systemic metabolic decompensation. This is in accordance with the finding that in experimental biotin deficiency in the rat biotin concentrations (42) and carboxylase (43) were better preserved in the CNS than in the liver.…”

Section: Discussionsupporting

confidence: 81%

Biotinidase Deficiency: A Cause of Subacute Necrotizing Encephalomyelopathy (Leigh Syndrome). Report of a Case with Lethal Outcome

Wick

et al. 1989

Pediatr Res

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Section: Discussionsupporting

confidence: 81%

Biotinidase Deficiency: A Cause of Subacute Necrotizing Encephalomyelopathy (Leigh Syndrome). Report of a Case with Lethal Outcome

Wick

et al. 1989

Pediatr Res

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“…Since cells from patients with the late-onset form of the disease have normal holocarboxylase synthetase activity [5], it has been assumed that this condition results from a defect in either the renal or intestinal transport of biotin and studies from several laboratories have therefore focused on the intestinal absorption and renal excretion of the vitamin [6-S]. However, the hepatic biotin pool is very large in comparison to the small amount of biotin which is normally absorbed from the diet or intestinal flora each day [9,10]. We therefore sought to test the alternative hypothesis that late-onset MCD results from an abnormality in biotin metabolism or turnover rather than a primary defect in biotin transport.…”

mentioning

confidence: 99%

Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency

Wolf¹,

Grier²,

Allen³

et al. 1983

Clinica Chimica Acta

318

196

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Late-onset multiple carboxylase deficiency is characterized clinically by skin rash, alopecia, seizures and ataxia and occasionally by candidiasis and developmental delay. Biochemically, these individuals exhibit findings consistent with a combined deficiency of the biotin-dependent carboxylases. We have found that the activity of the enzyme biotinidase is also deficient in the sera of five affected children (0 to 3% of mean control activity, 5.80 +/- 0.89 nmol X min-1 X ml-1 serum), and believe that it represents the primary biochemical defect in this disease. Biotinidase catalyzes the removal of biotin from the epsilon-amino group of lysine, through which biotin is covalently bound to the four known human carboxylases, thereby regenerating biotin for reutilization. The deficient activity in our patients was not due to an inhibitor, particularly biotin. It is also not a consequence of feedback control in affected individuals under treatment with pharmacologic doses of biotin. The biotinidase activities of the parents of those children who were available for study were intermediate between deficient and normal values (46% to 65% of mean normal activity). Children lacking biotinidase activity are unable to recycle biotin, and are thus entirely dependent upon exogenous biotin to prevent deficiency. Our findings indicate that the primary biochemical defect in late-onset multiple carboxylase deficiency is in biotinidase activity which is inherited as an autosomal recessive trait.

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“…The importance of biotin and biocytin (lysine-conjugated biotin) is illustrated by the many symptoms associated with dietary biotin deficiency and with congenital defects in biotin-related enzymes and carrier proteins (Rosenberg, 1976;Theone et al, 1981; see also Dakshinamurti and Bhagavan, 1985). Biotin deficiency affects a variety of organ systems, including the integumentum, the immune system, and the nervous system, in a variety of animals (Achuta Murthy and Mistry, 1977;Dakshinamurti and Bhagavan, 1985). Since most eukaryote cells do not have the capacity for manufacturing biotin, their ability to take up and accumulate biotin is crucial.…”

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confidence: 99%

Biotin staining in the giant fiber systems of the lobster

Pokay

1994

J of Comparative Neurology

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The avidin-biotin-complex method is a popular immunocytochemical technique. This method labels consistently a group of neurons in the lobster ventral nerve cord in the absence of primary antibodies. The specific staining is due to a relatively high level of endogenous biotin (or biocytin) in these neurons. These biotin-positive neurons are located in the supraesophageal, thoracic, and abdominal ganglia. Intraaxonal injection of Lucifer yellow followed by Texas red-conjugated streptavidin staining reveals that the neurons are members of the medial giant (MG) and lateral giant (LG) systems, which are important in mediating rapid tail flipping during escape maneuvers. In neuronal somata, staining is restricted to the cytoplasm. Within MG axons, staining appears as punctate, subaxolemmal structures. Preincubating nerve cords in biocytin or direct intraaxonal injection of biocytin enhances staining of these punctate organelles. In LG axons, staining is localized to fragments of braided filamentous structures that also appear to be associated with the axolemma. Preincubation of ventral nerve cords in various concentrations of biocytin results in the appearance of additional groups of stained neurons, suggesting that there are subsets of neurons with specific biocytin-uptake or -retention mechanisms. In the crayfish, biotin-positive staining is confined to the MG neurons; the LG neurons are not stained. In the earthworm, no staining is observed in the MG and LG axon escape systems. In the goldfish, no biotin-staining is seen in the Mauthner neurons and their axons. The significance of specific localization of biotin or biocytin to subsets of neurons is unclear. It may reflect the presence of high levels of biocytin moieties on biotin-dependent enzymes. Biotin is an important cofactor in the catalytic functions of several decarboxylases crucial in energy production and lipogenesis. Axons of the giant fiber systems in lobsters and crayfish may have high energy and fatty acid synthesis requirements. Increased levels of biotin accumulation may also be related to other functions of the giant axon systems, such as the formation of electrical synapses among themselves and with phasic motoneurons.

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Some Aspects of Biotin Binding to Protein Catalyzed by Biotin-Deficient Chicken Liver Preparations

Cited by 10 publications

References 0 publications

Biotinidase Deficiency: A Cause of Subacute Necrotizing Encephalomyelopathy (Leigh Syndrome). Report of a Case with Lethal Outcome

Biotinidase Deficiency: A Cause of Subacute Necrotizing Encephalomyelopathy (Leigh Syndrome). Report of a Case with Lethal Outcome

Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency

Biotin staining in the giant fiber systems of the lobster

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