SLC22A5 Membrane Protein Introduction

Introduction of SLC22A5

Solute carrier family 22 member 5 (SLC22A5), also known as organic cation/carnitine transporter 2 (OCTN2), which in humans is encoded by the SLC22A5 gene. SLC22A5 is a membrane transport protein associated with primary carnitine deficiency. SLC22A5 is widely distributed in the body, such as in the kidney, heart, skeletal muscle, placenta, small intestine, liver and brain. The most important physiological function of SLC22A5 is to mediate transmembrane transport of carnitine with a high affinity, and its transport process also depends on the difference in sodium ion concentration inside and outside the membrane.

Basic Information of SLC22A5
Protein Name	Solute carrier family 22 member 5
Gene Name	SLC22A5
Aliases	High-affinity sodium-dependent carnitine cotransporter, Organic cation/carnitine transporter 2, OCTN2
Organism	Homo sapiens (Human)
UniProt ID	O76082
Transmembrane Times	12
Length (aa)	557
Sequence	MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF

Function of SLC22A5 Membrane Protein

SLC22A5 is the main transporter of carnitine in renal reabsorption, which is closely related to body fat metabolism. The weakening or loss of SLC22A5 function may cause systemic carnitine deficiency and cause diseases of the myocardium, central nervous system and musculoskeletal. SLC22A5 expressed on cardiac vascular endothelial cells and skeletal muscle cells are critical for maintaining carcass concentration balance and normal organ function in the body. In addition, the expression level of SLC22A5 in the small intestine is similar to that of the small peptide transporter PEPT1. SLC22A5 mainly participates in the intestinal absorption process of carnitine. Primary carnitine deficiency is an autosomal recessive genetic disease mainly caused by functional defects of SLC22A5 and it is different from secondary carnitine deficiency. OCTNs are associated with diseases such as diabetes and obesity, which also means that SLC22A5, as the main transporter of carnitine, may become a biological target for glucose metabolism diseases.

Fig.1 SLC22A5 transports carnitine into the mitochondrial matrix.

Application of SLC22A5 Membrane Protein in Literature

Luo J.A., et al. Phytochemicals Mediate the Expression and Activity of OCTN2 as Activators of the PPARγ/RXRα Pathway. Front Pharmacol. 2016, 7: 189. PubMed ID: 27445823

This article showed that kaempferol, curcumin, and puerarin functioned as PPARγ ligands to potentiate the expression and activity of OCTN2.
Zhou X., et al. The pro-inflammatory cytokine tumor necrosis factor α stimulates expression of the carnitine transporter OCTN2 (novel organic cation transporter 2) and carnitine uptake via nuclear factor-κB in Madin-Darby bovine kidney cells. J Dairy Sci. 2015, 96(6): 3840-3848. PubMed ID: 25892691

This article demonstrated that bovine OCTN2 expression and carnitine uptake were regulated by NF-κB.
Qu Q., et al. Different involvement of promoter methylation in the expression of organic cation/carnitine transporter 2 (OCTN2) in cancer cell lines. PLoS One. 2013, 8(10): e76474. PubMed ID: 24146874

The authors revealed that OCTN2 played an important role in cancer cell uptake of chemotherapeutics, and thus treatment efficacy. So, pretreatment with a demethylating reagent was a possible strategy for optimizing pharmacotherapies against cancers.
Castelli M.P., et al. Human OCTN2 (SLC22A5) is down-regulated in virus- and nonvirus-mediated cancer. Cell Biochem Funct. 2012, 30(5): 419-425. PubMed ID: 22374795

This article revealed that OCTN2 transporter was generally down-regulated in virus and nonvirus-mediated epithelial cancers, probably via methylation of its promoter region.
Furuichi Y., et al. Muscle contraction increases carnitine uptake via translocation of OCTN2. Biochem Biophys Res Commun. 2012, 418(4): 774-779. PubMed ID: 22310714

This article revealed that muscle contraction facilitated carnitine uptake in skeletal muscles, possibly via the contraction-induced translocation of its specific transporter OCTN2 to the plasma membrane.

SLC22A5 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC22A5 antibody development services.

Creative Biolabs' skillful scientists are glad to leverage our expertise and advanced technologies to help you with the member protein research. If you are interested, please feel free to contact us for more details.

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