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Cholecystokinin-33 (human)

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Cholecystokinin-33 (human) is a peptide hormone, holding great significance in biomedical research as it enables exploration into the intricacies of cholecystokinin receptors.

Category

Peptide Inhibitors

Catalog number

BAT-015255

CAS number

96827-04-2

Molecular Formula

C167H263N51O52S4

Molecular Weight

3945.44

Specification
Reference Reading

IUPAC Name

(3S)-3-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-carbamimidamido-2-[[2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]pentanoyl]amino]-4-methylsulfanylbutanoyl]amino]-3-hydroxypropanoyl]amino]-3-methylpentanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-4-oxobutanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoyl]amino]-4-oxobutanoyl]amino]-4-methylpentanoyl]amino]-3-carboxypropanoyl]pyrrolidine-2-carbonyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-3-carboxypropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-4-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-1-oxo-3-(4-sulfooxyphenyl)propan-2-yl]amino]-4-oxobutanoic acid

Synonyms

CCK-39 (7-39) (human); H-Lys-Ala-Pro-Ser-Gly-Arg-Met-Ser-Ile-Val-Lys-Asn-Leu-Gln-Asn-Leu-Asp-Pro-Ser-His-Arg-Ile-Ser-Asp-Arg-Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2; L-lysyl-L-alanyl-L-prolyl-L-seryl-glycyl-L-arginyl-L-methionyl-L-seryl-L-isoleucyl-L-valyl-L-lysyl-L-asparagyl-L-leucyl-L-glutaminyl-L-asparagyl-L-leucyl-L-alpha-aspartyl-L-prolyl-L-seryl-L-histidyl-L-arginyl-L-isoleucyl-L-seryl-L-alpha-aspartyl-L-arginyl-L-alpha-aspartyl-O4-sulfo-L-tyrosyl-L-methionyl-glycyl-L-tryptophyl-L-methionyl-L-alpha-aspartyl-L-phenylalaninamide

Appearance

White Lyophilized Powder

Purity

≥90%

Sequence

KAPSGRMSIVKNLQNLDPSHRISDRD-Y(SO3H)-MGWMDF

Storage

Store at -20°C

Solubility

Soluble in Acetic Acid

InChI

InChI=1S/C167H263N51O52S4/c1-15-85(9)132(161(263)213-118(79-221)156(258)208-112(69-127(228)229)152(254)192-98(38-27-54-183-166(177)178)140(242)206-114(71-129(232)233)154(256)202-107(64-89-42-44-92(45-43-89)270-274(267,268)269)147(249)195-101(48-58-271-12)136(238)186-76-126(227)191-108(65-90-73-185-95-35-21-20-33-93(90)95)148(250)197-102(49-59-272-13)142(244)207-113(70-128(230)231)153(255)199-104(134(174)236)63-88-31-18-17-19-32-88)215-144(246)99(39-28-55-184-167(179)180)193-149(251)109(66-91-74-181-81-188-91)203-155(257)117(78-220)212-159(261)121-41-30-57-218(121)164(266)115(72-130(234)235)209-146(248)106(62-83(5)6)201-151(253)111(68-124(173)225)205-141(243)100(46-47-122(171)223)194-145(247)105(61-82(3)4)200-150(252)110(67-123(172)224)204-139(241)97(36-23-25-52-169)198-160(262)131(84(7)8)214-162(264)133(86(10)16-2)216-157(259)119(80-222)210-143(245)103(50-60-273-14)196-138(240)96(37-26-53-182-165(175)176)190-125(226)75-187-137(239)116(77-219)211-158(260)120-40-29-56-217(120)163(265)87(11)189-135(237)94(170)34-22-24-51-168/h17-21,31-33,35,42-45,73-74,81-87,94,96-121,131-133,185,219-222H,15-16,22-30,34,36-41,46-72,75-80,168-170H2,1-14H3,(H2,171,223)(H2,172,224)(H2,173,225)(H2,174,236)(H,181,188)(H,186,238)(H,187,239)(H,189,237)(H,190,226)(H,191,227)(H,192,254)(H,193,251)(H,194,247)(H,195,249)(H,196,240)(H,197,250)(H,198,262)(H,199,255)(H,200,252)(H,201,253)(H,202,256)(H,203,257)(H,204,241)(H,205,243)(H,206,242)(H,207,244)(H,208,258)(H,209,248)(H,210,245)(H,211,260)(H,212,261)(H,213,263)(H,214,264)(H,215,246)(H,216,259)(H,228,229)(H,230,231)(H,232,233)(H,234,235)(H4,175,176,182)(H4,177,178,183)(H4,179,180,184)(H,267,268,269)/t85-,86-,87-,94-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,111-,112-,113-,114-,115-,116-,117-,118-,119-,120-,121-,131-,132-,133-/m0/s1

InChI Key

DXECUDAXXFQOCL-RVOUEEJYSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CO)C(=O)NC(CC(=O)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC(=O)O)C(=O)NC(CC1=CC=C(C=C1)OS(=O)(=O)O)C(=O)NC(CCSC)C(=O)NCC(=O)NC(CC2=CNC3=CC=CC=C32)C(=O)NC(CCSC)C(=O)NC(CC(=O)O)C(=O)NC(CC4=CC=CC=C4)C(=O)N)NC(=O)C(CCCNC(=N)N)NC(=O)C(CC5=CNC=N5)NC(=O)C(CO)NC(=O)C6CCCN6C(=O)C(CC(=O)O)NC(=O)C(CC(C)C)NC(=O)C(CC(=O)N)NC(=O)C(CCC(=O)N)NC(=O)C(CC(C)C)NC(=O)C(CC(=O)N)NC(=O)C(CCCCN)NC(=O)C(C(C)C)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(CCSC)NC(=O)C(CCCNC(=N)N)NC(=O)CNC(=O)C(CO)NC(=O)C7CCCN7C(=O)C(C)NC(=O)C(CCCCN)N

1. Characterization of cholecystokinin from the human brain

I Jardine,L J Miller,V L Go,D Speicher,E Weissman J Neurochem . 1984 Sep;43(3):835-40. doi: 10.1111/j.1471-4159.1984.tb12806.x.

Human forms of cholecystokinin have not previously been characterized chemically. In this study, we have extracted and purified the predominant molecular form of cholecystokinin present in human cerebral cortex. The peptide was characterized by amino acid analysis, automated peptide sequencing, and fast atom bombardment mass spectrometry. It appears to be identical to porcine cholecystokinin-octapeptide, with the sequence of Asp-Tyr(SO3)-Met-Gly-Trp-Met-Asp-Phe(NH2). This structural identity is consistent with the observations that the peptide in human brain and porcine cholecystokinin-octapeptide are recognized similarly by a battery of antisera to porcine cholecystokinin; that they coelute from several chromatographic systems, including gel filtration, ion exchange, and reversed-phase; and that they possess similar biological activities.

2. Cholecystokinin and adrenal-cortex secretion

Gastone G Nussdorfer,Raffaella Spinazzi,Giuseppina Mazzocchi Vitam Horm . 2005;71:433-53. doi: 10.1016/S0083-6729(05)71015-3.

Cholecystokinin, or CCK, is a 33-amino acid peptide, originally considered a gut hormone, that acts via two subtypes of receptors, named CCK1-R and CCK2-R. CCK, along with its receptors, has been subsequently localized in the central nervous system, where it exerts, among other fuctions, antiorexinogenic actions. In this survey, we describe findings indicating that CCK, similar to other peptides modulating food intake (e.g., neuropeptide Y, leptin, and orexins), is also able to regulate the function of the hypothalamo-pituitary-adrenal axis, acting on both its central and peripheral branches. CCK stimulates aldosterone secretion via specific receptors (CCK1-Rs and CCK2-Rs in rats, and CCK2-Rs in humans) located in zona glomerulosa cells and coupled to the adenylate cyclase-dependent signaling cascade; and enhances glucocorticoid secretion from zona fasciculata-reticularis cells via an indirect mechanism mainly involving the CCK2-R-mediated stimulation of corticotropin-releasing hormone-dependent ACTH release.

3. Human pancreatic acinar cells do not respond to cholecystokinin

Yan Bi,Richard M Mortensen,Diane Simeone,Craig D Logsdon,Baoan Ji Pharmacol Toxicol . 2002 Dec;91(6):327-32. doi: 10.1034/j.1600-0773.2002.910610.x.

Pancreatic secretion can be influenced by cholecystokinin (CCK) either directly via actions on acinar cells or indirectly via actions on nerves. The presence and functional roles of CCK receptors on human pancreatic acinar cells remains unclear. In the current study human pancreatic acini were isolated and then treated with CCK-8, gastrin and/or carbachol. Functional parameters were measured including intracellular [Ca2+] and amylase secretion. It was observed that human acini did not respond to CCK agonists but did respond to carbachol with robust increases in functional parameters. Adenoviral-mediated gene transfer of CCK1 or CCK2 receptors to the human cells resulted in cell responses to CCK agonists. In order to determine the reason for the lack of responsiveness of the human acini, expression of receptor mRNAs was determined using quantitative RT-PCR and localized by in situ hybridization. mRNA levels for CCK1 receptors were approximately 30 times lower than those of CCK2 receptors, which were approximately 10 times lower than those of m3 Ach receptors as measured by quantitative PCR. Neither CCK1 nor CCK2 receptors were localized in adult human pancreas by in situ hybridization. These results indicate that human pancreatic acinar cells do not respond directly to CCK receptor activation and this is likely due to an insufficient level of receptor expression.

4. Cholecystokinin attenuates β-cell apoptosis in both mouse and human islets

Joseph T Blumer,Carly R Kibbe,Danielle A Fontaine,Hung Tae Kim,Jacob T Bartosiak,Heidi Umhoefer,Jeeyoung Han,Arnaldo H Desouza,Mieke Baan,Dawn Belt Davis,Rashaun A Williams,Steven J Sacotte,Lucille Anzia Transl Res . 2022 May;243:1-13. doi: 10.1016/j.trsl.2021.10.005.

Loss of functional pancreatic β-cell mass and increased β-cell apoptosis are fundamental to the pathophysiology of type 1 and type 2 diabetes. Pancreatic islet transplantation has the potential to cure type 1 diabetes but is often ineffective due to the death of the islet graft within the first few years after transplant. Therapeutic strategies to directly target pancreatic β-cell survival are needed to prevent and treat diabetes and to improve islet transplant outcomes. Reducing β-cell apoptosis is also a therapeutic strategy for type 2 diabetes. Cholecystokinin (CCK) is a peptide hormone typically produced in the gut after food intake, with positive effects on obesity and glucose metabolism in mouse models and human subjects. We have previously shown that pancreatic islets also produce CCK. The production of CCK within the islet promotes β-cell survival in rodent models of diabetes and aging. We demonstrate a direct effect of CCK to reduce cytokine-mediated apoptosis in a β-cell line and in isolated mouse islets in a receptor-dependent manner. However, whether CCK can protect human β-cells was previously unknown. Here, we report that CCK can also reduce cytokine-mediated apoptosis in isolated human islets and CCK treatment in vivo decreases β-cell apoptosis in human islets transplanted into the kidney capsule of diabetic NOD/SCID mice. Collectively, these data identify CCK as a novel therapy that can directly promote β-cell survival in human islets and has therapeutic potential to preserve β-cell mass in diabetes and as an adjunct therapy after transplant.