TRPV2 Membrane Protein Introduction

Introduction of TRPV2

Transient receptor potential cation channel subfamily V member 2, a member of transient receptor potential (TRP) superfamily, is encoded by the TRPV2 gene. TRPV2 consists of a large N-terminal cytoplasmic domain (~390 residues), followed by six transmembrane segments (~250 residues) containing a pore-forming loop, and a C-terminal cytoplasmic domain (~100 residues). The S1-S4 segments and the N- and C-terminal cytoplasmic domains are modulating domains that are important to the gating of the channel, with the S5-S6 segments defining the pore and selectivity filter. TRPV2 is a homo-tetrameric N-glycosylated protein that translocates from intracellular membrane compartments to the plasma membrane after stimulation of the phosphatidylinositol 3-kinase (PI3K) and other kinase signaling pathways. Two compounds have shown promising results as more specific modulators of TRPV2: probenecid and tranilast, as activator and inhibitor, respectively. There is a broad expression of TRPV2 in the lymph nodes, spleen, lung, appendix, and placenta, with the highest expression in the lungs.

Basic Information of TRPV2
Protein Name	Transient receptor potential cation channel subfamily V member 2(TrpV2)
Gene Name	TRPV2, VRL
Aliases	Osm-9-like TRP channel 2 (OTRPC2), Vanilloid receptor-like protein 1 (VRL-1)
Organism	Homo sapiens (Human)
UniProt ID	Q9Y5S1
Transmembrane Times	6
Length (aa)	764
Sequence	MTSPSSSPVFRLETLDGGQEDGSEADRGKLDFGSGLPPMESQFQGEDRKFAPQIRVNLNYRKGTGASQPDPNRFDRDRLFNAVSRGVPEDLAGLPEYLSKTSKYLTDSEYTEGSTGKTCLMKAVLNLKDGVNACILPLLQIDRDSGNPQPLVNAQCTDDYYRGHSALHIAIEKRSLQCVKLLVENGANVHARACGRFFQKGQGTCFYFGELPLSLAACTKQWDVVSYLLENPHQPASLQATDSQGNTVLHALVMISDNSAENIALVTSMYDGLLQAGARLCPTVQLEDIRNLQDLTPLKLAAKEGKIEIFRHILQREFSGLSHLSRKFTEWCYGPVRVSLYDLASVDSCEENSVLEIIAFHCKSPHRHRMVVLEPLNKLLQAKWDLLIPKFFLNFLCNLIYMFIFTAVAYHQPTLKKQAAPHLKAEVGNSMLLTGHILILLGGIYLLVGQLWYFWRRHVFIWISFIDSYFEILFLFQALLTVVSQVLCFLAIEWYLPLLVSALVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLLIYLVFLFGFAVALVSLSQEAWRPEAPTGPNATESVQPMEGQEDEGNGAQYRGILEASLELFKFTIGMGELAFQEQLHFRGMVLLLLLAYVLLTYILLLNMLIALMSETVNSVATDSWSIWKLQKAISVLEMENGYWWCRKKQRAGVMLTVGTKPDGSPDERWCFRVEEVNWASWEQTLPTLCEDPSGAGVPRTLENPVLASPPKEDEDGASEENYVPVQLLQSN

Function of TRPV2 Membrane Protein

In homo sapiens, TRPV2 is broadly expressed in numerous organ systems where it displays tissue-specific physiological functions. TRPV2 channels can open by noxious temperatures greater than 52°C. TRPV2 initially was characterized as a noxious heat sensor channel, but more evidence suggests its importance in various osmosensory and mechanosensory mechanisms. TRPV2 is involved in axon outgrowth, consistent with its cellular localization in the axon shafts and growth cones in embryonic DRG sensory and spinal motor neurons. TRPV2 functions as a mechanosensor in the intestine where it contributes to transit within the gastrointestinal tract. Recently, many reports have indicated that TRPV2 is involved in the disease progression of bladder or prostate cancer. It has been found that there is a significant relationship between the overexpression of TRP genes, including TRPV2, and the survival of patients with glioblastoma.

TRPV2 Membrane Protein Introduction

Application of TRPV2 Membrane Protein in Literature

Kojima I. and Nagasawa M. TRPV2. Handbook of Experimental Pharmacology. 2014, 222:247-72. PubMed ID: 24756709

This article finds that the expression of TRPV2 is high in some types of cells including neurons, neuroendocrine cells, immune cells involved in innate immunity, and certain types of cancer cells. TRPV2 may modulate various cellular functions in these cells.
Lorin C., et al. Dystrophic cardiomyopathy: role of TRPV2 channels in stretch-induced cell damage. Cardiovasc Research. 2015, 106(1):153-62. PubMed ID: 25616416

This article suggests a major role of TRPV2 channels in the cardiac dystrophic Ca²⁺ signaling pathology and provides compelling evidence that the TRPV2 proteins form a subunit of stretch-activated channels.
Shibasaki K. Physiological significance of TRPV2 as a mechanosensor, thermosensor and lipid sensor. J Physiol Sci. 2016, 66(5):359-65. PubMed ID: 26841959

This article suggests that TRP channels contribute to the progression and survival of glioblastoma patients. Thus, future studies into the physiological function of TRPV2 may reveal new mechanisms behind several diseases.
Zanou N., et al. Osmosensation in TRPV2 dominant negative expressing skeletal muscle fibres. J Physiol. 2015, 593(17):3849-63. PubMed ID: 26108786

This article reveals that TRPV2 is involved in osmosensation in skeletal muscle fibres, acting in concert with P-SPAK-activated NKCC1.
Kokubun S., et al. Distribution of TRPV1 and TRPV2 in the human stellate ganglion and spinal cord. Neurosci Lett. 2015, 590:6-11. PubMed ID: 25641129

This article suggests that the human stellate ganglion and spinal cord probably have TRPV1-or TRPV2-IR sympathetic pathway.

TRPV2 Preparation Options

Membrane protein studies have advanced significantly over the past few years. Based on our versatile Magic™ membrane protein production platform, we could offer a series of membrane protein preparation services for worldwide customers in reconstitution forms as well as multiple active formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-TRPV2 antibody development services.

During the past years, Creative Biolabs has successfully generated many functional membrane proteins for our global customers. We are happy to accelerate the development of our clients’ programs with our one-stop, custom-oriented service. For more detailed information, please feel free to contact us.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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