Biotin
Sources réglementaires consultées
Indications approuvées
- États carentiels en biotine, besoins accrus en biotine et troubles métaboliques nécessitant de la biotine.
Contre-indications
Absolues
- Hypersensibilité à la biotine.
Mises en garde cliniques
- Mise en garde majeure · Ne pas dépasser les doses recommandées. La biotine peut interférer avec les tests fondés sur l’interaction biotine-streptavidine et produire des résultats faussement élevés ou faibles, notamment des résultats de troponine faussement négatifs ; informer le laboratoire et utiliser d’autres tests si une interférence est suspectée. — https://cima.aemps.es/cima/dochtml/ft/34236/FT_34236.html
Interactions médicamenteuses
- ModéréeMédicaments antiépileptiques
Mécanisme: Les médicaments antiépileptiques peuvent réduire la concentration plasmatique de biotine en augmentant ses besoins métaboliques.
Recommandation: Surveiller la réponse clinique et le statut en biotine pendant l’utilisation concomitante.
https://cima.aemps.es/cima/dochtml/ft/34236/FT_34236.html
Effets indésirables
Communs (≥1%)
Rarement : réaction allergique · Rarement : troubles gastro-intestinaux
Grossesse et allaitement
Aucun problème n’a été rapporté aux doses nutritionnelles recommandées; les besoins pendant la grossesse et l’allaitement sont de 30 et 35 microgrammes/jour. Cela n’établit pas la sécurité des doses pharmacologiques.
Bibliographie récente (PubMed)
Trace elements and vitamins, named together micronutrients (MNs), are essential for human metabolism. Recent research has shown the importance of MNs in common pathologies, with significant deficiencies impacting the outcome. This guideline aims to provide information for daily clinical nutrition practice regarding assessment of MN status, monitoring, and prescription. It proposes a consensus terminology, since many words are used imprecisely, resulting in confusion. This is particularly true for the words "deficiency", "repletion", "complement", and "supplement". The expert group attempted to apply the 2015 standard operating procedures (SOP) for ESPEN which focuses on disease. However, this approach could not be applied due to the multiple diseases requiring clinical nutrition resulting in one text for each MN, rather than for diseases. An extensive search of the literature was conducted in the databases Medline, PubMed, Cochrane, Google Scholar, and CINAHL. The search focused on physiological data, historical evidence (published before PubMed release in 1996), and observational and/or randomized trials. For each MN, the main functions, optimal analytical methods, impact of inflammation, potential toxicity, and provision during enteral or parenteral nutrition were addressed. The SOP wording was applied for strength of recommendations. There was a limited number of interventional trials, preventing meta-analysis and leading to a low level of evidence. The recommendations underwent a consensus process, which resulted in a percentage of agreement (%): strong consensus required of >90% of votes. Altogether the guideline proposes sets of recommendations for 26 MNs, resulting in 170 single recommendations. Critical MNs were identified with deficiencies being present in numerous acute and chronic diseases. Monitoring and management strategies are proposed. This guideline should enable addressing suboptimal and deficient status of a bundle of MNs in at-risk diseases. In p
Proximity biotinylation is a commonly used method to identify the in vivo proximal proteome for proteins of interest. This technology typically relies on fusing a bait protein to a biotin ligase using overexpression or clustered regularly interspaced short palindromic repeats (CRISPR)-based tagging, thus prohibiting the use of such assays in cell types that are difficult to transfect or transduce. We recently developed an 'off-the-shelf' proximity biotinylation method that makes use of a recombinant enzyme consisting of the biotin ligase TurboID fused to the antibody-recognizing moiety Protein A. In this method, a bait-specific antibody and the ProteinA-Turbo enzyme are consecutively added to permeabilized fixed or unfixed cells. Following incubation, during which ProteinA-Turbo antibody-antigen complexes are formed, unbound molecules are washed away, after which bait-proximal biotinylation is triggered by the addition of exogenous biotin. Finally, biotinylated proteins are enriched from crude lysates using streptavidin beads followed by mass spectrometry-based protein identification. In principle, any scientist can perform this protocol within 3 days, although generating the proteomics data requires access to a high-end liquid chromatography-mass spectrometry setup. Data analysis and data visualization are relatively straightforward and can be performed using any type of software that converts raw mass spectrometry spectra files into identified and quantified proteins. The protocol has been optimized for nuclear targets but may also be adapted to other subcellular regions of interest.
Immunoassays are powerful qualitative and quantitative analytical techniques. Since the first description of an immunoassay method in 1959, advances have been made in assay designs and analytical characteristics, opening the door for their widespread implementation in clinical laboratories. Clinical endocrinology is closely linked to laboratory medicine because hormone quantification is important for the diagnosis, treatment, and prognosis of endocrine disorders. Several interferences in immunoassays have been identified through the years; although some are no longer encountered in daily practice, cross-reaction, heterophile antibodies, biotin, and anti-analyte antibodies still cause problems. Newer interferences are also emerging with the development of new therapies. The interfering substance may be exogenous (e.g., a drug or substance absorbed by the patient) or endogenous (e.g., antibodies produced by the patient), and the bias caused by interference can be positive or negative. The consequences of interference can be deleterious when clinicians consider erroneous results to establish a diagnosis, leading to unnecessary explorations or inappropriate treatments. Clinical laboratories and manufacturers continue to investigate methods for the detection, elimination, and prevention of interferences. However, no system is completely devoid of such incidents. In this review, we focus on the analytical interferences encountered in daily practice and possible solutions for their detection or elimination.
Biotin (vitamin B7, or vitamin H) is a water-soluble B-vitamin that functions as a cofactor for carboxylases, i.e., enzymes involved in the cellular metabolism of fatty acids and amino acids and in gluconeogenesis; moreover, as reported, biotin may be involved in gene regulation. Biotin is not synthesized by human cells, but it is found in food and is also produced by intestinal bacteria. Biotin status/homeostasis in human individuals depends on several factors, including efficiency/deficiency of the enzymes involved in biotin recycling within the human organism (biotinidase, holocarboxylase synthetase), and/or effectiveness of intestinal uptake, which is mainly accomplished through the sodium-dependent multivitamin transporter. In the last years, administration of biotin at high/"pharmacological" doses has been proposed to treat specific defects/deficiencies and human disorders, exhibiting mainly neurological and/or dermatological symptoms and including biotinidase deficiency, holocarboxylase synthetase deficiency, and biotin-thiamine-responsive basal ganglia disease. On the other hand, according to warnings of the Food and Drug Administration, USA, high biotin levels can affect clinical biotin-(strept)avidin assays and thus lead to false results during quantification of critical biomarkers. In this review article, recent findings/advancements that may offer new insight in the abovementioned research fields concerning biotin will be presented and briefly discussed.
Biotin has widespread popularity as a hair supplement. We sought to review the literature regarding biotin's efficacy as a hair supplement. We conducted a literature search of PubMed for articles specifically studying the use of oral biotin for hair growth or quality. Case reports and case series were excluded. Three studies met our inclusion criteria. The first study was the highest quality, with a double-blind and placebo-controlled study design, but their results found no difference between the biotin and placebo groups for hair growth. The other two studies investigated specific patient populations (patients on isotretinoin and female patients post-sleeve gastrectomy). Both studies were susceptible to multiple potential biases and neither had striking results in favor of biotin. Our review is limited by lack of available studies. Given the widespread popularity of biotin as a hair supplement, one would presume that this claim must be grounded in strong evidence; however, there is a large discrepancy between the public's perception of its efficacy and the scientific literature. The utility of biotin as a hair supplement is not supported by high-quality studies.