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CCK identified at bottom right.

Cholecystokinin (CCK or CCK-PZ; from Greek chole, "bile"; cysto, "sac"; kinin, "move"; hence, move the bile-sac (gallbladder)) is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fat and protein. Cholecystokinin, previously called pancreozymin, is synthesized by I-cells in the mucosal epithelium of the small intestine and secreted in the duodenum, the first segment of the small intestine, and causes the release of digestive enzymes and bile from the pancreas and gallbladder, respectively. It also acts as a hunger suppressant. Recent evidence has suggested that it also plays a major role in inducing drug tolerance to opioids like morphine and heroin, and is partly implicated in experiences of pain hypersensitivity during opioid withdrawal.^[1]^[2]

Structure

CCK is composed of varying numbers of amino acids depending on post-translational modification of the CCK gene product, preprocholecystokinin. Thus CCK is actually a family of hormones identified by number of amino acids, e.g., CCK58, CCK33, and CCK8. CCK58 assumes a helix-turn-helix configuration.^[3] Its existence was first suggested in 1905 by the British physiologist Joy Simcha Cohen. CCK is very similar in structure to gastrin, another of the gastrointestinal hormones. CCK and gastrin share the same five amino acids at their C-termini.

Functions

CCK mediates a number of physiological processes, including digestion and satiety. It is released by I cells located in the mucosal epithelium of the small intestine (mostly in the duodenum and jejunum), neurons of the enteric nervous system and neurons in the brain. Release of CCK is stimulated by monitor peptide released by pancreatic acinar cells as well as CCK-releasing protein, a paracrine factor secreted by enterocytes in the gastrointestinal mucosa. In addition, release of acetylcholine by the parasympathetic nerve fibers of the vagus nerve also stimulate its secretion. The presence of fatty acids and/or certain amino acids in the chyme entering the duodenum is the greatest stimulator of CCK release.

CCK mediates digestion in the small intestine by inhibiting gastric emptying and gastric acid secretion. It stimulates the acinar cells of the pancreas to release digestive enzymes and stimulates the secretion of a juice rich in pancreatic digestive enzymes, hence the old name pancreozymin. Together these enzymes catalyze the digestion of fat, protein, and carbohydrates. Thus, as the levels of the substances that stimulated the release of CCK drop, the concentration of the hormone drops as well. The release of CCK is also inhibited by somatostatin. Trypsin, a protease released by pancreatic acinar cells hydrolyzes CCK-releasing peptide and monitor peptide effectively turning off the additional signals to secrete CCK.

CCK also causes the increased production of hepatic bile, and stimulates the contraction of the gall bladder and the relaxation of the Sphincter of Oddi (Glisson's sphincter), resulting in the delivery of bile into the duodenal part of the small intestine. Bile salts form amphipathic micelles that emulsify fats, aiding in their digestion and absorption.

Neurobiology

As a neuropeptide, CCK mediates satiety by acting on the CCK receptors distributed widely throughout the central nervous system. In humans, it has been suggested that CCK administration causes nausea and anxiety, and induces a satiating effect. CCK-4 is routinely used to induce anxiety in humans though certainly different forms of CCK are being shown to have highly variable effects.^[4] The mechanism for this hunger suppression is thought to be a decrease in the rate of gastric emptying.^[5]

CCK also has stimulatory effects on the vagus nerve, effects that can be inhibited by capsaicin.^[6] The stimulatory effects of CCK oppose those of ghrelin, which has been shown to inhibit the vagus nerve.^{[citation needed]} The CCK tetrapeptide fragment CCK-4 (Trp-Met-Asp-Phe-NH₂) reliably causes anxiety when administered to humans, and is commonly used in scientific research to induce panic attacks for the purpose of testing new anxiolytic drugs.^[7]

The effects of CCK vary between individuals. For example, in rats, CCK administration significantly reduces hunger in young males, but is slightly less effective in older subjects, and even slightly less effective in females. The hunger-suppressive effects of CCK also are reduced in obese rats.^[8]

Interactions

Cholecystokinin has been shown to interact with the Cholecystokinin A receptor located mainly on pancreatic acinar cells and Cholecystokinin B receptor mostly in the brain and stomach. CCK_B receptor also binds gastrin, a gastrointestinal hormone involved in stimulating gastric acid release and growth of the gastric mucosa.^[9]^[10]^[11]

CCK has also been shown to interact with calcineurin in the pancreas. Calcineurin will go on to activate the transcription factors NFAT 1–3, which will stimulate hypertrophy and growth of the pancreas. CCK can be stimulated by a diet high in protein, or by protease inhibitors.^[12]

Cholecystokinin has been shown to interact with orexin neurons which control appetite and wakefulness (sleep).^[13] Cholecystokinin can have indirect effects on sleep regulation.^[14]

Cholecystokinin in the body cannot cross the blood brain barrier, but certain parts of the hypothalamus and brainstem aren't protected by the barrier.

References

^ Kissin I, Bright CA, Bradley EL (2000). "Acute tolerance to continuously infused alfentanil: the role of cholecystokinin and N-methyl-D-aspartate-nitric oxide systems". Anesth. Analg. 91 (1): 110–6. doi:10.1097/00000539-200007000-00021. PMID 10866896. http://www.anesthesia-analgesia.org/cgi/content/abstract/91/1/110.
^ Fukazawa Y, Maeda T, Kiguchi N, Tohya K, Kimura M, Kishioka S (2007). "Activation of spinal cholecystokinin and neurokinin-1 receptors is associated with the attenuation of intrathecal morphine analgesia following electroacupuncture stimulation in rats". J. Pharmacol. Sci. 104 (2): 159–66. doi:10.1254/jphs.FP0070475. PMID 17558184.
^ Reeve JR Jr, Eysselein VE, Rosenquist G, Zeeh J, Regner U, Ho FJ, Chew P, Davis MT, Lee TD, Shively JE, Brazer SR, Liddle RA (1996). "Evidence that CCK-58 has structure that influences its biological activity". Am. J. Physiol. 270 (5 Pt 1): G860-8. PMID 8967499.
^ Greenough A, Cole G, Lewis J, Lockton A, Blundell J (1998). "Untangling the effects of hunger, anxiety, and nausea on energy intake during intravenous cholecystokinin octapeptide (CCK-8) infusion". Physiol. Behav. 65 (2): 303–10. doi:10.1016/S0031-9384(98)00169-3. PMID 9855480.
^ Shillabeer G, Davison JS (1987). "Proglumide, a cholecystokinin antagonist, increases gastric emptying in rats". Am. J. Physiol. 252 (2 Pt 2): R353–60. PMID 3812772. http://ajpregu.physiology.org/cgi/content/abstract/252/2/R353.
^ Holzer P (July 1998). "Neural injury, repair, and adaptation in the GI tract. II. The elusive action of capsaicin on the vagus nerve". Am. J. Physiol. 275 (1 Pt 1): G8–13. PMID 9655678. http://ajpgi.physiology.org/content/275/1/G8.full#cited-by.
^ Bradwejn J (July 1993). "Neurobiological investigations into the role of cholecystokinin in panic disorder". J Psychiatry Neurosci 18 (4): 178–88. PMC 1188527. PMID 8104032. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1188527/.
^ Fink H, Rex A, Voits M, Voigt JP (1998). "Major biological actions of CCK—a critical evaluation of research findings". Exp Brain Res 123 (1–2): 77–83. doi:10.1007/s002210050546. PMID 9835394.
^ Harikumar KG, Clain J, Pinon DI, Dong M, Miller LJ (January 2005). "Distinct molecular mechanisms for agonist peptide binding to types A and B cholecystokinin receptors demonstrated using fluorescence spectroscopy". J. Biol. Chem. 280 (2): 1044–50. doi:10.1074/jbc.M409480200. PMID 15520004.
^ Aloj L, Caracò C, Panico M, Zannetti A, Del Vecchio S, Tesauro D, De Luca S, Arra C, Pedone C, Morelli G, Salvatore M (March 2004). "In vitro and in vivo evaluation of 111In-DTPAGlu-G-CCK8 for cholecystokinin-B receptor imaging". J. Nucl. Med. 45 (3): 485–94. PMID 15001692.
^ Galés C, Poirot M, Taillefer J, Maigret B, Martinez J, Moroder L, Escrieut C, Pradayrol L, Fourmy D, Silvente-Poirot S (May 2003). "Identification of tyrosine 189 and asparagine 358 of the cholecystokinin 2 receptor in direct interaction with the crucial C-terminal amide of cholecystokinin by molecular modeling, site-directed mutagenesis, and structure/affinity studies". Mol. Pharmacol. 63 (5): 973–82. doi:10.1124/mol.63.5.973. PMID 12695525.
^ Gurda GT, Guo L, Lee SH, Molkentin JD, Williams JA (January 2008). "Cholecystokinin activates pancreatic calcineurin-NFAT signaling in vitro and in vivo". Mol. Biol. Cell 19 (1): 198–206. doi:10.1091/mbc.E07-05-0430. PMC 2174201. PMID 17978097. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2174201/.
^ Tsujino N, Yamanaka A, Ichiki K, Muraki Y, Kilduff TS, Yagami K, Takahashi S, Goto K, Sakurai T (August 2005). "Cholecystokinin activates orexin/hypocretin neurons through the cholecystokinin A receptor". J. Neurosci. 25 (32): 7459–69. doi:10.1523/JNEUROSCI.1193-05.2005. PMID 16093397.
^ Kapas, Levente (2010). Metabolic signals in sleep regulation: the role of cholecystokinin (PhD thesis). University of Szeged. http://www.phd.szote.u-szeged.hu/Elmeleti_DI/Disszertaciok/2010/de_Levente_Kapas.pdf.

External links

Cholecystokinin at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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1. コレシストキニンの生理学 physiology of cholecystokinin
2. 成人における胆嚢機能障害 functional gallbladder disorder in adults
3. 膵外分泌機能不全 exocrine pancreatic insufficiency
4. オッディ括約筋機能不全の臨床症状よび診断 clinical manifestations and diagnosis of sphincter of oddi dysfunction
5. 慢性膵炎の治療 treatment of chronic pancreatitis

English Journal

Fluorescent Visualisation of the Hypothalamic Oxytocin Neurones Activated by Cholecystokinin-8 in Rats Expressing c-fos-Enhanced Green Fluorescent Protein and Oxytocin-Monomeric Red Fluorescent Protein 1 Fusion Transgenes.

Katoh A1, Shoguchi K, Matsuoka H, Yoshimura M, Ohkubo JI, Matsuura T, Maruyama T, Ishikura T, Aritomi T, Fujihara H, Hashimoto H, Suzuki H, Murphy D, Ueta Y.Author information 1Department of Physiology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan; Otorhynolaryngology-Head and Neck Surgery, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan; Department of Otorhynolaryngology, National Kyushu Medical Center, Fukuoka, Japan.AbstractThe up-regulation of c-fos gene expression is widely used as a marker of neuronal activation elicited by various stimuli. Anatomically precise observation of c-fos gene products can be achieved at the RNA level by in situ hybridisation or at the protein level by immunocytochemistry. Both of these methods are time and labour intensive. We have developed a novel transgenic rat system that enables the trivial visualisation of c-fos expression using an enhanced green fluorescent protein (eGFP) tag. These rats express a transgene consisting of c-fos gene regulatory sequences that drive the expression of a c-fos-eGFP fusion protein. In c-fos-eGFP transgenic rats, robust nuclear eGFP fluorescence was observed in osmosensitive brain regions 90 min after i.p. administration of hypertonic saline. Nuclear eGFP fluorescence was also observed in the supraoptic nucleus (SON) and paraventricular nucleus (PVN) 90 min after i.p. administration of cholecystokinin (CCK)-8, which selectively activates oxytocin (OXT)-secreting neurones in the hypothalamus. In double transgenic rats that express c-fos-eGFP and an OXT-monomeric red fluorescent protein 1 (mRFP1) fusion gene, almost all mRFP1-positive neurones in the SON and PVN expressed nuclear eGFP fluorescence 90 min after i.p. administration of CCK-8. It is possible that not only a plane image, but also three-dimensional reconstruction image may identify cytoplasmic vesicles in an activated neurone at the same time.
Journal of neuroendocrinology.J Neuroendocrinol.2014 May;26(5):341-7. doi: 10.1111/jne.12150.
The up-regulation of c-fos gene expression is widely used as a marker of neuronal activation elicited by various stimuli. Anatomically precise observation of c-fos gene products can be achieved at the RNA level by in situ hybridisation or at the protein level by immunocytochemistry. Both of these me
PMID 24730419

Nocebo and placebo modulation of hypobaric hypoxia headache involves the cyclooxygenase-prostaglandins pathway.

Benedetti F1, Durando J2, Vighetti S3.Author information 1Department of Neuroscience, University of Turin Medical School, Turin 10125, Italy; National Institute of Neuroscience Matterhorn Laboratories, Plateau Rosà Research Station, Breuil-Cervinia 11021, Italy. Electronic address: fabrizio.benedetti@unito.it.2National Institute of Neuroscience Matterhorn Laboratories, Plateau Rosà Research Station, Breuil-Cervinia 11021, Italy.3Department of Neuroscience, University of Turin Medical School, Turin 10125, Italy; National Institute of Neuroscience Matterhorn Laboratories, Plateau Rosà Research Station, Breuil-Cervinia 11021, Italy.AbstractNocebo and placebo effects have been found to modulate several neurochemical systems, such as cholecystokinin, endogenous opioids, and endocannabinoids. Here we show that also the cyclooxygenase-prostaglandins pathway can be modulated by both nocebos and placebos. In fact, we found that negative expectation, the crucial element of the nocebo effect, about headache pain led to the enhancement of the cyclooxygenase-prostaglandins pathway, which, in turn, induced pain worsening. As an experimental model, we studied hypobaric hypoxia headache at high altitude in 2 populations of subjects. Whereas the experimental nocebo group received negative information by a single individual who was informed about the risk of headache, the control group did not know about the possible occurrence of headache. We found a significant increase in headache and salivary prostaglandins and thromboxane in the nocebo group compared to the control group, suggesting that negative expectations enhance cyclooxygenase activity. In addition, placebo administration to headache sufferers at high altitude inhibited the nocebo-related component of pain and prostaglandins synthesis, which indicates that the cyclooxygenase pathway can be modulated by both nocebos and placebos. Our results show for the first time how nocebos and placebos affect the synthesis of prostaglandins, which represent an important target of analgesic drugs, thus emphasizing once again the notion that placebos and drugs may use common biochemical pathways.
Pain.Pain.2014 May;155(5):921-8. doi: 10.1016/j.pain.2014.01.016. Epub 2014 Jan 21.
Nocebo and placebo effects have been found to modulate several neurochemical systems, such as cholecystokinin, endogenous opioids, and endocannabinoids. Here we show that also the cyclooxygenase-prostaglandins pathway can be modulated by both nocebos and placebos. In fact, we found that negative exp
PMID 24462931

Simultaneous quantification of the glucagon-like peptide-1 (GLP-1) and cholecystokinin (CCK) receptor agonists in rodent plasma by on-line solid phase extraction and LC-MS/MS.

Wang Y1, Roth JD2, Taylor SW2.Author information 1Amylin Pharmaceuticals, LLC (a wholly-owned subsidiary of Bristol-Myers Squibb), 9625 Towne Centre Drive, San Diego, CA 92121, USA. Electronic address: yan.wang555@gmail.com.2Amylin Pharmaceuticals, LLC (a wholly-owned subsidiary of Bristol-Myers Squibb), 9625 Towne Centre Drive, San Diego, CA 92121, USA.AbstractPeptide agonists of the glucagon-like peptide-1 receptor (GLP-1R) and the cholecystokinin-1 receptor (CCK1-R) have therapeutic potential because of their marked anorexigenic and weight lowering effects. Furthermore, recent studies in rodents have shown that co-administration of these agents may prove more effective than treatment either of the peptide classes alone. To correlate the pharmacodynamic effects to the pharmacokinetics of these peptide drugs in vivo, a sensitive and robust bioanalytical method is essential. Furthermore, the simultaneous determination of both analytes in plasma samples by a single method offers obvious advantages. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) is well suited to this goal through its ability to simultaneously monitor multiple analytes through selected reaction monitoring (SRM). However, it is a challenge to find appropriate conditions that allow two peptides with widely disparate physiochemical properties to be simultaneously analyzed while maintaining the necessary sensitivity for their accurate plasma concentrations. Herein, we report an on-line solid phase extraction (SPE) LC-MS/MS method for simultaneous quantification of the CCK1-R agonist AC170222 and the GLP-1R agonist AC3174 in rodent plasma. The assay has a linear range from 0.0975 to 100ng/mL, with lower limits of quantification of 0.0975ng/mL and 0.195ng/mL for AC3174 and AC170222, respectively. The intra- and inter-day precisions were below 15%. The developed LC-MS/MS method was used to simultaneously quantify AC3174 and AC170222, the results showed that the terminal plasma concentrations of AC3174 or AC170222 were comparable between groups of animals that were administered with the peptides alone (247±15pg/mL of AC3174 and 1306±48pg/mL of AC170222), or in combination (222±32pg/mL and 1136±47pg/mL of AC3174 and AC170222, respectively). These data provide information on the drug exposure to aid in assessing the combination effects of AC3174 and AC170222 on rodent metabolism.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.J Chromatogr B Analyt Technol Biomed Life Sci.2014 Apr 15;957:24-9. doi: 10.1016/j.jchromb.2014.02.040. Epub 2014 Mar 4.
Peptide agonists of the glucagon-like peptide-1 receptor (GLP-1R) and the cholecystokinin-1 receptor (CCK1-R) have therapeutic potential because of their marked anorexigenic and weight lowering effects. Furthermore, recent studies in rodents have shown that co-administration of these agents may prov
PMID 24657407

Japanese Journal

コレシストキニン・パンクレオザイミン(CCK-PZ) (広範囲血液・尿化学検査免疫学的検査(第7版・4)その数値をどう読むか) -- (内分泌学的検査膵・消化管関係)

坂口浩樹,岩田康博,小林絢三 [他]
日本臨床 68(-), 544-546, 2010-07
NAID 40017200805

Inhibition of cholecystokinin-pancreozymin release by somatostatin

SCHLEGEL W
Lancet ii, 166-168, 1997
NAID 10014884317

Secretin-Pancreozymin Test (SPT) and Endoscopic Retrograde Cholangiopancreatography (ERCP) : Both Are Necessary for Diagnosing or Excluding Chronic Pancreatitis

LANKISCH Paul Georg,SEIDENSTICKER Frank,OTTO Jutta,LUBBERS Heiko,MAHLKE Reiner,STOCKMANN Fritz,FOLSCH Ulrich R.,CREUTZFELDT Werner
Pancreas 12(2), 149-152, 1996-03-01
NAID 10016415550

Related Pictures

★リンクテーブル★

リンク元	「コレシストキニン」
拡張検索	「cholecystokinin pancreozymin」「pancreozymin secretin test」

「コレシストキニン」

Cholecystokinin
Identifiers
Symbols	CCK; MGC117187
External IDs	OMIM: 118440 MGI: 88297 HomoloGene: 583 ChEMBL: 1649050 GeneCards: CCK Gene
Gene Ontology
Molecular function	• hormone activity; • neuropeptide hormone activity;
Cellular component	• extracellular region; • extracellular space; • axon; • dendrite; • axon initial segment; • terminal button; • axon hillock; • perikaryon;
Biological process	• behavioral fear response; • neuron migration; • release of cytochrome c from mitochondria; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • signal transduction; • protein kinase C-activating G-protein coupled receptor signaling pathway; • axonogenesis; • positive regulation of cell proliferation; • negative regulation of appetite; • positive regulation of protein oligomerization; • eating behavior; • positive regulation of apoptotic process; • positive regulation of peptidyl-tyrosine phosphorylation; • positive regulation of mitochondrial depolarization; • regulation of sensory perception of pain;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

英: cholecystokinin, CCK
同: コレシストキニン・パンクレオザイミン cholecystokinin pancreozymin CCK-PZ; パンクレオザイミン pancreozymin
関: 消化管ホルモン、胆嚢収縮物質

[show details]

コレシストキニン : 約 25,900 件
パンクレオザイミン : 約 4,080 件

まとめ

小腸内タンパク質分解産物、酸、脂肪酸、アルコールが刺激となって、小腸のI細胞から分泌され、消化酵素に富む膵液を分泌させる。またオッディ括約筋を弛緩させ、胆嚢を収縮させて胆汁の分泌を促す。

分泌部位と細胞

十二指腸、空腸のI細胞

作用

胃

↓：胃排出(First Aid step 1 p.269)
↑：胃酸分泌(CBT QB vol2 p.295)

胆嚢

↑：胆嚢を収縮 (SP.706)
↑：胆嚢外分泌腺増加

胆膵管

↓：胆膵管膨大部括約筋(オッディ括約筋)を弛緩 (SP.706)

膵

↑：膵液分泌(First Aid step 1 p.269)
↑：外分泌腺増加

調節 (First Aid step 1 p.269)

↑

脂肪酸、アミノ酸

↓

セクレチン
胃のpH<1.5

臨床関連

胆石症

脂肪摂取→CCK↑→胆汁↑→いたいっ

「cholecystokinin pancreozymin」

　　[★] コレシストキニン。コレシストキニン・パンクレオザイミン

「pancreozymin secretin test」

　　[★] パンクレオザイミン・セクレチン試験

[pmid10866896-0] Kissin I, Bright CA, Bradley EL (2000). "Acute tolerance to continuously infused alfentanil: the role of cholecystokinin and N-methyl-D-aspartate-nitric oxide systems". Anesth. Analg. 91 (1): 110–6. doi:10.1097/00000539-200007000-00021. PMID 10866896. http://www.anesthesia-analgesia.org/cgi/content/abstract/91/1/110.

[pmid17558184-1] Fukazawa Y, Maeda T, Kiguchi N, Tohya K, Kimura M, Kishioka S (2007). "Activation of spinal cholecystokinin and neurokinin-1 receptors is associated with the attenuation of intrathecal morphine analgesia following electroacupuncture stimulation in rats". J. Pharmacol. Sci. 104 (2): 159–66. doi:10.1254/jphs.FP0070475. PMID 17558184.

[pmid8967499-2] Reeve JR Jr, Eysselein VE, Rosenquist G, Zeeh J, Regner U, Ho FJ, Chew P, Davis MT, Lee TD, Shively JE, Brazer SR, Liddle RA (1996). "Evidence that CCK-58 has structure that influences its biological activity". Am. J. Physiol. 270 (5 Pt 1): G860-8. PMID 8967499.

[pmid9855480-3] Greenough A, Cole G, Lewis J, Lockton A, Blundell J (1998). "Untangling the effects of hunger, anxiety, and nausea on energy intake during intravenous cholecystokinin octapeptide (CCK-8) infusion". Physiol. Behav. 65 (2): 303–10. doi:10.1016/S0031-9384(98)00169-3. PMID 9855480.

[pmid3812772-4] Shillabeer G, Davison JS (1987). "Proglumide, a cholecystokinin antagonist, increases gastric emptying in rats". Am. J. Physiol. 252 (2 Pt 2): R353–60. PMID 3812772. http://ajpregu.physiology.org/cgi/content/abstract/252/2/R353.

[pmid9655678-5] Holzer P (July 1998). "Neural injury, repair, and adaptation in the GI tract. II. The elusive action of capsaicin on the vagus nerve". Am. J. Physiol. 275 (1 Pt 1): G8–13. PMID 9655678. http://ajpgi.physiology.org/content/275/1/G8.full#cited-by.

[pmid8104032-6] Bradwejn J (July 1993). "Neurobiological investigations into the role of cholecystokinin in panic disorder". J Psychiatry Neurosci 18 (4): 178–88. PMC 1188527. PMID 8104032. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1188527/.

[pmid9835394-7] Fink H, Rex A, Voits M, Voigt JP (1998). "Major biological actions of CCK—a critical evaluation of research findings". Exp Brain Res 123 (1–2): 77–83. doi:10.1007/s002210050546. PMID 9835394.

[pmid15520004-8] Harikumar KG, Clain J, Pinon DI, Dong M, Miller LJ (January 2005). "Distinct molecular mechanisms for agonist peptide binding to types A and B cholecystokinin receptors demonstrated using fluorescence spectroscopy". J. Biol. Chem. 280 (2): 1044–50. doi:10.1074/jbc.M409480200. PMID 15520004.

[pmid15001692-9] Aloj L, Caracò C, Panico M, Zannetti A, Del Vecchio S, Tesauro D, De Luca S, Arra C, Pedone C, Morelli G, Salvatore M (March 2004). "In vitro and in vivo evaluation of 111In-DTPAGlu-G-CCK8 for cholecystokinin-B receptor imaging". J. Nucl. Med. 45 (3): 485–94. PMID 15001692.

[pmid12695525-10] Galés C, Poirot M, Taillefer J, Maigret B, Martinez J, Moroder L, Escrieut C, Pradayrol L, Fourmy D, Silvente-Poirot S (May 2003). "Identification of tyrosine 189 and asparagine 358 of the cholecystokinin 2 receptor in direct interaction with the crucial C-terminal amide of cholecystokinin by molecular modeling, site-directed mutagenesis, and structure/affinity studies". Mol. Pharmacol. 63 (5): 973–82. doi:10.1124/mol.63.5.973. PMID 12695525.

[pmid17978097-11] Gurda GT, Guo L, Lee SH, Molkentin JD, Williams JA (January 2008). "Cholecystokinin activates pancreatic calcineurin-NFAT signaling in vitro and in vivo". Mol. Biol. Cell 19 (1): 198–206. doi:10.1091/mbc.E07-05-0430. PMC 2174201. PMID 17978097. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2174201/.

[pmid16093397-12] Tsujino N, Yamanaka A, Ichiki K, Muraki Y, Kilduff TS, Yagami K, Takahashi S, Goto K, Sakurai T (August 2005). "Cholecystokinin activates orexin/hypocretin neurons through the cholecystokinin A receptor". J. Neurosci. 25 (32): 7459–69. doi:10.1523/JNEUROSCI.1193-05.2005. PMID 16093397.

[13] Kapas, Levente (2010). Metabolic signals in sleep regulation: the role of cholecystokinin (PhD thesis). University of Szeged. http://www.phd.szote.u-szeged.hu/Elmeleti_DI/Disszertaciok/2010/de_Levente_Kapas.pdf.

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案内

案内

pancreozymin