PATOJENİK DERMAFİTLERİN MONOFLOROMETİLAGMATİNE DUYARLILIK MEKANİZMASININ ARAŞTIRILMASI

Poliaminler, bitki, hayvan, bakterileri ve mantarların normal büyüme ve gelişmesi için gerekli olan temel alifatikkatyonlardır. Microsporumve Trichophytonsırasıyla ornitin ODC ve arginin-dekarboksilazın ADC suicideinhibitörleri olan diflorometilarjinin DFMA ve diflorometilornitin DFMO büyüme inhibisyonuna in-vitroduyarlılık göstermişlerdir. Bununla birlikte DFMA’ya olan duyarlılığı destekleyecek bilgiler net değildir. Bu konudayapılan başlangıç çalışmalarda, her iki mantarın ekstrelerinde gözlenebilir. ADC, arginaz veya agmatin ürehidrolaz AUH ’a olan aktiviteyi saptayamamışlardır. Bizim çalışmamızda arginaz, AUH ve ADC aktivitelerinin tekrarincelenmesinin yanı sıra dermatofitlerin AUH’ı yok edici bir inhibitör olan Monoflorometilagmatine tithylagmatine olanduyarlılıkları incelenmiştir. Elde ettiğimiz bulgular dermatofitlerde AUH’ın olduğu gibi arginazın da mevcudiyetinigöstermiş ve ayrıca Microsporum,Trichophyton’da DFMA ve DFMAg açısından her iki mantarın arginaz veAUH enzimlerinin Kmsve Kıs Kinetiği=Lineweawer-Burke değerleri bulunmuştur

Anahtar Kelimeler:

Dekarboksilaz, monoflorometilagmatin, mikrosporum, poliamamin sentezi

The Nature Of The Susceptibility Of Pathogenic Dermatophytes To Monofluoromethylagmatıne MFMag

Polyamines are essential aliphatic cations required for normal growth and develepment in plants, animals,bacteria and fungi. M i c r o s p o r u m, and T r i c h o p h y t o nwere in-vitro susceptible to growth inhibition bydifluoromethylornithine DFMO and difluoromethylarginine DFMA , suicide inhibitors of the ornithine ODC andarginine decarboxylase ADC respectively. However, the basis for the susceptibility to DFMA was unclear as initialstudies failed to find detectable ADC, arginase nor agmatine ureohydrolase AUH activities in extracts fromeither genus. We have re-examined the arginase, AUH and ADC activities as well as dermatophytes’susceptibilities to MFMAg, a suicide inhibitor of AUH. The data demonstrated existence of arginase as well asAUH’ in these dermatophytes and found the Lineweayer-Burke Kmsand K1sof arginase and AUH withrespect to DFMA and MFMAg in both Microsporum, and Trichophyton

Keywords:

Decarboxylase, monofluoromethylagmatine, Microsporum, polyamines,

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l-Tabor, CW, Tabor H. Polyamines in microorganism. Microbiol Rev 1985; 49: 81-89.
McCann PP, Pegg AE, Sjoerdsma A. Inhibition of polyamine metabolism. Orlando: Academic Press, 1987.
Szumanski MBW, Boyle SM. Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli. J Bact 1996; 172: 538.
Boyle SM, Sriranganathan N, Cordes D. Susceptibility of Microsporumand Trichophytonspecies to suicide inhibitors of polyamine biosyntheses. J Med Vet Mycol 1998; 26: 227.
Pfaller MA, Riley J. Gerarden T. Polyamine depletion and growth inhibition in C.albicansand C.tropicalisby α-difluoromethylornithine and Cyclohexylamine. J Vet Med Mycol 1988; 26:119-126.
Birecka H. Garraway MO, Baumann RJ, McCann PP. Inhibition of ornithine decarboxylase and growth of the fungus Helminthosporium maydis. Plant Physiol 1986; 80: 798-800.
Mussel H, Osmeloski J, Wettlaufr S. Weinstein LH. Suppression of Verticullium wilt of tomatoes by difluoromethylornithine, a suicidal inhibitor of polyamine biosyntheses. Plant Dis 1987; 7: 3134-3150.
Rajam MV, Galston AW. The effects of some polyamine biosynthetic inhibitors on growth and morphology of phytopathogenic fungi. Plant Cell Physiol 1985; 26: 683-692.
Rajam MV, Weinstein LH, Galstone AW. Prevention of a plant disease by specific inhibition of fungal polyamine biosynthesis. Proc Natl Acad Sci USA 1985; 82:6874-6878.
West HM, Walters DR. The effects of polyamine biosynthesis inhibitors on infection of Hordeum vulgareL. by Erysiphe graminisf.sp. hordeiMarchal. New Phytolog 1988;110: 193-200.
Rajam MV, Galstone AW. The effects of some polyamine biosynthetic inhibitors on growth and morphology of phytopathogenic fungi. Plant Cell Physiol 1985; 26: 683.
Slocum RD, Bilonti AJ, McCann P, Feirer R. DL-α-Difluoromethyl [3,4-3H] arginine metabolism in tobacco and mammalian cells. Biochem J 1988; 255: 197-202.
Slocum RD, Galston AW. Arginase-mediated hydrolysis of DFMA to DFMO in vivo. Plant Physiol 1985; 45: 4.
Gruhn CM, Boyle SM. Biochemical and morphological effects of polyamine biosynthesis inhibitors on Trichophytonand Microsporum. J Med Vet Mycol 1991; 29: 63-72.
Ruegy UT. Russell AS. A rapid and sensitive assay for arginase. Anal Biochem 1980;102: 206.
Boyle SM, Gruhn CM. Biochemical and morphological effects of polyamine biosynthesis inhibitors on Trichophytonand Microsporum. J Med Vet Mycol 1991; 29:29-32.
Vissers S, Legrain C, Wiame JM. Control of futile urea cycle by arginine feedback inhibition of ornithine carbamoyltransferase in Agrobacterium tumefaciencesand Rhizobia.Eur J Biochem 1986; 155: 507-511.
Khan AJ, Minocha SC. Biosynthetic arginine decarboxylase in phytopathogenic fungi. Life Sci 1989; 44: 1222.
Bacchi GJ. Content, synthesis and function of polyamines in trypanosomatids: Relationship to chemotherapy. J Protozool 1981; 28: 20-27.
Pegg AE, McCann PP. Polyamine metabolism and function. Cell Physiol 1992; 243: 212-221.
Stevens L, Winter MD. Spermine, spermidine and putrescine in fungal development. Adv Microbiol Physiol 1997; : 63-148.
Kierszenbaum F, Wirth JJ, McCann PP, Sjoerdsma A. Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells. Proc Natl Acad Sci USA 1987; 84: 4278-4282.