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Last update 08 May 2025

CPT1B

Last update 08 May 2025

Basic Info

Synonyms

Carnitine O-palmitoyltransferase 1, muscle isoform, Carnitine O-palmitoyltransferase I, muscle isoform, carnitine palmitoyltransferase 1B

+ [7]

Introduction

Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion.

Drugs associated with CPT1B

Etomoxir

Target

CPT1B

Mechanism

CPT1B inhibitors

Active Org.

Numiera Therapeutics, Inc.

Originator Org.

Meta-IQ

Active Indication

Glioblastoma [+1]

Inactive Indication

Multiple Sclerosis [+1]

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

MP-2000

Target

CPT1B

Mechanism

CPT1B inhibitors

Active Org.-

Originator Org.

MetrioPharm AG

Active Indication-

Inactive Indication

Heart Diseases

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

SDZ-269-518

Target

CPT1B

Mechanism

CPT1B inhibitors

Active Org.-

Originator Org.

Sandoz Ltd.

Active Indication-

Inactive Indication

Diabetes Mellitus, Type 2

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with CPT1B

100 Translational Medicine associated with CPT1B

0 Patents (Medical) associated with CPT1B

466

Literatures (Medical) associated with CPT1B

01 May 2025·Pharmacological Reviews

International Union of Basic and Clinical Pharmacology. CXIX. Fundamental insights and clinical relevance regarding the carnitine palmitoyltransferase family of enzymes

Review

Author: Fadó, Rut ; Rodríguez-Rodríguez, Rosalía ; Paraiso, West Kristian ; Baena, Miguel ; Zagmutt, Sebastián ; Reguera, Ana Cristina ; Casals, Núria

The carnitine palmitoyltransferases (CPTs) play a key role in controlling the oxidation of long-chain fatty acids and are potential therapeutic targets for diseases with a strong metabolic component, such as obesity, diabetes, and cancer. Four distinct proteins are CPT1A, CPT1B, CPT1C, and CPT2, differing in tissue expression and catalytic activity. CPT1s are finely regulated by malonyl-CoA, a metabolite whose intracellular levels reflect the cell's nutritional state. Although CPT1C does not exhibit significant catalytic activity, it is capable of modulating the functioning of other neuronal proteins. Structurally, all CPTs share a Y-shaped catalytic tunnel that allows the entry of 2 substrates and accommodation of the acyl group in a hydrophobic pocket. Several molecules targeting these enzymes have been described, some showing potential in normalizing blood glucose levels in diabetic patients, and others that, through a central mechanism, are anorexigenic and enhance energy expenditure. However, given the critical roles that CPTs play in certain tissues, such as the heart, liver, and brain, it is essential to fully understand the differences between the various isoforms. We analyze in detail the structure of these proteins, their cellular and physiological functions, and their potential as therapeutic targets in diseases such as obesity, diabetes, and cancer. We also describe drugs identified to date as having inhibitory or activating capabilities for these proteins. This knowledge will support the design of new drugs specific to each isoform, and the development of nanomedicines that can selectively target particular tissues or cells. SIGNIFICANCE STATEMENT: Carnitine palmitoyltransferase (CPT) proteins, as gatekeepers of fatty acid oxidation, have great potential as pharmacological targets to treat metabolic diseases like obesity, diabetes, and cancer. In recent years, significant progress has been made in understanding the 3-dimensional structure of CPTs and their pathophysiological functions. A deeper understanding of the differences between the various CPT family members will enable the design of selective drugs and therapeutic approaches with fewer side effects.

01 Apr 2025·Journal of Dairy Science

Effects of Maternal Blood β-Hydroxybutyrate on Brown Adipose Tissue Functions and Thermogenic and Metabolic Health in Neonatal Calves

Article

Author: Ma, Yulin ; Ghaffari, Morteza H ; Gai, Yang ; Hu, Zhiyong ; Chen, Yanting ; Yang, Shuyan ; Huang, Shilong ; Azzaz, Hossam H ; Gu, Zhaobing ; Zhang, Yu ; He, Rui ; Mao, Shengyong ; Ma, Guiling

Maternal metabolic health, particularly during late pregnancy, plays a crucial role in fetal development and postnatal metabolic function. Elevated levels of β-hydroxybutyrate (BHB) in dry cows, commonly observed in late gestation, may affect offspring development, but the effects on brown adipose tissue (BAT) and metabolic health remain unclear. In this study, 60 pregnant Holstein dairy cows were categorized into 2 groups based on serum BHB concentrations measured at 1, 3, 5 and 7 wk after dry-off: Maternal-Low-BHB (n = 30; mean ± SEM, 0.21 ± 0.005 mM) and Maternal-High-BHB (n = 30; mean ± SEM, 0.64 ± 0.02 mM). Blood metabolites, including BHB, nonesterified fatty acids (NEFA) and glucose, were monitored throughout the dry period. Calves born from these cows were evaluated for body growth, body temperature, glucose sensitivity, fecal and cough score during the first month of life, with perirenal BAT and skin samples collected for analysis of thermogenic gene expression. Expression of stress genes, including Cold-Inducible RNA-Binding Protein (CIRBP), Heat Shock Protein 70 (HSP70) and Heat Shock Factor Binding Protein 1 (HSBP1), was analyzed in skin tissue. Expression of thermogenic genes, including Uncoupling Protein 1 (UCP-1), Cyclic AMP Response Element-Binding Protein 4 (CREBP4) and Carnitine Palmitoyltransferase 1B (CPT1B), and protein contents of UCP-1, Activated Receptor Gamma Coactivator 1 Alpha (PGC-1a) were analyzed in BAT. In vitro, stromal vascular fractions (SVFs) were also isolated in calf's BAT, and further induced for brown adipocyte formation with dosed BHB supplementation. Results showed no differences in birth weight, body size and body temperatures of calves born to Maternal High BHB cows compared with calves born to Maternal Low BHB cows. However, the calves from the Maternal High BHB group had higher expressions of stress genes in the skin, and decreased BAT mass and expression of thermogenic genes. Compared with the Maternal Low BHB group, one-month-old calves in the Maternal High BHB group also showed significantly lower BAT mass, decreased expression of thermogenic genes such as UCP-1, CREBP4 and CPT1B, and decreased mitochondrial density, indicating impaired BAT development. In addition, the calves from the Maternal High BHB group showed reduced glucose sensitivity, as evidenced by their inability to maintain stable blood glucose levels during a glucose tolerance test. Protein concentrations of UCP-1 and PGC-1a were significantly lower in the BAT of calves born to Maternal High BHB cows. In vitro, BHB supplementation inhibited brown adipocyte differentiation and thermogenesis, supporting the elevated maternal BHB impairs brown adipogenesis and mitochondrial biogenesis. Overall, this study demonstrates that calves born from elevated maternal BHB levels (∼0.64 mM) within the normal physiological range in dry period significantly had impaired perinatal BAT development, thermogenesis, and glucose metabolism, highlighting the roles of maternal metabolic health in programming metabolic and thermoregulatory capacity in offspring.

17 Mar 2025·The Journal of Clinical Endocrinology & Metabolism

Characterizing 24-Hour Skeletal Muscle Gene Expression Alongside Metabolic and Endocrine Responses Under Diurnal Conditions

Article

Author: Clayton, David J ; Tsintzas, Kostas ; Thompson, Dylan ; Johnston, Jonathan D ; James, Lewis J ; Betts, James A ; Karagounis, Leonidas G ; Slater, Tommy ; Smith, Harry A ; Templeman, Iain ; Davis, Max ; Gonzalez, Javier T ; Middleton, Benita ; Walhin, Jean-Philippe ; Varley, Ian

AbstractContextSkeletal muscle plays a central role in the storage, synthesis, and breakdown of nutrients, yet little research has explored temporal responses of this human tissue, especially with concurrent measures of systemic biomarkers of metabolism.ObjectiveTo characterize temporal profiles in skeletal muscle expression of genes involved in carbohydrate metabolism, lipid metabolism, circadian clocks, and autophagy and descriptively relate them to systemic metabolites and hormones during a controlled laboratory protocol.MethodsTen healthy adults (9M/1F, [mean ± SD] age 30 ± 10 years; BMI 24.1 ± 2.7 kg·m−2) rested in the laboratory for 37 hours with all data collected during the final 24 hours (08:00–08:00 hours). Participants ingested hourly isocaloric liquid meal replacements alongside appetite assessments during waking before a sleep opportunity from 22:00 to 07:00 hours. Blood samples were collected hourly for endocrine and metabolite analyses, with muscle biopsies occurring every 4 hours from 12:00 to 08:00 hours the following day to quantify gene expression.ResultsPlasma insulin displayed diurnal rhythmicity peaking at 18:04 hours. Expression of skeletal muscle genes involved in carbohydrate metabolism (Name, Acrophase [hours]: GLUT4, 14:40; PPARGC1A, 16:13; HK2, 18:24) and lipid metabolism (FABP3, 12:37; PDK4, 05:30; CPT1B, 12:58) displayed 24-hour rhythmicity that reflected the temporal rhythm of insulin. Equally, circulating glucose (00:19 hours), nonesterified fatty acids (04:56), glycerol (04:32), triglyceride (23:14), urea (00:46), C-terminal telopeptide (05:07), and cortisol (22:50) concentrations also all displayed diurnal rhythmicity.ConclusionDiurnal rhythms were present in human skeletal muscle gene expression as well systemic metabolites and hormones under controlled diurnal conditions. The temporal patterns of genes relating to carbohydrate and lipid metabolism alongside circulating insulin are consistent with diurnal rhythms being driven in part by the diurnal influence of cyclic feeding and fasting.

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CPT1B

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