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Collagen Triple Helix Repeat-Containing Protein 1 Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:NMTC1, CTHRC1
  • Species:Human
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Cat. No. Size Price


RD191394200R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Plasma-EDTA, Plasma-Heparin, Plasma-Citrate, Tissue extract

Sample Requirements

10 µl

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box)

Calibration Curve

Calibration Range

78 – 2500 pg/ml

Limit of Detection

27 pg/ml

Intra-assay (Within-Run)

n = 8; CV = 5.9 %

Inter-assay (Run-to-Run)

n = 8; CV = 5.1 %

Spiking Recovery

98.3 %

Dilutation Linearity

98.4 %

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3.5 hours
  • The kit measures human CTHRC1 in serum, plasma (EDTA, citrate, heparin) and tissue extracts
  • Assay format is 96 wells
  • Standard is recombinant protein based
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Atherosclerosis, Bone and cartilage metabolism, Cardiovascular disease, Coronary artery disease, Energy metabolism and body weight regulation, Oncology

Summary

Collagen triple helix repeat-containing protein 1 (CTHRC1) was identified in a screen for differentially expressed sequences in balloon-injured versus normal arteries. CTHRC1 expression was not detectable in normal arteries. However, on injury it was transiently expressed by fibroblasts of the remodeling adventitia and by smooth muscle cells of the neointima. It was also found in the matrix of calcifying human atherosclerotic plaques. CTHRC1 is a secreted 28-kDa protein that is glycosylated and highly conserved from lower chordates to mammals. A short collagen motif with 12 Gly-X-Y repeats appears to be responsible for trimerization of the protein and this renders the molecule susceptible to cleavage by collagenase. CTHRC1 is highly associated with calcified tissues and cartilaginous matrix, but not with endothelial cells. This is consistent with expression study results that showed CTHRC1 to be highly expressed in the developing skull bones, ribs, vertebrae, and cartilage primordia. CTHRC1 is a circulating factor detectable qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels were also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. Hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially broad implications for cell metabolism and physiology. Deletion of the CTHRC1 gene leads to fatty liver (steatosis) formation in mice while others showed that inactivation of this gene also results in low bone mass. CTHRC1 was identified in skeletal and cardiac muscles of mice, representing Duchenne and congenital muscle dystrophies (DMD and CMD) and dysferlinopathy. CTHRC1 is involved in postnatal bone formation and is secreted by mature functional osteoclasts. It acts on stromal/osteo­blastic cells by binding to a putative cell surface receptor in order to stimulate osteoblastic differentiation as well as recruitment, thereby promoting bone formation. Among the cancer cells reported to express CTHRC1 are melanomas, hepatocellular carcinoma, oral cancer, breast ductal carcinoma, pancreatic cancer, colorectal cancer, gastric cancer, and dermatofibrosarcoma protuberans, but a more recent study demonstrated that CTHRC1 expression in human cancers originates from activated stromal cells, not from the tumor cells themselves. CTHRC1 may have therapeutic value in antifibrotic treatment strategies and could have major clinical applications in the fields of vascular disease, repair, and fibrosis. The results indicate that CTHRC1 increases bone mass as a positive regulator of osteoblastic bone formation and offers an anabolic approach for the treatment of osteoporosis. CTHRC1 could serve as a potential marker for predicting progression and metastasis of the aforementioned types of cancers.

References to Summary

References to Collagen Triple Helix Repeat-Containing Protein 1

  • Chen YL, Wang TH, Hsu HC, Yuan RH, Jeng YM. Overexpression of CTHRC1 in hepatocellular carcinoma promotes tumor invasion and predicts poor prognosis. PLoS One. 2013;8 (7):e70324
  • Duarte CW, Stohn JP, Wang Q, Emery IF, Prueser A, Lindner V. Elevated plasma levels of the pituitary hormone Cthrc1 in individuals with red hair but not in patients with solid tumors. PLoS One. 2014;9 (6):e100449
  • Durmus T, LeClair RJ, Park KS, Terzic A, Yoon JK, Lindner V. Expression analysis of the novel gene collagen triple helix repeat containing-1 (Cthrc1). Gene Expr Patterns. 2006 Oct;6 (8):935-40
  • Kharaishvili G, Cizkova M, Bouchalova K, Mgebrishvili G, Kolar Z, Bouchal J. Collagen triple helix repeat containing 1 protein, periostin and versican in primary and metastatic breast cancer: an immunohistochemical study. J Clin Pathol. 2011 Nov;64 (11):977-82
  • Kim JH, Baek TH, Yim HS, Kim KH, Jeong SH, Kang HB, Oh SS, Lee HG, Kim JW, Kim KD. Collagen triple helix repeat containing-1 (CTHRC1) expression in invasive ductal carcinoma of the breast: the impact on prognosis and correlation to clinicopathologic features. Pathol Oncol Res. 2013 Oct;19 (4):731-7
  • Kimura H, Kwan KM, Zhang Z, Deng JM, Darnay BG, Behringer RR, Nakamura T, de Crombrugghe B, Akiyama H. Cthrc1 is a positive regulator of osteoblastic bone formation. PLoS One. 2008;3 (9):e3174
  • Liu G, Sengupta PK, Jamal B, Yang HY, Bouchie MP, Lindner V, Varelas X, Kukuruzinska MA. N-glycosylation induces the CTHRC1 protein and drives oral cancer cell migration. J Biol Chem. 2013 Jul 12;288 (28):20217-27
  • Palma M, Lopez L, Garcia M, de Roja N, Ruiz T, Garcia J, Rosell E, Vela C, Rueda P, Rodriguez MJ. Detection of collagen triple helix repeat containing-1 and nuclear factor (erythroid-derived 2)-like 3 in colorectal cancer. BMC Clin Pathol. 2012;12:2
  • Park EH, Kim S, Jo JY, Kim SJ, Hwang Y, Kim JM, Song SY, Lee DK, Koh SS. Collagen triple helix repeat containing-1 promotes pancreatic cancer progression by regulating migration and adhesion of tumor cells. Carcinogenesis. 2013 Mar;34 (3):694-702
  • Pyagay P, Heroult M, Wang Q, Lehnert W, Belden J, Liaw L, Friesel RE, Lindner V. Collagen triple helix repeat containing 1, a novel secreted protein in injured and diseased arteries, inhibits collagen expression and promotes cell migration. Circ Res. 2005 Feb 4;96 (2):261-8
  • Spector I, Zilberstein Y, Lavy A, Genin O, Barzilai-Tutsch H, Bodanovsky A, Halevy O, Pines M. The involvement of collagen triple helix repeat containing 1 in muscular dystrophies. Am J Pathol. 2013 Mar;182 (3):905-16
  • Stohn JP, Perreault NG, Wang Q, Liaw L, Lindner V. Cthrc1, a novel circulating hormone regulating metabolism. PLoS One. 2012;7 (10):e47142
  • Takeshita S, Fumoto T, Matsuoka K, Park KA, Aburatani H, Kato S, Ito M, Ikeda K. Osteoclast-secreted CTHRC1 in the coupling of bone resorption to formation. J Clin Invest. 2013 Sep;123 (9):3914-24
  • Tan F, Liu F, Liu H, Hu Y, Liu D, Li G. CTHRC1 is associated with peritoneal carcinomatosis in colorectal cancer: a new predictor for prognosis. Med Oncol. 2013 Mar;30 (1):473
  • Tang L, Dai DL, Su M, Martinka M, Li G, Zhou Y. Aberrant expression of collagen triple helix repeat containing 1 in human solid cancers. Clin Cancer Res. 2006 Jun 15;12 (12):3716-22
  • Zhang G, Li G. Novel multiple markers to distinguish melanoma from dysplastic nevi. PLoS One. 2012;7 (9):e45037
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