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the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system
amide combining the amino group of one amino acid with the carboxyl group of another; usually obtained by partial hydrolysis of protein

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carbonの化学記号
cesiumの化学記号
cadmiumの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/02/11 05:10:41」(JST)

wiki en

Not to be confused with C-reactive protein or Protein C.

The connecting peptide, or C-peptide, is a short 31-amino-acid protein that connects insulin's A-chain to its B-chain in the proinsulin molecule.

In the insulin synthesis pathway, first preproinsulin is translocated into the endoplasmic reticulum of beta cells of the pancreas with an A-chain, a C-peptide, a B-chain, and a signal sequence. The signal sequence is cleaved from the N-terminus of the peptide by a signal peptidase, leaving proinsulin. After proinsulin is packaged into vesicles in the Golgi apparatus, the C-peptide is removed, leaving the A-chain and B-chain, bound together by disulfide bonds, that constitute the insulin molecule.

History[edit]

Proinsulin C-peptide was first described in 1967 in connection with the discovery of the insulin biosynthesis pathway.^[2] It serves as a linker between the A- and the B- chains of insulin and facilitates the efficient assembly, folding, and processing of insulin in the endoplasmic reticulum. Equimolar amounts of C-peptide and insulin are then stored in secretory granules of the pancreatic beta cells and both are eventually released to the portal circulation. Initially, the sole interest in C-peptide was as a marker of insulin secretion and has as such been of great value in furthering the understanding of the pathophysiology of type 1 and type 2 diabetes. The first documented use of the C-peptide test was in 1972. During the past decade, however, C-peptide has been found to be a bioactive peptide in its own right, with effects on microvascular blood flow and tissue health.

Function[edit]

Cellular effects of C-peptide[edit]

C-peptide has been shown to bind to the surface of a number of cell types such as neuronal, endothelial, fibroblast and renal tubular, at nanomolar concentrations to a receptor that is likely G-protein-coupled. The signal activates Ca²⁺-dependent intracellular signaling pathways such as MAPK, PLCγ, and PKC, leading to upregulation of a range of transcription factors as well as eNOS and Na+K+ATPase activities.^[3] The latter two enzymes are known to have reduced activities in patients with type I diabetes and have been implicated in the development of long-term complications of type I diabetes such as peripheral and autonomic neuropathy.

In vivo studies in animal models of type 1 diabetes have established that C-peptide administration results in significant improvements in nerve and kidney function. Thus, in animals with early signs of diabetes-induced neuropathy, C peptide treatment in replacement dosage results in improved peripheral nerve function, as evidenced by increased nerve conduction velocity, increased nerve Na+,K+ ATPase activity, and significant amelioration of nerve structural changes.^[4] Likewise, C-peptide administration in animals that had C-peptide deficiency (type 1 model) with nephropathy improves renal function and structure; it decreases urinary albumin excretion and prevents or decreases diabetes-induced glomerular changes secondary to mesangial matrix expansion.^[5]^[6]^[7]^[8] C-peptide also has been reported to have anti-inflammatory effects as well as aid repair of smooth muscle cells.^[9]^[10]

Clinical uses of C-peptide testing[edit]

Patients with diabetes may have their C-peptide levels measured as a means of distinguishing type 1 diabetes from type 2 diabetes or Maturity Onset Diabetes of the Young (MODY)^[11]. Measuring C-peptide can help to determine how much of their own natural insulin a person is producing as C-peptide is secreted in equimolar amounts to insulin. C-peptide levels are measured instead of insulin levels because C-peptide can assess a persons own insulin secretion even if they receive insulin injections, and because the liver metabolizes a large and variable amount of insulin secreted into the portal vein but does not metabolise C-peptide, meaning blood C-peptide may be a better measure of portal insulin secretion than insulin itself^[12]^[13]. A very low C-peptide confirms Type 1 diabetes and insulin dependence and is associated with high glucose variability, hypoglycaemia and increased complications. The test may be less helpful close to diagnosis, particularly where a patient is overweight and insulin resistant, as levels close to diagnosis in Type 1 diabetes may be high and overlap with those seen in type 2 diabetes.

Differential diagnosis of hypoglycemia. The test may be used to help determine the cause of hypoglycaemia (low glucose), values will be low if a person has taken an overdose of insulin but not suppressed if hypoglycaemia is due to an insulinoma or sulphonylureas.

C-peptide may be used for determining the possibility of gastrinomas associated with Multiple Endocrine Neoplasm syndromes (MEN 1). Since a significant number of gastrinomas are associated with MEN involving other hormone producing organs (pancreas, parathyroids, and pituitary), higher levels of C-peptide together with the presence of a gastrinoma suggest that organs besides the stomach may harbor neoplasms.

C-peptide levels may be checked in women with Polycystic Ovarian Syndrome (PCOS) to help determine degree of insulin resistance.

Therapeutics[edit]

Several physiological effects have been observed in several Phase 1 and exploratory Phase 2 studies in almost 300 type 1 diabetes patients, who lacked endogenous C-peptide. Improvements were seen on diabetic peripheral neuropathy, nephropathy and other decrements associated with long-term complications of type I diabetes.^[14]^[15]^[16]^[17]^[18]^[19]^[20]^[21]^[22] So far, dosing with C-peptide has shown to be safe and there were no effects of C-peptide demonstrated in healthy subjects (who make their own C-peptide).

References[edit]

^ C-Peptide - Compound Summary, PubChem.
^ Steiner D.F., Cunningham D., Spigelman L., Aten B. (1967). "Insulin Biosynthesis: Evidence for a Precursor". Science 157 (3789): 697–700. doi:10.1126/science.157.3789.697. PMID 4291105.
^ Hills CE, Brunskill NJ (2008). "Intracellular signalling by C-peptide". Exp Diabetes Res 2008: 635158. doi:10.1155/2008/635158. PMC 2276616. PMID 18382618.
^ Sima AA, Zhang W, Sugimoto K, et al. (July 2001). "C-peptide prevents and improves chronic Type I diabetic polyneuropathy in the BB/Wor rat". Diabetologia 44 (7): 889–97. doi:10.1007/s001250100570. PMID 11508275.
^ Samnegård B, Jacobson SH, Jaremko G, Johansson BL, Sjöquist M (October 2001). "Effects of C-peptide on glomerular and renal size and renal function in diabetic rats". Kidney Int. 60 (4): 1258–65. doi:10.1046/j.1523-1755.2001.00964.x. PMID 11576340.
^ Samnegård B, Jacobson SH, Jaremko G, et al. (March 2005). "C-peptide prevents glomerular hypertrophy and mesangial matrix expansion in diabetic rats". Nephrol. Dial. Transplant. 20 (3): 532–8. doi:10.1093/ndt/gfh683. PMID 15665028.
^ Nordquist L, Brown R, Fasching A, Persson P, Palm F (November 2009). "Proinsulin C-peptide reduces diabetes-induced glomerular hyperfiltration via efferent arteriole dilation and inhibition of tubular sodium reabsorption". Am. J. Physiol. Renal Physiol. 297 (5): F1265–72. doi:10.1152/ajprenal.00228.2009. PMC 2781335. PMID 19741019.
^ Nordquist L, Wahren J (2009). "C-Peptide: the missing link in diabetic nephropathy?". Rev Diabet Stud 6 (3): 203–10. doi:10.1900/RDS.2009.6.203. PMC 2827272. PMID 20039009.
^ Luppi P, Cifarelli V, Tse H, Piganelli J, Trucco M (August 2008). "Human C-peptide antagonises high glucose-induced endothelial dysfunction through the nuclear factor-kappaB pathway". Diabetologia 51 (8): 1534–43. doi:10.1007/s00125-008-1032-x. PMID 18493738.
^ Mughal RS, Scragg JL, Lister P, et al. (August 2010). "Cellular mechanisms by which proinsulin C-peptide prevents insulin-induced neointima formation in human saphenous vein". Diabetologia 53 (8): 1761–71. doi:10.1007/s00125-010-1736-6. PMC 2892072. PMID 20461358.
^ Jones AG, Hattersley AT. The clinical utility of C-peptide measurement in the care of patients with diabetes. Diabetic Medicine 2013 Jul;30(7):803-17.
^ Clark PM. Assays for insulin, proinsulin and C-peptide. Ann Clin Biochem 1999;36:541-564
^ Shapiro ET, Tillil H, Rubenstein AH, Polonsky KS. Peripheral insulin parallels changes in insulin secretion more closely than C-peptide after bolus intravenous glucose administration. J Clin Endocrinol Metab. 1988 Nov;67(5):1094-9
^ Johansson BL, Borg K, Fernqvist-Forbes E, Kernell A, Odergren T, Wahren J (2000). "Beneficial effects of C-peptide on incipient nephropathy and neuropathy in patients with Type 1 diabetes mellitus". Diabet. Med. 17 (3): 181–9. doi:10.1046/j.1464-5491.2000.00274.x. PMID 10784221. "Respiratory heart rate variability increased by 21 +/- 9% (P < 0.05) during treatment with C-peptide [...] C-peptide ameliorates autonomic and sensory nerve dysfunction in patients with Type 1 diabetes mellitus." |accessdate= requires |url= (help)
^ Marques RG, Fontaine MJ, Rogers J (2004). "C-peptide: much more than a byproduct of insulin biosynthesis". Pancreas 29 (3): 231–8. PMID 15367890. |accessdate= requires |url= (help)
^ Wahren J, Ekberg K, Samnegård B, Johansson BL (2001). "C-peptide: a new potential in the treatment of diabetic nephropathy". Curr. Diab. Rep. 1 (3): 261–6. doi:10.1007/s11892-001-0044-4. PMID 12643208. "Administration of C-peptide to physiologic concentrations in patients with type 1 diabetes and incipient nephropathy for periods of 3 hours to 3 months is accompanied by reduced glomerular hyperfiltration and filtration fraction, and diminished urinary albumin excretion. C-peptide replacement together with insulin therapy may be beneficial in type 1 diabetes patients with nephropathy." |accessdate= requires |url= (help)
^ Wahren J (2004). "C-peptide: new findings and therapeutic implications in diabetes". Clin Physiol Funct Imaging 24 (4): 180–9. doi:10.1111/j.1475-097X.2004.00558.x. PMID 15233831. "In patients with type 1 diabetes, beneficial effects have been demonstrated on sensory nerve conduction velocity, vibration perception and autonomic nerve function. C-peptide also augments blood flow in several tissues in type 1 diabetes via its stimulation of endothelial NO release, emphasizing a role for C-peptide in maintaining vascular homeostasis." |accessdate= requires |url= (help)
^ Kamiya H, Zhang W, Sima AA (2004). "C-peptide prevents nociceptive sensory neuropathy in type 1 diabetes". Ann. Neurol. 56 (6): 827–35. doi:10.1002/ana.20295. PMID 15497155. "we conclude that replacement of insulinomimetic C-peptide prevents abnormalities of neurotrophins, their receptors, and nociceptive neuropeptides in type 1 BB/Wor-rats, resulting in the prevention of C-fiber pathology and nociceptive sensory nerve dysfunction. The data indicate that perturbed insulin/C-peptide action plays an important pathogenetic role in nociceptive sensory neuropathy and that C-peptide replacement may be of benefit in treating painful diabetic neuropathy in insulin-deficient diabetic conditions." |accessdate= requires |url= (help)
^ Ziegler D (2004). "Polyneuropathy in the diabetic patient--update on pathogenesis and management". Nephrol. Dial. Transplant. 19 (9): 2170–5. doi:10.1093/ndt/gfh398. PMID 15252164. Retrieved 2008-01-07.
^ Wahren J, Ekberg K, Jörnvall H (2007). "C-peptide is a bioactive peptide". Diabetologia 50 (3): 503–9. doi:10.1007/s00125-006-0559-y. PMID 17235526. |accessdate= requires |url= (help)
^ Wahren, J (February 2007). "C-peptide and Neuropathy in Type 1 Diabetes". Immunology, Endocrine & Metabolic Agents - Medicinal Chemistry 7 (1): 69–77. doi:10.2174/187152207779802455. Retrieved 2008-01-07. "C-peptide corrects diabetes-induced reductions in endoneurial blood flow and in Na+,K+-ATPase activity. In vitro studies demonstrate that C-peptide binds specifically to cell membranes, activating a G-protein-coupled receptor as well as Ca2+-, PKC-, and MAPK-dependent signaling pathways, resulting in stimulation of Na+,K+-ATPase and endothelial nitric oxide synthase (eNOS). In addition, C-peptide activates transcription factors resulting in augmented eNOS mRNA and protein content of endothelial cells and modulation of neurotrophic factors as well as apoptotic phenomena in neuroblastoma cells. Combined, the results demonstrate that C-peptide is a bioactive peptide, possibly of importance in the treatment of neuropathy in type 1 diabetes."
^ Dan Ziegler. "New drugs to prevent or treat diabetic polyneuropathy" (pdf). Retrieved 2008-01-07. ^{[dead link]}

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 糖尿病でない成人における低血糖症：診断的アプローチ hypoglycemia in adults without diabetes mellitus diagnostic approach
2. 1型糖尿病の病因 pathogenesis of type 1 diabetes mellitus
3. 虚偽性低血糖 factitious hypoglycemia
4. 2型糖尿病の治療のためのジペプチジルペプチダーゼ4（DPP-4）阻害剤 dipeptidyl peptidase 4 dpp 4 inhibitors for the treatment of type 2 diabetes mellitus
5. Evaluation of and initial approach to the adult patient with undifferentiated hypotension and shock

English Journal

Transfection with follicular dendritic cell secreted protein to affect phenotype expression of human periodontal ligament cells.

Xiang L1, Ma L, He Y, Wei N, Gong P.Author information 1State Key Laboratory of Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, 610041, P.R. China; Dental Implant Center, West China Hospital of Stomatology, Sichuan University, Chengdu, 610041, P.R. China.AbstractFollicular dendritic cell secreted protein (FDC-SP), has been found to inhibit osteogenic differentiation of human periodontal ligament cells (hPDLCs) in recent studies. Based on these findings, we further investigate its effect on phenotype expression of hPDLCs in the present study, aiming to contribute to a better understanding of the biological functions governing FDC-SP-induced hPDLC differentiation. hPDLCs were firstly identified with immunocytochemical staining, followed by transfection with FDC-SP lentiviral vector. Western blot analysis was used to confirm the expression of FDC-SP. Then the influence of FDC-SP transfection on hPDLC proliferation, osteogenic and fibrogenic phenotype expression was evaluated at the mRNA and protein level. Procollagen type I c-peptide production was measured and alizarin red staining was then conducted to demonstrate effect of FDC-SP on functional differentiation. We found that hPDLCs could be successfully transfected with FDC-SP. Cell proliferation and cell cycle tests indicated that transfection with FDC-SP did not affect hPDLC proliferation. Moreover, according to real-time PCR and Western blot results, expression levels of type 1 collagen alpha 1, type 1 collagen alpha 2 and type 3 collagen were upregulated while that of osteocalcin, osteopontin, and bone sialoprotein were downregulated in FDC-SP transfected cells. In addition, hPDLCs overexpressing FDC-SP exhibited higher PIP production than the controls. Our findings demonstrate that transfection with FDC-SP has negligible adverse effect on proliferation of hPDLCs and imply the biological function of FDC-SP as a fibroblastic phenotype stabilizer by inhibiting hPDLCs differentiation into mineralized tissue-forming cells, thus regulating regeneration in periodontal tissue engineering. J. Cell. Biochem. 115: 940-948, 2014. © 2013 Wiley Periodicals, Inc.
Journal of cellular biochemistry.J Cell Biochem.2014 May;115(5):940-8. doi: 10.1002/jcb.24736.
Follicular dendritic cell secreted protein (FDC-SP), has been found to inhibit osteogenic differentiation of human periodontal ligament cells (hPDLCs) in recent studies. Based on these findings, we further investigate its effect on phenotype expression of hPDLCs in the present study, aiming to contr
PMID 24357406

Effect and mechanisms of human Wharton's jelly-derived mesenchymal stem cells on type 1 diabetes in NOD model.

Hu J1, Wang Y, Wang F, Wang L, Yu X, Sun R, Wang Z, Wang L, Gao H, Fu Z, Zhao W, Yan S.Author information 1Stem Cell Research Center, The Affiliated Hospital of Medical College, Qingdao University, No. 16, Jiangsu Road, Qingdao, 266003, China.AbstractType 1 diabetes is an autoimmune disease that results from an inflammatory destruction of β-cells in islets. Mesenchymal stem cells derived from Wharton's jelly (WJ-MSCs) own a peculiar immunomodulatory feature and might reverse the inflammatory destruction and repair the function of β-cells. Sixty NOD mice were divided into four groups, including normal control group, WJ-MSCs prevention group (before onset), WJ-MSCs treatment group (after onset), and diabetic control group. After homologous therapy, onset time of diabetes, levels of fasting plasma glucose (FPG), fed blood glucose and C-peptide, regulation of cytokines, and islet cells were examined and evaluated. After WJ-MSCs infusion, FPG and fed blood glucose in WJ-MSCs treatment group decreased to normal level in 6-8 days and maintained for 6 weeks. Level of fasting C-peptide of these mice was higher compared to diabetic control mice (P = 0.027). In WJ-MSCs prevention group, WJ-MSCs played a protective role for 8-week delayed onset of diabetes, and fasting C-peptide in this group was higher compared to the other two diabetic groups (P = 0.013, 0.035). Compared with diabetic control group, frequencies of CD4+CD25+Foxp3+ Tregs in WJ-MSCs prevention group and treatment group were higher, while levels of IL-2, IFN-γ, and TNF-α were lower (P < 0.001); the degree of insulitis was also depressed, especially for WJ-MSCs prevention group(P < 0.05). Infusion of WJ-MSCs could aid in T1DM through regulation of the autoimmunity and recovery of islet β-cells no matter before or after onset of T1DM. WJ-MSCs might be an effective method for T1DM.
Endocrine.Endocrine.2014 Mar 4. [Epub ahead of print]
Type 1 diabetes is an autoimmune disease that results from an inflammatory destruction of β-cells in islets. Mesenchymal stem cells derived from Wharton's jelly (WJ-MSCs) own a peculiar immunomodulatory feature and might reverse the inflammatory destruction and repair the function of β-cells. Sixt
PMID 24590294

Endocrine responses, weight change, and energy sparing mechanisms during Ramadan among Gambian adolescent women.

Reiches MW1, Moore SE, Prentice AM, Ellison PT.Author information 1Department of Anthropology, University of Massachusetts Boston, Boston, Massachusetts.AbstractOBJECTIVES: Ramadan fasting imposes a diurnal rather than a chronic energetic challenge. When Ramadan occurs during the agricultural season in subsistence populations, diurnal and chronic effects combine. The impact of layered energetic challenges on adolescent activity, metabolism, and body composition have not been quantified. This study compares the effects of a Ramadan (30 July-3 October 2009) and subsequent non-Ramadan (14 July-12 August 2010) agricultural season in 67 Gambian subsistence agriculturalist women between 14 and 20 years old.
American journal of human biology : the official journal of the Human Biology Council.Am J Hum Biol.2014 Mar 3. doi: 10.1002/ajhb.22531. [Epub ahead of print]
OBJECTIVES: Ramadan fasting imposes a diurnal rather than a chronic energetic challenge. When Ramadan occurs during the agricultural season in subsistence populations, diurnal and chronic effects combine. The impact of layered energetic challenges on adolescent activity, metabolism, and body composi
PMID 24590590

Japanese Journal

Proinsulin C-peptide activates α-enolase : implications for C-peptide-cell membrane interaction

Ishii Tatsuya,Fukano Keigo,Shimada Kohei [他]
Journal of Biochemistry 152(1), 53-62, 2012-07
NAID 40019351035

症例報告 1型糖尿病発症前より血糖値,インスリン分泌能の変遷を観察し得た,多腺性自己免疫症候群3型の1例

添田幸恵,田中久美子,税所芳史 [他]
糖尿病 55(5), 340-344, 2012-05
NAID 40019347818

Related Pictures

★リンクテーブル★

リンク元	「Cペプチド」
関連記事	「C」「Cs」「Cd」「c」

「Cペプチド」

C-peptide
Identifiers
CAS number	59112-80-0
PubChem	16132309
ChemSpider	17288968
MeSH	C-Peptide
Jmol-3D images	Image 1
	SMILES CC(C)CC(C(=O)NC(C)C(=O)NC(CC(C)C)C(=O)NC(CCC(=O)O)C(=O)NCC(=O)NCC(=O)NCC(=O)NC(CCC(=O)N)C(=O)O)NC(=O)CNC(=O)C(CCC(=O)N)NC(=O)C(CC(C)C)NC(=O)CNC(=O)CNC(=O)C(C)NC(=O)CNC(=O)C1CCCN1C(=O)CNC(=O)CNC(=O)CNC(=O)C(CC(C)C)NC(=O)C(CCC(=O)O)NC(=O)CNC(=O)C(CCC(=O)N)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(CCC(=O)N)NC(=O)CNC(=O)C(CC(=O)O)NC(=O)C(CCC(=O)O)NC(=O)CNC(=O)C(CCC(=O)O)N ;
	InChI InChI=1S/C112H179N35O46/c1-51(2)32-66(144-104(184)63(21-29-92(170)171)137-85(161)46-127-99(179)59(16-23-72(114)148)134-87(163)49-131-111(191)95(55(9)10)146-106(186)62(18-25-74(116)150)135-86(162)47-129-103(183)70(36-94(174)175)145-105(185)64(22-30-93(172)173)136-84(160)45-124-98(178)58(113)15-27-90(166)167)102(182)126-41-80(156)119-38-77(153)122-50-89(165)147-31-13-14-71(147)110(190)130-44-81(157)132-56(11)96(176)123-39-78(154)121-43-83(159)140-68(34-53(5)6)108(188)141-60(17-24-73(115)149)100(180)128-48-88(164)139-67(33-52(3)4)107(187)133-57(12)97(177)143-69(35-54(7)8)109(189)142-61(20-28-91(168)169)101(181)125-40-79(155)118-37-76(152)120-42-82(158)138-65(112(192)193)19-26-75(117)151/h51-71,95H,13-50,113H2,1-12H3,(H2,114,148)(H2,115,149)(H2,116,150)(H2,117,151)(H,118,155)(H,119,156)(H,120,152)(H,121,154)(H,122,153)(H,123,176)(H,124,178)(H,125,181)(H,126,182)(H,127,179)(H,128,180)(H,129,183)(H,130,190)(H,131,191)(H,132,157)(H,133,187)(H,134,163)(H,135,162)(H,136,160)(H,137,161)(H,138,158)(H,139,164)(H,140,159)(H,141,188)(H,142,189)(H,143,177)(H,144,184)(H,145,185)(H,146,186)(H,166,167)(H,168,169)(H,170,171)(H,172,173)(H,174,175)(H,192,193)/t56-,57-,58-,59-,60-,61-,62-,63-,64-,65-,66-,67-,68-,69-,70-,71-,95-/m0/s1 ; Key: XTUNIGNWBZZIPT-NTMYLOQBSA-N InChI=1/C112H179N35O46/c1-51(2)32-66(144-104(184)63(21-29-92(170)171)137-85(161)46-127-99(179)59(16-23-72(114)148)134-87(163)49-131-111(191)95(55(9)10)146-106(186)62(18-25-74(116)150)135-86(162)47-129-103(183)70(36-94(174)175)145-105(185)64(22-30-93(172)173)136-84(160)45-124-98(178)58(113)15-27-90(166)167)102(182)126-41-80(156)119-38-77(153)122-50-89(165)147-31-13-14-71(147)110(190)130-44-81(157)132-56(11)96(176)123-39-78(154)121-43-83(159)140-68(34-53(5)6)108(188)141-60(17-24-73(115)149)100(180)128-48-88(164)139-67(33-52(3)4)107(187)133-57(12)97(177)143-69(35-54(7)8)109(189)142-61(20-28-91(168)169)101(181)125-40-79(155)118-37-76(152)120-42-82(158)138-65(112(192)193)19-26-75(117)151/h51-71,95H,13-50,113H2,1-12H3,(H2,114,148)(H2,115,149)(H2,116,150)(H2,117,151)(H,118,155)(H,119,156)(H,120,152)(H,121,154)(H,122,153)(H,123,176)(H,124,178)(H,125,181)(H,126,182)(H,127,179)(H,128,180)(H,129,183)(H,130,190)(H,131,191)(H,132,157)(H,133,187)(H,134,163)(H,135,162)(H,136,160)(H,137,161)(H,138,158)(H,139,164)(H,140,159)(H,141,188)(H,142,189)(H,143,177)(H,144,184)(H,145,185)(H,146,186)(H,166,167)(H,168,169)(H,170,171)(H,172,173)(H,174,175)(H,192,193)/t56-,57-,58-,59-,60-,61-,62-,63-,64-,65-,66-,67-,68-,69-,70-,71-,95-/m0/s1; Key: XTUNIGNWBZZIPT-NTMYLOQBBL ;
Properties
Molecular formula	C112H179N35O46
Molar mass	3020.29 g/mol
	(verify) (what is: /?); Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
	Infobox references

　　[★]

英: C-peptide、connecting peptide
同: C-ペプチド
関: インスリン

プロインスリン架橋ペプチド

http://www.crc-group.co.jp/crc/q_and_a/127.html 糖尿病患者ではインスリン分泌能の指標となり、24時間尿中CPRが20μg/日以下、または空腹時血中CPRが0.5ng/mL以下であれば、インスリン分泌が高度に低下した状態（インスリン依存状態）と考えられ、インスリン治療が必要とされます。　　さらに、2型糖尿病患者において治療法を選択する上で、早朝空腹時のCPRインデックス（CPI）が有用な指標として使用されています。　　CPI＝血中CPR÷血糖値×100 　　CPIが1.2以上の場合、食事・経口薬治療で、0.8未満の場合、インスリン治療で良好な血糖コントロールが得られると報告されています。　　ただし、CPRの大部分は腎において代謝・排泄されるため、腎機能障害では血中CPRが高値に、尿中CPRが低値に傾くので注意を要します。また、24時間尿中CPR排泄量では正確な蓄尿と、日差間のバラツキがあるため連続3日間の測定が重要です。

「C」

　　[★]

炭素 carbon
シトシン cytosine
システイン cysteine
シチジン
セルシウス度摂氏 degrees Celsius degree C
産婦人科領域で「子宮外頚子宮外頚部 exocervix」を表現するための略語

「Cs」

　　[★] セシウム, caesium, cesium 　

「Cd」

　　[★] カドミウム

関: cadmium

「c」

　　[★]

光速, speed of light

[1] C-Peptide - Compound Summary, PubChem.

[2] Steiner D.F., Cunningham D., Spigelman L., Aten B. (1967). "Insulin Biosynthesis: Evidence for a Precursor". Science 157 (3789): 697–700. doi:10.1126/science.157.3789.697. PMID 4291105.

[3] Hills CE, Brunskill NJ (2008). "Intracellular signalling by C-peptide". Exp Diabetes Res 2008: 635158. doi:10.1155/2008/635158. PMC 2276616. PMID 18382618.

[4] Sima AA, Zhang W, Sugimoto K, et al. (July 2001). "C-peptide prevents and improves chronic Type I diabetic polyneuropathy in the BB/Wor rat". Diabetologia 44 (7): 889–97. doi:10.1007/s001250100570. PMID 11508275.

[5] Samnegård B, Jacobson SH, Jaremko G, Johansson BL, Sjöquist M (October 2001). "Effects of C-peptide on glomerular and renal size and renal function in diabetic rats". Kidney Int. 60 (4): 1258–65. doi:10.1046/j.1523-1755.2001.00964.x. PMID 11576340.

[6] Samnegård B, Jacobson SH, Jaremko G, et al. (March 2005). "C-peptide prevents glomerular hypertrophy and mesangial matrix expansion in diabetic rats". Nephrol. Dial. Transplant. 20 (3): 532–8. doi:10.1093/ndt/gfh683. PMID 15665028.

[7] Nordquist L, Brown R, Fasching A, Persson P, Palm F (November 2009). "Proinsulin C-peptide reduces diabetes-induced glomerular hyperfiltration via efferent arteriole dilation and inhibition of tubular sodium reabsorption". Am. J. Physiol. Renal Physiol. 297 (5): F1265–72. doi:10.1152/ajprenal.00228.2009. PMC 2781335. PMID 19741019.

[8] Nordquist L, Wahren J (2009). "C-Peptide: the missing link in diabetic nephropathy?". Rev Diabet Stud 6 (3): 203–10. doi:10.1900/RDS.2009.6.203. PMC 2827272. PMID 20039009.

[9] Luppi P, Cifarelli V, Tse H, Piganelli J, Trucco M (August 2008). "Human C-peptide antagonises high glucose-induced endothelial dysfunction through the nuclear factor-kappaB pathway". Diabetologia 51 (8): 1534–43. doi:10.1007/s00125-008-1032-x. PMID 18493738.

[10] Mughal RS, Scragg JL, Lister P, et al. (August 2010). "Cellular mechanisms by which proinsulin C-peptide prevents insulin-induced neointima formation in human saphenous vein". Diabetologia 53 (8): 1761–71. doi:10.1007/s00125-010-1736-6. PMC 2892072. PMID 20461358.

[11] Jones AG, Hattersley AT. The clinical utility of C-peptide measurement in the care of patients with diabetes. Diabetic Medicine 2013 Jul;30(7):803-17.

[12] Clark PM. Assays for insulin, proinsulin and C-peptide. Ann Clin Biochem 1999;36:541-564

[13] Shapiro ET, Tillil H, Rubenstein AH, Polonsky KS. Peripheral insulin parallels changes in insulin secretion more closely than C-peptide after bolus intravenous glucose administration. J Clin Endocrinol Metab. 1988 Nov;67(5):1094-9

[pmid10784221-14] Johansson BL, Borg K, Fernqvist-Forbes E, Kernell A, Odergren T, Wahren J (2000). "Beneficial effects of C-peptide on incipient nephropathy and neuropathy in patients with Type 1 diabetes mellitus". Diabet. Med. 17 (3): 181–9. doi:10.1046/j.1464-5491.2000.00274.x. PMID 10784221. "Respiratory heart rate variability increased by 21 +/- 9% (P < 0.05) during treatment with C-peptide [...] C-peptide ameliorates autonomic and sensory nerve dysfunction in patients with Type 1 diabetes mellitus." |accessdate= requires |url= (help)

[Marquez-15] Marques RG, Fontaine MJ, Rogers J (2004). "C-peptide: much more than a byproduct of insulin biosynthesis". Pancreas 29 (3): 231–8. PMID 15367890. |accessdate= requires |url= (help)

[pmid12643208-16] Wahren J, Ekberg K, Samnegård B, Johansson BL (2001). "C-peptide: a new potential in the treatment of diabetic nephropathy". Curr. Diab. Rep. 1 (3): 261–6. doi:10.1007/s11892-001-0044-4. PMID 12643208. "Administration of C-peptide to physiologic concentrations in patients with type 1 diabetes and incipient nephropathy for periods of 3 hours to 3 months is accompanied by reduced glomerular hyperfiltration and filtration fraction, and diminished urinary albumin excretion. C-peptide replacement together with insulin therapy may be beneficial in type 1 diabetes patients with nephropathy." |accessdate= requires |url= (help)

[pmid15233831-17] Wahren J (2004). "C-peptide: new findings and therapeutic implications in diabetes". Clin Physiol Funct Imaging 24 (4): 180–9. doi:10.1111/j.1475-097X.2004.00558.x. PMID 15233831. "In patients with type 1 diabetes, beneficial effects have been demonstrated on sensory nerve conduction velocity, vibration perception and autonomic nerve function. C-peptide also augments blood flow in several tissues in type 1 diabetes via its stimulation of endothelial NO release, emphasizing a role for C-peptide in maintaining vascular homeostasis." |accessdate= requires |url= (help)

[pmid15497155-18] Kamiya H, Zhang W, Sima AA (2004). "C-peptide prevents nociceptive sensory neuropathy in type 1 diabetes". Ann. Neurol. 56 (6): 827–35. doi:10.1002/ana.20295. PMID 15497155. "we conclude that replacement of insulinomimetic C-peptide prevents abnormalities of neurotrophins, their receptors, and nociceptive neuropeptides in type 1 BB/Wor-rats, resulting in the prevention of C-fiber pathology and nociceptive sensory nerve dysfunction. The data indicate that perturbed insulin/C-peptide action plays an important pathogenetic role in nociceptive sensory neuropathy and that C-peptide replacement may be of benefit in treating painful diabetic neuropathy in insulin-deficient diabetic conditions." |accessdate= requires |url= (help)

[pmid15252164-19] Ziegler D (2004). "Polyneuropathy in the diabetic patient--update on pathogenesis and management". Nephrol. Dial. Transplant. 19 (9): 2170–5. doi:10.1093/ndt/gfh398. PMID 15252164. Retrieved 2008-01-07.

[pmid17235526-20] Wahren J, Ekberg K, Jörnvall H (2007). "C-peptide is a bioactive peptide". Diabetologia 50 (3): 503–9. doi:10.1007/s00125-006-0559-y. PMID 17235526. |accessdate= requires |url= (help)

[titleIngentaConnect_C-peptide_and_Neuropathy_in_Type_1_Diabetes-21] Wahren, J (February 2007). "C-peptide and Neuropathy in Type 1 Diabetes". Immunology, Endocrine & Metabolic Agents - Medicinal Chemistry 7 (1): 69–77. doi:10.2174/187152207779802455. Retrieved 2008-01-07. "C-peptide corrects diabetes-induced reductions in endoneurial blood flow and in Na+,K+-ATPase activity. In vitro studies demonstrate that C-peptide binds specifically to cell membranes, activating a G-protein-coupled receptor as well as Ca2+-, PKC-, and MAPK-dependent signaling pathways, resulting in stimulation of Na+,K+-ATPase and endothelial nitric oxide synthase (eNOS). In addition, C-peptide activates transcription factors resulting in augmented eNOS mRNA and protein content of endothelial cells and modulation of neurotrophic factors as well as apoptotic phenomena in neuroblastoma cells. Combined, the results demonstrate that C-peptide is a bioactive peptide, possibly of importance in the treatment of neuropathy in type 1 diabetes."

[zeigler2-22] Dan Ziegler. "New drugs to prevent or treat diabetic polyneuropathy" (pdf). Retrieved 2008-01-07. ^{[dead link]}

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C-peptide