Prof. R. J. D. Graham

Smith, W. W.

doi:10.1038/166976a0

Cited by 18 publications

(25 citation statements)

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“…TRPV3: a thermosensor? TRPV3 (ENST00000301365), which shares 43% sequence similarity with the first identified TRPV1, was cloned by three groups (16)(17)(18). After its identification, it appeared as a surprise that this channel was not highly expressed in the sensory dorsal root (DRG) or trigeminal (TG) ganglia (at least in rodents).…”

Section: Trpv Familymentioning

confidence: 99%

“…Instead, TRPV3 was found to be most abundantly expressed in the skin, especially in epidermal and hair follicle keratinocytes, as well as in the tongue, testis, cornea, the distal colon, human larynx and inner ear (17)(18)(19)(20)(21)(22)(23)(24). TRPV3, expressed by mouse epidermal keratinocytes (or in heterologous expression systems), was found to be activated by innocuous warm temperatures above 33°C (16)(17)(18). Yet, the role of TRPV3 as a thermosensor is still not clearly understood.…”

Section: Trpv Familymentioning

confidence: 99%

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TRPV3: a ‘more than skinny’ channel

Nilius

Bı́ró

2013

Experimental Dermatology

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The skin is our largest organ serving different tasks from barrier formation through somatosensing to hair development. Recently, members of the large trp (Transient Receptor Potential, TRP) gene family encoding proteins that form cation selective ion channel have been identified to play a crucial role in skin functions. Within the 28 different mammalian TRP channels, TRPV3 might be the most important member in the skin. This review gives an overview on functional properties of TRPV3 in skin physiology and in certain skin diseases. TRP channels: an introductionIn 1969, a Drosophila mutant was discovered which was defective in light sensing and exhibited only transient light-induced receptor potentials (TRP) instead the normal maintained response (1). This finding was explained by a defect in an ion channel and triggered the discovery of the trp gene family which encodes TRP channels (for the history of this discovery see (2-4)). The TRP channel superfamily contains 28 mammalian members (27 in human) subdivided in six subfamilies which all permeate cations (5,6). TRP channels -which probably function mostly as hetero-or homotetramers (7,8) (more detailed information see in TRP channel data base Clapham/Owsianik/Nilius (9)) -are located in the plasma membrane (PM) as cation entry pores and generate upon activation cell depolarization; this can result in activation or inactivation of voltage-dependent ion channels, thereby modulating the driving force of ion flux through channels and transporters. Some TRPs also act as intracellular ion channels, mainly as Ca 2+ release channels, in several cell organelles such as lysosomes, endosomes, Golgi network, endoplasmic reticulum and synaptic vesicles (10). TRPV familyMembers of the TRPV (vanilloid) family comprise six ion channels based on homology. Four groups can be identified: TRPV1/ TRPV2, TRPV3, TRPV4, and TRPV5/6. This family is named after the first mammalian member of the TRPV subfamily, which binds vanilloids (e.g. capsaicin) and was first coined as vanilloid receptor-1 (VR1) (6,11). Members of the TRPV family function as homo and/or heterotetrameric complexes but can also heteromultimerize with other TRP channels such as TRPC1 and TRPP2 (7,12,13).Among the TRPVs channels, TRPV1, 2, 3 and 4 have striking temperature sensitivities. Indeed, TRPV1 is activated at >43°C; TRPV2 at >52°C; TRPV3 at >33°C; and TRPV4 at >30°C (14). These thermo-TRPVs are modestly permeable to Ca 2+ , whereas TRPV5 and TRPV6 are the only highly Ca 2+ selective channels in the TRP family. Nevertheless, functions of all of these channels are tightly regulated by the intracellular Ca 2+ concentration ([Ca 2+ ] i ) and phosphoinositides (15).With respect to skin physiology and pathophysiology, probably TRPV3 is the most important TRPV channel. Therefore, the cutaneous role of TRPV3 will be detailed in this review.

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Section: Trpv Familymentioning

confidence: 99%

Section: Trpv Familymentioning

confidence: 99%

TRPV3: a ‘more than skinny’ channel

Nilius

Bı́ró

2013

Experimental Dermatology

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“…The development of antibodies to tuberculinsensitized cells following intradermal tuberculin inoculations was described by Smith and Scott (1950) and by Gerstl, Kirsh, Andros, Winter, and Kidder (1952) and would, if confirmed, have to be taken into account in the interpretation of the test. In the cases reported here, however, neither large intramuscular doses of tuberculin nor previous Mantoux testing affected the lysis test, although a small rise in the haemagglutinin titres was sometimes detected.…”

Section: Effect On the Haemagglutination And Lysis Tests Of Previous mentioning

confidence: 91%

“…Some investigations have been reported of the relationship between haemagglutinin titres and the extent, severity, and prognosis of the tuberculous disease (Gernez-Rieux and Tacquet, 1950b ;Sohier, Juillard, and Trimberger, 1950;Spain, Childress, and Rowe, 1952;Hinson et al, 1952), but much less work has been done on this aspect of the subject with the lytic modification of the test. The results of this series suggest that the lysis titre is related, in part at least, to the activity of the lesion, but the cases were not followed up for long enough to show what other factors may be involved.…”

Section: Effect On the Haemagglutination And Lysis Tests Of Previous mentioning

confidence: 99%

“…Adcock, Haley, and Davey (1951) and Hinson, Jones, and Chamberlin (1952) used the same antigen, but replaced the sheep cells by human Group 0 cells. Sohier, Juillard, and Trimberger (1950) used the purified tuberculin prepared by the Pasteur Institute as the sensitizing antigen, and this was compared with the original extract of Middlebrook and Dubos by Gernez-Rieux and Tacquet (1950a and b), who found a close correspondence between the results obtained. Further modifications were described by Sohier, Trimberger, and Juillard (1950) using human Group 0 Rh-negative cells, the purified tuberculin of the Pasteur Institute as the sensitizing antigen, and a shorter test period.…”

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confidence: 99%

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The Middlebrook--Dubos Haemagglutination Test and Its Haemolytic Modification in the Diagnosis of Tuberculosis

Sherris¹

1953

Journal of Clinical Pathology

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Pseudouridine Deficiency in Transfer Ribonucleic Acids from Escherichia coli Treated with 2-Thiouracil

Gurchinoff¹,

Kaiser²

1973

Biochemistry

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Some of the properties of transfer ribonucleic acid from Escherichia coli B grown in the presence of 2-thiouracil were examined. These transfer ribonucleic acids were shown to be nearly 50% deficient in pseudouridine. The major nucleotide content was essentially unchanged, as were the levels of dihydrouridine, ribothymidine, and 4-thiouridine. No evidence was found for the incorporation of 2-thiouracil.Cosedimentation on sucrose gradients and cochromatography on Sephadex with normal E. coli transfer ribonucleic acids did T A he pyrimidine analog, 2-thiouracil, was first used medicinally in the treatment of hyperthyroidism in the 1940's. Since that time, it has been mainly used as a tool to study cellular metabolism in a variety of systems. In bacteria its reported effects have been somewhat inconsistent. When added to cultures of Escherichia coli, for example, Strandskov and Wyss (1945) reported complete inhibition of growth, whereas other workers noted little or no effect (Amos et al., 1958;Kerbiriou and Hervé, 1972). These inconsistencies probably result from growth under different conditions, such as the concentration of potassium ion in the medium (Amos et al., 1958). The most extensive incorporation of the analog into the RNA of a bacterial system was in Bacillus megaterium, to the extent of about 5 mol % (Hamers, 1956). In E. coli Hamers and Hamers-Casterman (1961) reported SHUra* 1 *replaced 1-2 % of the uracil residues (0.2-0.4 mol %) in RNA.Other workers, including ourselves, have not detected any SHUra incorporation into E. coli RNA (Cardeilhac, 1966;Goodrich and Cardeilhac, 1970;Bauernfeind and Griimmer, 1968). This inability to be extensively incorporated into RNA is apparently not the result of its inability to be converted to the triphosphate form (Amos et al., 1958;Lindsay et al., 1972;Yu et al., 1973).Reports have appeared in the literature which suggest that abnormal proteins are synthesized by E. coli in the presence of SHUra (Hamers and Hamers-Casterman, 1961;Kerbiriou and Hervé, 1972). These findings, particularly those of Kerbiriou and Hervé, strongly indicate that incorporation of SHUra or other modifications of m-or tRNA does occur in the presence of the analog.Our findings suggest that if SHUra incorporation does occur, it must be slight. On the other hand, there is a definite f From the

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Prof. R. J. D. Graham

Cited by 18 publications

References 0 publications

TRPV3: a ‘more than skinny’ channel

TRPV3: a ‘more than skinny’ channel

The Middlebrook--Dubos Haemagglutination Test and Its Haemolytic Modification in the Diagnosis of Tuberculosis

Pseudouridine Deficiency in Transfer Ribonucleic Acids from Escherichia coli Treated with 2-Thiouracil

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