Editing Cyclic adenosine monophosphate (section)

==Pathology==
Since cyclic AMP is a second messenger and plays vital role in cell signalling, it has been implicated in various disorders but not restricted to the roles given below:

=== Role in human carcinoma ===
Some research has suggested that a deregulation of cAMP pathways and an aberrant activation of cAMP-controlled genes is linked to the growth of some cancers.<ref>{{cite journal| url = http://cancerres.aacrjournals.org/cgi/content/full/64/4/1338| title = American Association for Cancer Research (cAMP-responsive Genes and Tumor Progression)| journal = Cancer Research| date = 15 February 2004| volume = 64| issue = 4| pages = 1338–1346| doi = 10.1158/0008-5472.CAN-03-2089| last1 = Abramovitch| first1 = Rinat| last2 = Tavor| first2 = Einat| last3 = Jacob-Hirsch| first3 = Jasmine| last4 = Zeira| first4 = Evelyne| last5 = Amariglio| first5 = Ninette| last6 = Pappo| first6 = Orit| last7 = Rechavi| first7 = Gideon| last8 = Galun| first8 = Eithan| last9 = Honigman| first9 = Alik| pmid = 14973073| s2cid = 14047485}}</ref><ref>{{cite journal| url = http://cancerres.aacrjournals.org/cgi/content/abstract/66/19/9483| title = American Association for Cancer Research (cAMP Dysregulation and Melonoma)| journal = Cancer Research| date = October 2006| volume = 66| issue = 19| pages = 9483–9491| doi = 10.1158/0008-5472.CAN-05-4227| last1 = Dumaz| first1 = Nicolas| last2 = Hayward| first2 = Robert| last3 = Martin| first3 = Jan| last4 = Ogilvie| first4 = Lesley| last5 = Hedley| first5 = Douglas| last6 = Curtin| first6 = John A.| last7 = Bastian| first7 = Boris C.| last8 = Springer| first8 = Caroline| last9 = Marais| first9 = Richard| pmid = 17018604| doi-access = free}}</ref><ref>{{cite journal| url = http://clincancerres.aacrjournals.org/cgi/content/abstract/2/1/201| title = American Association for Cancer Research (cAMP-binding Proteins' Presence in Tumors)| journal = Clinical Cancer Research| date = January 1996| volume = 2| issue = 1| pages = 201–206| last1 = Simpson| first1 = B. J.| last2 = Ramage| first2 = A. D.| last3 = Hulme| first3 = M. J.| last4 = Burns| first4 = D. J.| last5 = Katsaros| first5 = D.| last6 = Langdon| first6 = S. P.| last7 = Miller| first7 = W. R.}}</ref>

=== Role in prefrontal cortex disorders ===
Research suggests that cAMP affects the function of higher-order thinking in the [[prefrontal cortex]] through its regulation of ion channels called [[hyperpolarization-activated cyclic nucleotide-gated channels]] (HCN). HCN channels will open when exposed to cAMP. Once the HCN channel is open, the electrical activity within the neuron is disrupted and the cell becomes less responsive. This interferes with the function of the [[prefrontal cortex]] in working memory tasks. Inhibition of cAMP has been observed to improve spatial working memory.<ref>{{cite web| last1 = Arnsten| first1 = Amy| last2 = McCormick| first2 = David| title = Cyclic AMP, a molecule linked to stress, also plays a role in memory loss| date = 2007| url = https://medicine.yale.edu/news/yale-medicine-magazine/article/cyclic-amp-a-molecule-linked-to-stress-also/}}</ref><ref>{{cite journal| doi = 10.1016/j.cell.2007.03.015| issn = 00928674| volume = 129| issue = 2| pages = 397–410| last1 = Wang| first1 = Min| last2 = Ramos| first2 = Brian P.| last3 = Paspalas| first3 = Constantinos D.| last4 = Shu| first4 = Yousheng| last5 = Simen| first5 = Arthur| last6 = Duque| first6 = Alvaro| last7 = Vijayraghavan| first7 = Susheel| last8 = Brennan| first8 = Avis| last9 = Dudley| first9 = Anne| last10 = Nou| first10 = Eric| last11 = Mazer| first11 = James A.| last12 = McCormick| first12 = David A.| last13 = Arnsten| first13 = Amy F.T.| title = α2A-Adrenoceptors Strengthen Working Memory Networks by Inhibiting cAMP-HCN Channel Signaling in Prefrontal Cortex| journal = Cell| access-date = 2025-03-03| date = April 2007 | url = https://linkinghub.elsevier.com/retrieve/pii/S0092867407003443}}</ref>

cAMP is involved in activation of trigeminocervical system leading to neurogenic inflammation and causing migraine. <ref>{{cite journal |last1=Segatto |first1=Marco |title=Neurogenic Inflammation: The Participant in Migraine and Recent Advancements in Translational Research |journal=Biomedicines |year=2021 |volume=10 |issue=1 |page=76 |doi=10.3390/biomedicines10010076 |pmid=35052756 |pmc=8773152 |doi-access=free }}</ref>

=== Role in infectious disease agents' pathogenesis  ===
Disrupted functioning of cAMP has been noted as one of the mechanisms of several bacterial exotoxins. 

They can be subgrouped into two distinct categories:<ref name="klin-wochenschr">{{cite journal |last1=Kather |first1=H |last2=Aktories |first2=K |date=November 15, 1983 |title=cAMP-System und bakterielle Toxine [The cAMP system and bacterial toxins] |url=https://pubmed.ncbi.nlm.nih.gov/6317939/ |journal=Klin Wochenschr |volume= 61|issue= 22|pages= 1109–1114| pmid=6317939 |doi=10.1007/BF01530837 |s2cid=33162709 |access-date=February 26, 2022}}</ref>

* Toxins that interfere with enzymes [[ADP-ribosylation|ADP-ribosyl-transferase]]s, and
* [[Adenylate cyclase toxin|invasive adenylate cyclases]].

==== ADP-ribosyl-transferases related toxins ====
{{Main article|Cholera toxin}}
* [[Cholera toxin]] is an [[AB toxin]] that has five B subunints and one A subunit. The toxin acts by the following mechanism:  First, the B subunit ring of the cholera toxin binds to [[GM1]] [[ganglioside]]s on the surface of target cells. If a cell lacks GM1 the toxin most likely binds to other types of glycans, such as Lewis Y and Lewis X, attached to proteins instead of lipids.<ref>{{cite news |url=https://elifesciences.org/content/4/e09545 |title=Fucosylation and protein glycosylation create functional receptors for cholera toxin |author=Amberlyn M Wands |author2=Akiko Fujita |journal=eLife | date=October 2015 |volume=4 |doi=10.7554/eLife.09545 |doi-access=free }}</ref><ref>Cervin J, Wands AM, Casselbrant A, Wu H, Krishnamurthy S, Cvjetkovic A, et al. (2018) GM1 ganglioside-independent intoxication by Cholera toxin. PLoS Pathog 14(2): e1006862. https://doi.org/10.1371/journal.ppat.1006862</ref><ref>{{Cite journal |last=Wands |first=Amberlyn M. |last2=Cervin |first2=Jakob |last3=Huang |first3=He |last4=Zhang |first4=Ye |last5=Youn |first5=Gyusaang |last6=Brautigam |first6=Chad A. |last7=Matson Dzebo |first7=Maria |last8=Björklund |first8=Per |last9=Wallenius |first9=Ville |last10=Bright |first10=Danielle K. |last11=Bennett |first11=Clay S. |last12=Wittung-Stafshede |first12=Pernilla |last13=Sampson |first13=Nicole S. |last14=Yrlid |first14=Ulf |last15=Kohler |first15=Jennifer J. |date=2018-05-11 |title=Fucosylated Molecules Competitively Interfere with Cholera Toxin Binding to Host Cells |url=https://pubs.acs.org/doi/10.1021/acsinfecdis.7b00085 |journal=ACS Infectious Diseases |language=en |volume=4 |issue=5 |pages=758–770 |doi=10.1021/acsinfecdis.7b00085 |issn=2373-8227 |pmc=5948155 |pmid=29411974}}</ref><ref name="klin-wochenschr" />