The localization of guanylate cyclase in rat small intestinal epithelium

Jonge, Hugo R. de

doi:10.1016/0014-5793(75)80028-7

Cited by 79 publications

(30 citation statements)

References 28 publications

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“…Assay of guanylate cyclase activity and purification of the labeled product were done essentially as before [7]. [14] it was assumed that all GTP was present as the MnGTP 2-complex.…”

Section: Methodsmentioning

confidence: 99%

“…Our previous work [7] showed that the major part of the intestinal enzyme activity is associated with the microvillous membrane of the brushborder, the remaining part being localized in the basal-lateral plasma membranes. Accordingly, proliferative crypt cells displayed a much lower guanylate cyclase activity than the mature villous cells [7]. Since intestinal brushborders: which are easily obtained in a relatively pure state, provide one of the richest sources of particulate guanylate cyclase in the rat, the kinetic and other properties of this enzyme may be measured accurately even in the absence of an activating detergent used in other studie s [6,8].…”

Section: Introductionmentioning

confidence: 98%

“…The function of cyclic GMP in the small intestine is however entirely unknown. Its level as well as the activity of the particulate form of the enzyme guanylate cyclase in rat small intestinal epithelium are relatively high as compared to most other mammalian tissues [4][5][6][7]. The soluble form of guanylate cyclase which, at least in rat heart [6] and lung [8], clearly differs from the particulate enzyme in kinetic and physical properties, is nearly absent in small intestinal mucosa [4,6,7].…”

Section: Introductionmentioning

confidence: 99%

“…Its level as well as the activity of the particulate form of the enzyme guanylate cyclase in rat small intestinal epithelium are relatively high as compared to most other mammalian tissues [4][5][6][7]. The soluble form of guanylate cyclase which, at least in rat heart [6] and lung [8], clearly differs from the particulate enzyme in kinetic and physical properties, is nearly absent in small intestinal mucosa [4,6,7]. Our previous work [7] showed that the major part of the intestinal enzyme activity is associated with the microvillous membrane of the brushborder, the remaining part being localized in the basal-lateral plasma membranes.…”

Section: Introductionmentioning

confidence: 99%

“…The soluble form of guanylate cyclase which, at least in rat heart [6] and lung [8], clearly differs from the particulate enzyme in kinetic and physical properties, is nearly absent in small intestinal mucosa [4,6,7]. Our previous work [7] showed that the major part of the intestinal enzyme activity is associated with the microvillous membrane of the brushborder, the remaining part being localized in the basal-lateral plasma membranes. Accordingly, proliferative crypt cells displayed a much lower guanylate cyclase activity than the mature villous cells [7].…”

Section: Introductionmentioning

confidence: 99%

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Properties of guanylate cyclase and levels of cyclic GMP in rat small intestinal villous and crypt cells

Jonge

1975

FEBS Letters

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“…Assay of guanylate cyclase activity and purification of the labeled product were done essentially as before [7]. [14] it was assumed that all GTP was present as the MnGTP 2-complex.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Properties of guanylate cyclase and levels of cyclic GMP in rat small intestinal villous and crypt cells

Jonge

1975

FEBS Letters

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Studies of N-methyl-N′–nitro-N-nitrosoguanidine action on the guanylate cyclase-guanosine 3′5′ monophosphate system of isolated colonic epithelial cells

DeRubertis¹,

Craven²,

Saito³

1980

Cancer

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The effects of the colon carcinogen N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) on the guanylate cyclase (GC)-guanosine 3'5' monophosphate (cGMP) system were examined in epithelial cells isolated from the distal colon of the rabbit. MNNG (1 p M to 1 mM) increased cGMP accumulation 2-to 50-fold within 5 minutes, without producing concurrent increases in adenosine 3'5' monophosphate. The action of MNNG to increase cGMP was expressed in the ahsence of both extracellular calcium and molecular 02. cGMP was also increased hy nitrite and by nitric oxide (NO), a reactive derivative of MNNG and nitrite. Increases in cGMP induced hy MNNG in colonic epithelial cells were suppressed by retinol and hutylated hydroxyanisole (BHA), whereas the effect of a submaximal concentration of MNNG was potentiated by 0.1 mM deoxycholate. MNNG, nitrite, and NO activated GC in the 100,000 x g particulate fraction, the predominant form of the enzyme in colonic epithelial cells. However, this action was expressed only in the presence of an appropriate concentration of a reducing agent (dithiothreitol, glutathione or ascorbate), which concurrently led to formation of a paramagnetic complex with the ESR spectral characteristics of NO-heme in colonic particulate fractions exposed to MNNG. By contrast, several preformed paramagnetic NO-hemeprotein complex (NOhemoglobin, NO-catalase and NO-cytochrome P-450) increased particulate GC of colonic epithelial cells in the absence of added co-factors. These observations suggest that formation of NO-heme may be involved in the process by which MNNG activates particulate GC of colonic epithelium. Retinol, BHA, high concentrations of dithiothreitol, and the thiol blocker N-ethylmaleimide suppress the effects of both MNNG and of preformed NO-heme complexes to activate GC. Thus, the effects of these inhibitors may be expressed, at least in part, at point(s) in the enzyme activation pathway distal to generation of NO-heme from MNNG. Stimulation of the GC system of colonic epithelium by MNNG, as well as the inhibition of this effect by antioxidants (BHA and retinol) and its potentiation by a putative co-carcinogen (deoxycholate) could play a role in the expression of the oncogenic actions of MNNG in colon.

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Toxins which Activate Guanylate Cyclase: Heat‐Stable Enterotoxins

Rao¹

1985

Novartis Foundation Symposia

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The localization of guanylate cyclase in rat small intestinal epithelium

Cited by 79 publications

References 28 publications

Properties of guanylate cyclase and levels of cyclic GMP in rat small intestinal villous and crypt cells

Properties of guanylate cyclase and levels of cyclic GMP in rat small intestinal villous and crypt cells

Studies of N-methyl-N′–nitro-N-nitrosoguanidine action on the guanylate cyclase-guanosine 3′5′ monophosphate system of isolated colonic epithelial cells

Toxins which Activate Guanylate Cyclase: Heat‐Stable Enterotoxins

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