Cyclic AMP and cyclic GMP content and binding in malignancy

Goldberg, Melvin L.; Burke, Gertrude C.; Morris, Harold P.

doi:10.1016/s0006-291x(75)80141-0

Cited by 53 publications

(13 citation statements)

References 23 publications

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“…Similarly, while some rat hepatomas have reduced cAMP or increased cGMP (19,21), in others cAMP has been the same or higher than that of the surrounding liver (18)(19)(20). Moreover, under certain experiment conditions, cAMP has been implicated as a positive rather than negative signal for hepatocyte growth (41,42), and in the rapidly proliferating crypt cells of intestinal mucosa, adenylate cyclase activity has been reported to be higher than that of the more slowly growing superficial cells (43 (46,47), and an altered response pattern to hormonal stimuli (20,35,48,49) have now all been observed in neoplastic tissues. The extent to which such changes occur in colonic carcinomas remains to be determined.…”

Section: Methodsmentioning

confidence: 99%

The content and metabolism of cyclic adenosine 3', 5'-monophosphate and cyclic guanosine 3', 5'-monophosphate in adenocarcinoma of the human colon.

DeRubertis¹,

Chayoth²,

Field³

1976

J. Clin. Invest.

114

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Section: Methodsmentioning

confidence: 99%

The content and metabolism of cyclic adenosine 3', 5'-monophosphate and cyclic guanosine 3', 5'-monophosphate in adenocarcinoma of the human colon.

DeRubertis¹,

Chayoth²,

Field³

1976

J. Clin. Invest.

114

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“…It is therefore intriguing to speculate on a role of endogenous NO in the pathogenesis of gastric ulcer and cancer. Interestingly, cyclic GMP levels are elevated in neoplasms, proliferating tissues, and associated disease states (86)(87)(88)(89).…”

Section: Non-neural Cellsmentioning

confidence: 99%

Mapping of neural nitric oxide synthase in the rat suggests frequent co-localization with NADPH diaphorase but not with soluble guanylyl cyclase, and novel paraneural functions for nitrinergic signal transduction.

Schmidt¹,

Gagné²,

Nakane³

et al. 1992

J Histochem Cytochem.

595

246

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Nitric oxide synthase (NOS Types I-III) generate nitric oxide (NO), which in turn activates soluble guanylyl cyclase (GC-S). The distribution of this NO-mediated (nitrinergic) signal transduction pathway in the body is unclear. A polyclonal monospecific antibody to rat cerebellum NOS-I and a monoclonal antibody to rat lung GC-S were employed to localize the protein components of this pathway in different rat organs and tissues. We confirmed the localization of NOS-I in neurons of the central and peripheral nervous system, where NO may regulate cerebral blood flow and mediate long-term potentiation. GC-S was located in NOSnegative neurons, indicating that NO acts as an intercellular signal molecule or neurotransmitter. However, NOS-I was not confined to neurons but was widely distributed over IntroductionThe intracellular formation of nitric oxide (NO) has been extensively studied in various mammalian tissues. NO (1,2), or a labile intermediate that is able to release NO, is generated from a terminal guanidino nitrogen of L-arginine (3-5) by a family of NO synthases (NOS; EC 1.14.23). L-Citrulline is the byproduct of this metabolic pathway. NO is the first messenger molecule of a signal transduction pathway (Figure 1). Although other targets for NO Supported by research grants DK 30787 and H I . 28474 several non-neural cell types and tissues. These included glia cells, m a d densa of kidney, epithelial cells of lung, uterus, and stomach, and islets of Langerhans. Our findings suggest that NOS-I is the most widely distributed isoform of NOS and, in addition to its neural functions, regulates secretion and non-vascular smooth muscle function. With the exception of bone tissue, NADPH-diaphorase (NADPH-d) activity was generally co-localized with NOS-I immunoreactivity in both neural and non-neural cells, and is a suitable histochemical marker for NOS-I but not a selective neuronal marker. (J Histochem Cytochem 40:1439-1456, 1992) KEY WORDS: Cyclic GMP; Brain; Pancreas; Kidney; Stomach; Lung; Uterus; Bone; Epithelium; Endometrium. exist (6), its main mechanism of action involves binding to and activation of soluble guanylyl cyclase (GC-S; GTP pyrophosphatelyase (cyclizing), EC 4.6.1.2) (7), which then forms the second messenger molecule guanosine 3',5'-cyclic monophosphate (cGMP).NOS have been purified and characterized from brain (8-14), macrophages (15,16), and endothelial cells (17), and recently also from human cerebellum (18). Molecular cloning has provided clear evidence that brain (19) and macrophage (20) NOS are products of different genes. The relation between brain and endothelial NOS is unclear. Another polydonal antibody raised against rat brain NOS (21) was reported to bind to endothelial cell matrix, and the authors suggested that brain and endothelial NOS are highly homologous if not identical (22). Conversely, endothelial NOS was reported by our laboratory to differ from brain NOS with respect to molecular mass and subcellular location (17) and we proposed a classification of at least three types...

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“…Since glucocorticoids do not affect the mitotic activity of regenerating liver [19], our present results suggest that the loss of the glucocorticoid-independent response of TAT to DBcAMP is characteristic of the proliferating cells or calls ready to proliferate. In view of the recent finding that a specific cyclic AMP-binding site is deficient from hepatoma cells [20][21][22][23] and that during the developmental period of rat liver the cyclic AMP-binding activity changes [24], the cyclic AMP-binding protein was assayed on the cytosol fractions from the regenerating liver of adrenalectomized rats 18 h after partial hepatectomy. reported to be present in rat liver cytosol [22,25] and the lack of one of these proteins was shown with the HTC hepatoma cell line [22], which is highly insensitive to DBcAMP in terms of the TAT induction.…”

Section: Resultsmentioning

confidence: 99%

Evidence for the lack of response of tyrosine aminotransferase to dibutyryl cyclic AMP in regenerating rat liver

et al. 1977

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Cyclic AMP and cyclic GMP content and binding in malignancy

Cited by 53 publications

References 23 publications

The content and metabolism of cyclic adenosine 3', 5'-monophosphate and cyclic guanosine 3', 5'-monophosphate in adenocarcinoma of the human colon.

The content and metabolism of cyclic adenosine 3', 5'-monophosphate and cyclic guanosine 3', 5'-monophosphate in adenocarcinoma of the human colon.

Mapping of neural nitric oxide synthase in the rat suggests frequent co-localization with NADPH diaphorase but not with soluble guanylyl cyclase, and novel paraneural functions for nitrinergic signal transduction.

Evidence for the lack of response of tyrosine aminotransferase to dibutyryl cyclic AMP in regenerating rat liver

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