Intracellular transport of lipids

Glatz, Jan F. C.; Vusse, Ger J.

doi:10.1007/978-1-4613-1611-4_6

Cited by 7 publications

(12 citation statements)

References 34 publications

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“…It has been suggested that H-FABP might act as protective molecule against the toxic effect of (too) high intracellular levels of fatty acids (eg, occurring during ischemia) 21. In mice lacking H-FABP, the heart is unable to efficiently take up plasma-free long-chain fatty acids and use glucose instead leading to intolerance of acute exercise and later, resulting in asymmetrical septal hypertrophy 22.…”

Section: Discussionmentioning

confidence: 99%

Serum heart-type fatty acid-binding protein decreases and soluble isoform of suppression of tumorigenicity 2 increases significantly by long-term physical activity

Sponder

Lichtenauer

Wernly

et al. 2019

Journal of Investigative Medicine

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The aim of this prospective study was to investigate the influence of long-term physical activity on biomarkers for myocyte ischemia (heart-type fatty acid-binding protein, H-FABP), matrix remodelling/vascular stress (soluble isoform of suppression of tumorigenicity 2, sST2) and inflammation (soluble urokinase-type plasminogen activator receptor, suPAR). In this prospective observational study 109 subjects were recruited, 98 completed the study. Subjects were asked to perform exercise within the calculated training pulse for 8 months. The performance gain was measured/quantified by bicycle stress tests at the beginning and end of the observation period. Twenty-seven subjects with a performance gain <2.9% were excluded. suPAR, H-FABP and sST2 were measured in serum at baseline and after 2, 4 and 8 months by ELISA. We found a significant decrease in H-FABP (1.86 (0.86) to 1.29 (0.98) ng/mL; p<0.01) and a significant increase in sST2 levels (6126 (2759) to 6919 (3720) pg/mL; p=0.045) during the observation period of 8 months while there was no remarkable change in suPAR levels. We interpret the activity-induced decrease in H-FABP as sign of lower subclinical myocardial ischemia and better perfusion, probably due to a more economic metabolization and electrolyte balance. The increase in sST2 might reflect physiological sports-induced vascular stress. As H-FABP and sST2 play an important role in the pathomechanism of ischemic cardiomyopathy (iCMP) further studies should investigate the influence of regular physical activity on these biomarkers in a population of patients with iCMP.Trial registration number NCT02097199.

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Section: Discussionmentioning

confidence: 99%

Serum heart-type fatty acid-binding protein decreases and soluble isoform of suppression of tumorigenicity 2 increases significantly by long-term physical activity

Sponder

Lichtenauer

Wernly

et al. 2019

Journal of Investigative Medicine

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“…A significant fatty acid interaction with Mb would raise questions about the monolithic viewpoint that only fatty acid binding protein (FABP) traffics fatty acid in the cell (Glatz and van der Vusse, 1989). Even though FABP has a higher affinity for fatty acid than Mb, Mb exists in a significantly higher concentration than FABP in the cell.…”

Section: Other Functions Of Mb Poresmentioning

confidence: 99%

‘It's hollow’: the function of pores within myoglobin

Tomita

Kreutzer

Adachi

et al. 2010

Journal of Experimental Biology

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SUMMARY Despite a century of research, the cellular function of myoglobin (Mb), the mechanism regulating oxygen (O2) transport in the cell and the structure–function relationship of Mb remain incompletely understood. In particular, the presence and function of pores within Mb have attracted much recent attention. These pores can bind to Xe as well as to other ligands. Indeed, recent cryogenic X-ray crystallographic studies using novel techniques have captured snapshots of carbon monoxide (CO) migrating through these pores. The observed movement of the CO molecule from the heme iron site to the internal cavities and the associated structural changes of the amino acid residues around the cavities confirm the integral role of the pores in forming a ligand migration pathway from the protein surface to the heme. These observations resolve a long-standing controversy – but how these pores affect the physiological function of Mb poses a striking question at the frontier of biology.

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“…Thus FABPs may regulate cytoplasmic fatty acid concentrations and oxidative capacity (Glatz and Van der Vusse 1989;Kaikaus et al 1990;Matarese et al 1989;Veerkamp and Van Moerkerk 1993). The capability of FABPs to bind retinoic acid and metabolites of the eicosanoid pathway (Boylan and Gndas 199t;Dutta-Roy et al 1987;Raza et al 1989) suggests, moreover, their possible participation in cellular growth regulation and differentiation processes ).…”

Section: Introductionmentioning

confidence: 94%

“…With regard to their physicochemical, chemical and structural characteristics and to their ligand spectrum, they have been divided into three groups: (I) fatty acid-binding proteins (FABPs), (II) cellular retinol-binding proteins (CRBPs), and (lid cellular retinoic acid-binding protein (CRABP; for reviews see Bernier and JolRs 1987;Clarke and Armstrong 1989;Glatz and Van der Vusse 1989;. Data from both nucleic acid and amino acid sequence analyses revealed varying degrees of homology among members of the family of fatty acid-binding proteins, but with a highly conservative secondary and tertiary structure (Ockner 1990;Veerkamp etal.…”

Section: Introductionmentioning

confidence: 99%

Histochemical localization of heart-type fatty-acid binding protein in human and murine tissues

Zschiesche

Kleine

Spitzer

et al. 1995

Histochem Cell Biol

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A b s tra c t C ellular fatty acid-binding proteins (FABP) are a highly conserved fam ily of proteins consisting o f several subtypes» am ong them the m am m ary-derived growth inhibitor (M D G I) w hich is quite hom ologous to or even identical with the heart-type FABP (H-FABP). The FABPs and M D G I have been suggested to be in volved in intracellular fatty acid m etabolism and traffick ing. Recently, evidence for grow th and differentiation regulating properties of M D G I and H -FA B P was provid ed. U sing four affinity-purified polyclonal antibodies against bovine and hum an antigen preparations, the cel lular localization of M D G I/H -FA B P in hum an and mouse tissues and organs was studied. T he antibodies were weakly cross-reactive w ith adipose tissue extracts known to lack H-FABP, but failed to react by W estern blot analysis with liver-type FABP (L-FABP) and intesti nal-type FA B P (I-FABP). M D G I/H -FA B P protein was mainly detected in m yocardium , skeletal and sm ooth m uscle fibres, lipid and/or steroid synthesising cells (ad renals, Leydig cells, sebaceous glands, lactating m am mary gland) and term inally differentiated epithelia of the respiratory, intestinal and urogenital tracts. The results provide evidence that expression o f H -FA B P is associat ed with an irreversibly postm itotic and term inally differ entiated status of cells. Since all the antisera em ployed show ed spatially identical and qualitatively equal im m unostaining, it is suggested that hum an, bovine and m ouse M D G I/H -FA B P proteins share highly hom ologous epi topes.

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Intracellular transport of lipids

Cited by 7 publications

References 34 publications

Serum heart-type fatty acid-binding protein decreases and soluble isoform of suppression of tumorigenicity 2 increases significantly by long-term physical activity

Serum heart-type fatty acid-binding protein decreases and soluble isoform of suppression of tumorigenicity 2 increases significantly by long-term physical activity

‘It's hollow’: the function of pores within myoglobin

Histochemical localization of heart-type fatty-acid binding protein in human and murine tissues

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