Histochemical demonstration of a monocarboxylate transporter in the mouse perineurium with special reference to GLUT1

Takebe, Kumiko; Nio‐Kobayashi, Junko; Takahashi-Iwanaga, Hiromi; Iwanaga, Toshihiko

doi:10.2220/biomedres.29.297

Cited by 31 publications

(38 citation statements)

References 37 publications

(65 reference statements)

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“…Stark et al (135) have reported the lack of GLUT1 in the perineurium of peripheral nerves in P0 and P14 rats, in contrast to its intense expression in adult rats. In accordance with this, nerves in murine neonates at P5 and P10 were respectively negative and faintly immunoreactive for GLUT1 but intensely positive for MCT1 in these stages (142). Lactate is proposed as a fuel source for proper myelination in the central nervous system (126).…”

Section: The Peripheral Nervous Systemsupporting

confidence: 61%

“…Ultrastructually, the MCT1 and GLUT1 immunoreactivities in the thick perineurium show an intensity gradient decreasing towards the innermost layer. In neonates, the MCT1 immunoreactivity in the perineurium is intense, while the GLUT1 immunoreactivity is faint or absent (142). These findings suggest that peripheral nerves depend on monocarboxylates as one of the major energy sources and that MCT1 in the perineurium is responsible for the supply of monocarboxylates to nerve fibers and Schwann cells, possibly from outside the perineurium.…”

Section: The Peripheral Nervous Systemmentioning

confidence: 87%

“…In the peripheral nerves, MCT1 immunoreactivity is found in the perineurial sheath and colocalized with GLUT1 (Fig. 5a, b), while the endoneurial blood vessels express GLUT1 only (142). Ultrastructually, the MCT1 and GLUT1 immunoreactivities in the thick perineurium show an intensity gradient decreasing towards the innermost layer.…”

Section: The Peripheral Nervous Systemmentioning

confidence: 91%

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Cellular distributions of monocarboxylate transporters: a review

Iwanaga

Kishimoto

2015

Biomed. Res.

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Lactate and ketone bodies play important roles as alternative energy substrates, especially in conditions with a decreased utility of glucose. Short-chain fatty acids (acetate, propionate, and butyrate), produced by bacterial fermentation, supply most of the energy substrates in ruminants such as the cow and sheep. These monocarboxylates are transfered through the plasma membrane by proton-coupled monocarboxylate transporters (MCTs) and sodium-coupled MCTs (SMCTs). To reveal the metabolism and functional significance of monocarboxylates, the cellular localization of MCTs and SMCTs together with the expressed intensities holds great importance. This paper reviews the immunohistochemical localization of SMCTs and major MCT subtypes throughout the mammalian body. MCTs and SMCTs display a selective membrane-bound localization with porality. In contrast to the limited expression of SMCTs in the intestine and kidney, MCTs display a broader distribution pattern than GLUTs. The brain, kidney, placenta, and male genital tract express multiple subtypes of the MCT family. Determination of the cellular localization of MCTs is most controversial in the brain, possibly due to regional differences and the transcriptional modification of MCT proteins. Information on the localization of MCTs and SMCTs aids in understanding the nutrient absorption and metabolism throughout the mammalian body. In some cases, the body may use monocarboxylates as signal molecules, like hormones.

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Section: The Peripheral Nervous Systemsupporting

confidence: 61%

Section: The Peripheral Nervous Systemmentioning

confidence: 87%

Section: The Peripheral Nervous Systemmentioning

confidence: 91%

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Cellular distributions of monocarboxylate transporters: a review

Iwanaga

Kishimoto

2015

Biomed. Res.

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“…The perineurium and the vascular endothelium together form the blood-nerve barrier, and both are rich in GLUT1. This isoform mediates transport of glucose to the peripheral nerves (122). Thus, under conditions of hyperglycemia related to diabetes, increased glucose transport across this barrier may mediate peripheral neuropathy.…”

Section: Blood-retinal and Blood-neural Barrier Glut1mentioning

confidence: 99%

Will the original glucose transporter isoform please stand up!

Carruthers

DeZutter

Ganguly

et al. 2009

American Journal of Physiology-Endocrinology and Metabolism

182

190

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Monosaccharides enter cells by slow translipid bilayer diffusion by rapid, protein-mediated, cation-dependent cotransport and by rapid, protein-mediated equilibrative transport. This review addresses protein-mediated, equilibrative glucose transport catalyzed by GLUT1, the first equilibrative glucose transporter to be identified, purified, and cloned. GLUT1 is a polytopic, membranespanning protein that is one of 13 members of the human equilibrative glucose transport protein family. We review GLUT1 catalytic and ligand-binding properties and interpret these behaviors in the context of several putative mechanisms for protein-mediated transport. We conclude that no single model satisfactorily explains GLUT1 behavior. We then review GLUT1 topology, subunit architecture, and oligomeric structure and examine a new model for sugar transport that combines structural and kinetic analyses to satisfactorily reproduce GLUT1 behavior in human erythrocytes. We next review GLUT1 cell biology and the transcriptional and posttranscriptional regulation of GLUT1 expression in the context of development and in response to glucose perturbations and hypoxia in blood-tissue barriers. Emphasis is placed on transgenic GLUT1 overexpression and null mutant model systems, the latter serving as surrogates for the human GLUT1 deficiency syndrome. Finally, we review the role of GLUT1 in the absence or deficiency of a related isoform, GLUT3, toward establishing the physiological significance of coordination between these two isoforms. glucose transport; facilitated diffusion; major facilitator superfamily protein; bloodbrain barrier; placenta; diabetes; glucose transporter 1 deficiency syndrome; development MOST CELLS TRANSPORT SUGARS rapidly down the prevailing concentration gradient into or out of the cell. This equilibrative transport process is mediated by a family of sugar transporters called GLUTs. GLUT1 was the first glucose transporter isoform to be identified, purified (66, 132), and cloned (93) and is one of 13 proteins that comprise the human equilibrative glucose transporter family (63). GLUT1 is a membrane-spanning glycoprotein containing 12 transmembrane domains with a single N-glycosylation site, and its gene is located on chromosome 1 (1p35-31.3) (93). GLUT1 is expressed at the highest levels in the plasma membranes of proliferating cells forming the early developing embryo, in cells forming the blood-tissue barriers, in human erythrocytes and astrocytes, and in cardiac muscle (86). Having a catalytic turnover of ϳ1,200/s (115), glucose transporter 1 (GLUT1) provides an efficient pathway for cellular import and export of glucose. In addition, GLUT1 transports galactose and ascorbic acid (81,107). This review examines the catalytic properties, structure, molecular regulation, and physiology of GLUT1. GLUT1 CATALYTIC PROPERTIES Facilitated DiffusionThe cytoplasm of most cells equilibrates rapidly with nonmetabolizable extracellular sugars. This process is mediated by sugar transport proteins that catalyze unidirectional sugar up...

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“…The specificity of immunoreactions on sections was confirmed according to conventional procedures, including absorption tests. The ylate-dependent energy system by the expression profiles of MCTs, as has been shown in the female reproductive organ (19), placenta (25), and nervous systems (32,35). Adult stem cells are present in most self-renewing tissues, represented by the intestinal epithelium, the skin, and the hematopoietic organ.…”

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confidence: 94%

Intensified expressions of a monocarboxylate transporter in consistently renewing tissues of the mouse

2011

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Monocarboxylates-lactate and ketone bodies-can compensate for glucose as energy sources under certain physical conditions. To identify the main energy source used in self-renewing tissues, expression profiles of monocarboxylate transporters (MCTs) were mainly investigated immunohistochemically in the gastrointestinal tract, skin, and bone marrow of mice, with reference to glucose transporters. In the small intestine, MCT1-immunoreactive epithelial cells accumulated in crypts with a selective immunolabeling along the basolateral membrane of cells. BrdU-labeled dividing cells were included in the cryptal MCT1-immunoreactive foci. The skin displayed an intense and extensive immunoreactivity for MCT1 in the hair bulge, which gives rise to the epidermis, hair, and sebaceous gland. The stratified squamous epithelium in the esophagus contained MCT1-immunoreactive cells in the basal layer but frequently lacked GLUT1-immunoreactive cells. The bone marrow was largely immunoreactive for MCT1 but not for GLUT1, suggesting the active production and utilization of monocarboxylates for hematopoiesis under hypoxic conditions. These findings support the idea that monocarboxylates are favorite energy sources in self-renewing tissues.Mammals use two kinds of energy substrates, glucose and monocarboxylates. The latter includes lactate, acetate, ketone bodies, and others. These monocarboxylates, which are intermediate metabolites, provide a "ready-to-use" fuel in most cells or are converted into glucose (gluconeogenesis) and fatty acids (lipogenesis). They can compensate for glucose as an energy source under several physical conditions such as fasting, diabetes, and the neonatal period (16,35). The production of monocarboxylates does not need oxygen; therefore, they may be evolutionally older (more primitive) energy substrates than glucose, since the concentration of O 2 was low in ancient times. Hypoxic conditions exist in the bone marrow and tumors where proliferative activities are high, and some signals of hypoxia stimulate the cell proliferation (7, 9). There is a possibility that the monocarboxylates produced by anaerobic glycolysis are favorite energy sources for cell growth in selfrenewing tissues and tumors. In mammals, a membrane-bound transporter family mediates the uptake and excretion of monocarboxylates. A representative transporter for monocarboxylates is the monocarboxylate transporter (MCT) and the classified SLC16 gene family. MCT is a H + -coupled, electroneutral, and bi-directional transporter composed of twelve transmembrane domains with intracellular N and C terminal domains (10, 11). To date, fourteen MCT isoforms-each having a unique distribution and different sequence homology-have been identified in mammals, though only four (MCT1-MCT4) have been demonstrated experimentally to facilitate the proton-linked transport of metabolically important monocarboxylates (14,23). It is possible to evaluate the existence of a monocarbox-

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Histochemical demonstration of a monocarboxylate transporter in the mouse perineurium with special reference to GLUT1

Cited by 31 publications

References 37 publications

<b>Cellular distributions of monocarboxylate transporters: a r</b><b>eview </b>

<b>Cellular distributions of monocarboxylate transporters: a r</b><b>eview </b>

Will the original glucose transporter isoform please stand up!

Intensified expressions of a monocarboxylate transporter in consistently renewing tissues of the mouse

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