Top

Journal of Cancer Research and Clinical Oncology

Published in:

01-12-2018 | Review – Cancer Research

The heat shock protein 47 as a potential biomarker and a therapeutic agent in cancer research

Authors: Beatriz Dal Pont Duarte, Diego Bonatto

Published in: Journal of Cancer Research and Clinical Oncology | Issue 12/2018

Abstract

Heat shock protein 47 (HSP47) is an important chaperone required for the correct folding and secretion of collagen. Several studies revealed that HSP47 has a role in numerous steps of collagen synthesis, preventing procollagen aggregation and inducing hydroxylation of proline and lysine residues. HSP47 is encoded by the SERPINH1 gene, which is located on chromosome 11q13.5, one of the most frequently amplified regions in human cancer. The altered expression levels of HSP47 have been correlated with several types of cancer, such as cervical, breast, pancreatic and gastric cancers. Studies have shown that HSP47 promotes tumor angiogenesis, growth, migration and metastatic capacity. In this review, we highlight the fundamental aspects of the interaction between HSP47 and collagen and the recent discoveries of the role of this chaperone in different types of malignant neoplasias. We also discuss recent treatments using HSP47 as a therapeutic target, and present evidences that HSP47 is an essential protein for cancer biology and a potential molecular target for chemotherapy.

Alcantara MB, Nemazannikova N, Elahy M, Dass CR (2014) Pigment epithelium-derived factor upregulates collagen I and downregulates matrix metalloproteinase 2 in osteosarcoma cells, and colocalises to collagen i and heat shock protein 47 in fetal and adult bone. J Pharm Pharmacol 66:1586–1592. https://doi.org/10.1111/jphp.12289 CrossRefPubMed

Araki K, Mikami T, Yoshida T et al (2009) High expression of HSP47 in ulcerative colitis-associated carcinomas: proteomic approach. Br J Cancer 101:492–497. https://doi.org/10.1038/sj.bjc.6605163 CrossRefPubMedPubMedCentral

Azuma M, Takeda Y, Nakajima H et al (2016) Biphasic function of TLR3 adjuvant on tumor and spleen dendritic cells promotes tumor T cell infiltration and regression in a vaccine therapy. Oncoimmunology 5:1–16. https://doi.org/10.1080/2162402X.2016.1188244 CrossRef

Blokzijl A, Ten Dijke P, Ibáez CF (2002) Physical and functional interaction between GATA-3 and SMAD3 allows TGF-β regulation of gata target genes. Curr Biol 12:35–45. https://doi.org/10.1016/S0960-9822(01)00623-6 CrossRefPubMed

Brandvold KR, Morimoto RI (2015) The chemical biology of molecular chaperones—implications for modulation of proteostasis. J Mol Biol 427:2931–2947. https://doi.org/10.1016/j.jmb.2015.05.010 CrossRefPubMedPubMedCentral

Cao D, Maitra A, Saavedra J-A et al (2005) Expression of novel markers of pancreatic ductal adenocarcinoma in pancreatic nonductal neoplasms: additional evidence of different genetic pathways. Mod Pathol 18:752–761. https://doi.org/10.1038/modpathol.3800363 CrossRefPubMed

Chen Y, Terajima M, Yang Y et al (2015) Lysyl hydroxylase 2 induces a collagen cross-link switch in tumor stroma. J Clin Invest 125:1147–1162. https://doi.org/10.1172/JCI74725 CrossRefPubMedPubMedCentral

Chou J, Lin JH, Brenot A et al (2013) GATA3 suppresses metastasis and modulates the tumour microenvironment by regulating microRNA-29b expression. Nat Cell Biol 15:201–213. https://doi.org/10.1038/ncb2672 CrossRefPubMedPubMedCentral

Clarke EP, Jain N, Brickenden A et al (1993) Parallel regulation of procollagen-I and colligin, a collagen- binding protein and a member of the serine protease inhibitor family. JCell Biol 121:193–199. https://doi.org/10.1083/jcb.121.1.193 CrossRef

Curran CS, Keely PJ (2013) Breast tumor and stromal cell responses to TGF-β and hypoxia in matrix deposition. Matrix Biol 32:95–105. https://doi.org/10.1016/j.matbio.2012.11.016 CrossRefPubMed

Daniels CE, Jett JR (2005) Does interstitial lung disease predispose to lung cancer? Curr Opin Pulm Med 11:431–437. https://doi.org/10.1097/01.mcp.0000170521.71497.ba CrossRefPubMed

Dufey E, Urra H, Hetz C (2015) ER proteostasis addiction in cancer biology: Novel concepts. Semin Cancer Biol 33:40–47. https://doi.org/10.1016/j.semcancer.2015.04.003 CrossRefPubMed

Duran I, Martin JH, Weis MA et al (2017) A chaperone complex formed by HSP47, FKBP65, and BiP modulates telopeptide lysyl hydroxylation of type I procollagen. J Bone Miner Res 32:1309–1319. https://doi.org/10.1002/jbmr.3095 CrossRefPubMedPubMedCentral

Ek ETH, Dass CR, Contreras KG, Choong PFM (2007a) Pigment epithelium-derived factor overexpression inhibits orthotopic osteosarcoma growth, angiogenesis and metastasis. Cancer Gene Ther 14:616–626. https://doi.org/10.1038/sj.cgt.7701044 CrossRefPubMed

Ek ETH, Dass CR, Contreras KG, Choong PFM (2007b) Inhibition of orthotopic osteosarcoma growth and metastasis by multitargeted antitumor activities of pigment epithelium-derived factor. Clin Exp Metastasis 24:93–106. https://doi.org/10.1007/s10585-007-9062-1 CrossRefPubMed

Ferlay J, Soerjomataram I, Dikshit R et al (2015) Cancer incidence and mortality worldwide: Sources, methods and major patterns in GLOBOCAN 2012. Int J Cancer 136:E359–E386. https://doi.org/10.1002/ijc.29210 CrossRef

Fitchett CW, Hoffman GC (1986) Obstructing malignant lesions of the Colon. Surg Clin North Am 66:807–820. https://doi.org/10.1016/S0039-6109(16)43992-7 CrossRefPubMed

Ford AC, Moayyedi P, Hanauer SB (2013) Ulcerative colitis. BMJ 346:1–9. https://doi.org/10.1136/bmj.f432 CrossRef

Gelosa P, Sevin G, Pignieri A et al (2011) Terutroban, a thromboxane/prostaglandin endoperoxide receptor antagonist, prevents hypertensive vascular hypertrophy and fibrosis. Am J Physiol Heart Circ Physiol 300:H762–H768. https://doi.org/10.1152/ajpheart.00880.2010 CrossRefPubMed

Hebert C, Norris K, Della Coletta R et al (1999) Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines. J Cell Biochem 73:248–258. https://doi.org/10.1002/(SICI)1097-4644(19990501)73:2%3C248::AID-JCB11%3E3.0.CO;2-A CrossRefPubMed

Hebert C, Coletta RD, Norris K et al (2001) Non-natural CBP2 binding peptides and peptomers modulate carcinoma cell adhesion and invasion. J Cell Biochem 82:145–154. https://doi.org/10.1002/jcb.1146 CrossRefPubMed

Helleman J, Jansen MPHM, Ruigrok-Ritstier K et al (2008) Association of an extracellular matrix gene cluster with breast cancer prognosis and endocrine therapy response. Clin Cancer Res 14:5555–5564. https://doi.org/10.1158/1078-0432.CCR-08-0555 CrossRefPubMed

Hirai K, Kikuchi S, Kurita A et al (2006) Immunohistochemical Distribution of Heat Shock Protein 47 (HSP47) in Scirrhous Carcinoma of the Stomach. Anticancer Res 26:71–78PubMed

Hirayoshi K, Kudo H, Takechi H et al (1991) HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts. Mol Cell Biol 11:4036–4044. https://doi.org/10.1128/mcb.11.8.4036 CrossRefPubMedPubMedCentral

Hosaka K, Yang Y, Seki T et al (2016) Pericyte–fibroblast transition promotes tumor growth and metastasis. Proc Natl Acad Sci 113:E5618–E5627. https://doi.org/10.1073/pnas.1608384113 CrossRefPubMed

Hosono J, Morikawa S, Ezaki T et al (2017) Pericytes promote abnormal tumor angiogenesis in a rat RG2 glioma model. Brain Tumor Pathol 34:120–129. https://doi.org/10.1007/s10014-017-0291-y CrossRefPubMed

Huntoon CJ, Nye MD, Geng L et al (2010) Heat Shock Protein 90 (HSP90) inhibition depletes LATS1 and LATS2, two regulators of the mammalian Hippo tumor suppressor pathway. Cancer Res 70:8642–8650. https://doi.org/10.1158/0008-5472.CAN-10-1345 CrossRefPubMedPubMedCentral

Ito S, Ogawa K, Takeuchi K et al (2017) A small-molecule compound inhibits a collagen-specific molecular chaperone and could represent a potential remedy for fibrosis. J Biol Chem 292:20076–20085. https://doi.org/10.1074/jbc.M117.815936 CrossRefPubMed

Jiang X, Zhou T, Wang Z et al (2016) HSP47 promotes glioblastoma stemlike cell survival by modulating tumor microenvironment extracellular matrix through TGF-β pathway. ACS Chem Neurosci 8:128–134. https://doi.org/10.1021/acschemneuro.6b00253 CrossRefPubMed

Kamikawaji K, Seki N, Watanabe M et al (2016) Regulation of LOXL2 and SERPINH1 by antitumor microRNA-29a in lung cancer with idiopathic pulmonary fibrosis. J Hum Genet 61:1–9. https://doi.org/10.1038/jhg.2016.99 CrossRef

Kimata Y, Kimata YI, Shimizu Y et al (2003) Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol Biol Cell 14:2559–2569. https://doi.org/10.1091/mbc.E02 CrossRefPubMedPubMedCentral

Kobayashi E, Satow R, Ono M et al (2014) MicroRNA expression and functional profiles of osteosarcoma. Oncol 86:94–103. https://doi.org/10.1159/000357408 CrossRef

Koide T, Takahara Y, Asada S, Nagata K (2002) Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47. J Biol Chem 277:6178–6182. https://doi.org/10.1074/jbc.M106497200 CrossRefPubMed

Kouros-Mehr H, Slorach EM, Sternlicht MD, Werb Z (2006) GATA-3 maintains the differentiation of the Luminal cell fate in the mammary gland. Cell 127:1041–1055. https://doi.org/10.1016/j.cell.2006.09.048 CrossRefPubMedPubMedCentral

Layman DL, Ross R (1973) The production and secretion of procollagen peptidase by human fibroblasts in culture. Arch Biochem Biophys 157:451–456. https://doi.org/10.1016/0003-9861(73)90661-9 CrossRefPubMed

Li Y, Wang F, Xu J et al (2011) Progressive miRNA expression profiles in cervical carcinogenesis and identification of HPV-related target genes for miR-29. J Pathol 224:484–495. https://doi.org/10.1002/path.2873 CrossRefPubMed

Lindert U, Weis MA, Rai J et al (2015) Molecular consequences of the SERPINH1/HSP47 mutation in the dachshund natural model of osteogenesis imperfecta. J Biol Chem 290:17679–17689. https://doi.org/10.1074/jbc.M115.661025 CrossRefPubMedPubMedCentral

Ma Y, Hendershot LM (2004) ER chaperone functions during normal and stress conditions. J Chem Neuroanat 28:51–65. https://doi.org/10.1016/j.jchemneu.2003.08.007 CrossRefPubMed

Maitra A, Iacobuzio-Donahue C, Rahman A et al (2002) Immunohistochemical validation of a novel epithelial and a novel stromal marker of pancreatic ductal adenocarcinoma identified by global expression microarrays: Sea urchin fascin homolog and heat shock protein 47. Am J Clin Pathol 118:52–59. https://doi.org/10.1309/3PAM-P5WL-2LV0-R4EG CrossRefPubMed

Maloney A, Clarke PA, Naaby-Hansen S et al (2007) Gene and protein expression profiling of human ovarian cancer cells treated with the Heat Shock Protein 90 inhibitor 17-Allylamino-17-Demethoxygeldanamycin. Cancer Res 67:3239–3253. https://doi.org/10.1158/0008-5472.can-06-2968 CrossRefPubMed

Miyata S, Mizuno T, Koyama Y et al (2013) The endoplasmic reticulum-resident chaperone Heat Shock Protein 47 protects the Golgi apparatus from the effects of O-Glycosylation inhibition. PLoS One 8:1–20. https://doi.org/10.1371/journal.pone.0069732 CrossRef

Mori K, Toiyama Y, Otake K et al (2017) Proteomics analysis of differential protein expression identifies heat shock protein 47 as a predictive marker for lymph node metastasis in patients with colorectal cancer. Int J Cancer 140:1425–1435. https://doi.org/10.1002/ijc.30557 CrossRefPubMed

Nagata K, Yamada KM (1986) Phosphorylation and transformation sensitivity of a major collagen-binding protein of fibroblasts. J Biol Chem 261:7531–7536PubMed

Nagata K, Saga S, Yamada KM (1986) A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein. J Cell Biol 103:223–229. https://doi.org/10.1083/jcb.103.1.223 CrossRefPubMed

Nakai A, Satoh M, Hirayoshi K, Nagata K (1992) Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum. J Cell Biol 117:903–914. https://doi.org/10.1083/jcb.117.4.903 CrossRefPubMed

Nakayama S, Mukae H, Sakamoto N et al (2008) Pirfenidone inhibits the expression of HSP47 in TGF-β1-stimulated human lung fibroblasts. Life Sci 82:210–217. https://doi.org/10.1016/j.lfs.2007.11.003 CrossRefPubMed

Nan A, Ghandehari H, Hebert C et al (2005) Water-soluble polymers for targeted drug delivery to human squamous carcinoma of head and neck. J Drug Target 13:189–197. https://doi.org/10.1080/10611860500065187 CrossRefPubMed

Natsume T, Koide T, Yokota S et al (1994) Interactions between collagen-binding stress protein HSP47 and collagen: Analysis of kinetic parameters by surface plasmon resonance biosensor. J Biol Chem 269:31224–31228PubMed

Nishida N, Yano H, Nishida T et al (2006) Angiogenesis in cancer. Vasc Health Risk Manag 2:213–219. https://doi.org/10.2147/vhrm.2006.2.3.213 CrossRefPubMedPubMedCentral

Polydorou C, Mpekris F, Papageorgis P et al (2017) Pirfenidone normalizes the tumor microenvironment to improve chemotherapy. Oncotarget 8:24506–24517. https://doi.org/10.18632/oncotarget.15534 CrossRefPubMedPubMedCentral

Poschmann G, Sitek B, Sipos B et al (2009) Identification of proteomic differences between squamous cell carcinoma of the lung and bronchial epithelium. Mol Cell Proteomics 8:1105–1116. https://doi.org/10.1074/mcp.M800422-MCP200 CrossRefPubMedPubMedCentral

Sasaki K, Yoshida H (2015) Organelle autoregulation—stress responses in the ER, Golgi, mitochondria and lysosome. J Biochem 157:185–195. https://doi.org/10.1093/jb/mvv010 CrossRefPubMed

Sato Y (2003) Molecular diagnosis of tumor angiogenesis and anti-angiogenic cancer therapy. Int J Clin Oncol 8:200–206. https://doi.org/10.1007/s10147-003-0342-8 CrossRefPubMed

Sauk JJ, Norris K, Hebert C et al (1998) Hsp47 binds to the KDEL receptor and cell surface expression is modulated by cytoplasmic and endosomal pH. Connect Tissue Res 37:105–119. https://doi.org/10.3109/03008209809028904 CrossRefPubMed

Sauk JJ, Coletta RD, Norris K, Hebert C (2000) Binding motifs of CBP2 a potential cell surface target for carcinoma cells. J Cell Biochem 78(20000801):251–263. https://doi.org/10.1002/(SICI)1097-4644(20000801)78:2%3C251::AID-JCB8%3E3.0.CO;2-G CrossRefPubMed

Schedin P, Keely PJ (2011) Mammary gland ECM remodeling, stiffness, and mechanosignaling in normal development and tumor progression. Cold Spring Harb Perspect Biol 3:1–22. https://doi.org/10.1101/cshperspect.a003228 CrossRef

Schwab M (1998) Amplification of oncogenes in human cancer cells. BioEssays 20:473–479. https://doi.org/10.1002/(SICI)1521-1878(199806)20:6%3C473::AID-BIES5%3E3.0.CO;2-N CrossRefPubMed

Sepulveda D, Rojas-Rivera D, Rodríguez DA et al (2018) Interactome screening identifies the ER luminal chaperone Hsp47 as a regulator of the unfolded protein response transducer IRE1α. Mol Cell 69:238–252. https://doi.org/10.1016/j.molcel.2017.12.028 CrossRefPubMed

Sharbeen G, McAlpine S, Phillips P (2015) HSP47: the new heat shock protein therapeutic target. In: McAlpine S, A. E (eds) Heat shock protein inhibitors, vol 19. Springer, Cham

Siller-Matula JM, Krumphuber J, Jilma B (2010) Pharmacokinetic, pharmacodynamic and clinical profile of novel antiplatelet drugs targeting vascular diseases: REVIEW. Br J Pharmacol 159:502–517. https://doi.org/10.1111/j.1476-5381.2009.00555.x CrossRefPubMed

Suekane S, Ueda K, Nishihara K et al (2017) Personalized peptide vaccination as second-line treatment for metastatic upper tract urothelial carcinoma. Cancer Sci 108:2430–2437. https://doi.org/10.1111/cas.13404 CrossRefPubMedPubMedCentral

Takechi H, Hirayoshi K, Nakai A et al (1992) Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells. Eur J Biochem 206:323–329. https://doi.org/10.1111/j.1432-1033.1992.tb16930.x CrossRefPubMed

Tavassoli F, Deville P (eds) (2003) Pathology and genetics of tumours of the breast and female genital organs, 5th edn. IARC Press, Lyon

Thomson CA, Ananthanarayanan VS (2000) Structure–function studies on Hsp47: pH-dependent inhibition of collagen fibril formation in vitro. Biochem J 349:877–883. https://doi.org/10.1042/bj3490877 CrossRefPubMedPubMedCentral

Thomson CA, Atkinson HM, Ananthanarayanan VS (2005) Identification of small molecule chemical inhibitors of the collagen-specific chaperone Hsp47. J Med Chem 48:1680–1684. https://doi.org/10.1021/jm049148&%23x002B; CrossRefPubMed

Uozaki H, Ishida T, Kakiuchi C et al (2000) Expression of heat shock proteins in osteosarcoma and its relationship to prognosis. Pathol Res Pract 196:665–673. https://doi.org/10.1016/S0344-0338(00)80118-1 CrossRefPubMed

Verma V, Kim Y, Lee M-C et al (2016) Activated dendritic cells delivered in tissue compatible biomatrices induce in-situ anti-tumor CTL responses leading to tumor regression. Oncotarget 7:39894–39906. https://doi.org/10.18632/oncotarget.9529 CrossRefPubMedPubMedCentral

Walker LC, Overstreet MA, Yeowell HN (2005) Tissue-specific expression and regulation of the alternatively-spliced forms of lysyl hydroxylase 2 (LH2) in human kidney cells and skin fibroblasts. Matrix Biol 23:515–523. https://doi.org/10.1016/j.matbio.2004.11.002 CrossRefPubMed

Walter P, Ron D (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334:1081–1086. https://doi.org/10.1126/science.1209038 CrossRefPubMed

Wang SY (1994) A retinoic acid-inducible GATA-binding protein binds to the regulatory region of J6 serpin gene. J Biol Chem 269:607–613PubMed

Wang M, Kaufman RJ (2016) Protein misfolding in the endoplasmic reticulum as a conduit to human disease. Nature 529:326–335. https://doi.org/10.1038/nature17041 CrossRefPubMed

Wilson R, Lees JF, Bulleid NJ (1998) Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen. J Biol Chem 273:9637–9643. https://doi.org/10.1074/jbc.273.16.9637 CrossRefPubMed

Wu ZB, Cai L, Qiu C et al (2014) CTL responses to HSP47 associated with the prolonged survival of patients with glioblastomas. Neurology 82:1261–1265. https://doi.org/10.1212/WNL.0000000000000290 CrossRefPubMed

Wu ZB, Cai L, Lin SJ et al (2016) Heat shock protein 47 promotes glioma angiogenesis. Brain Pathol 26:31–42. https://doi.org/10.1111/bpa.12256 CrossRefPubMed

Wu Q, Pi L, Le Trinh T et al (2017) A novel vaccine targeting Glypican-3 as a treatment for Hepatocellular carcinoma. Mol Ther 25:2299–2308. https://doi.org/10.1016/j.ymthe.2017.08.005 CrossRefPubMedPubMedCentral

Xiang Q, Yang Y, Zhou Z et al (2012) Synthesis and in vitro anti-tumor activity of novel HPMA copolymer-drug conjugates with potential cell surface targeting property for carcinoma cells. Eur J Pharm Biopharm 80:379–386. https://doi.org/10.1016/j.ejpb.2011.10.020 CrossRefPubMed

Xu R, Mao J-H (2011) Gene transcriptional networks integrate microenvironmental signals in human breast cancer. Integr Biol 3:368–374. https://doi.org/10.1039/c0ib00087f CrossRef

Xu CJ, Mikami T, Nakamura T et al (2013) Tumor budding, myofibroblast proliferation, and fibrosis in obstructing colon carcinoma: the roles of Hsp47 and basic fibroblast growth factor. Pathol Res Pract 209:69–74. https://doi.org/10.1016/j.prp.2012.10.008 CrossRefPubMed

Yamamoto N, Kinoshita T, Nohata N et al (2013) Tumor-suppressive microRNA-29a inhibits cancer cell migration and invasion via targeting HSP47 in cervical squamous cell carcinoma. Int J Oncol 43:1855–1863. https://doi.org/10.3892/ijo.2013.2145 CrossRefPubMedPubMedCentral

Yamauchi M, Noyes C, Kuboki Y, Mechanic GL (1982) Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type I collagen. Proc Natl Acad Sci USA 79:7684–7688. https://doi.org/10.1073/pnas.79.24.7684 CrossRefPubMed

Zhang X, Yang J-J, Kim YS et al (2010) An 8-gene signature, including methylated and down-regulated glutathione peroxidase 3, of gastric cancer. Int J Oncol 36:405–414. https://doi.org/10.3892/ijo_00000513 CrossRefPubMed

Zhao D, Jiang X, Yao C et al (2014) Heat shock protein 47 regulated by miR-29a to enhance glioma tumor growth and invasion. J Neurooncol 118:39–47. https://doi.org/10.1007/s11060-014-1412-7 CrossRefPubMed

Zhao Y, Dang Z, Xu S, Chong S (2017) Heat shock protein 47 effects on hepatic stellate cell-associated receptors in hepatic fibrosis of Schistosoma japonicum-infected mice. Biol Chem 398:1357–1366. https://doi.org/10.1515/hsz-2017-0177 CrossRefPubMed

Zhu J, Xiong G, Fu H et al (2015) Chaperone Hsp47 drives malignant growth and invasion by modulating an ECM gene network. Cancer Res 75:1580–1591. https://doi.org/10.1158/0008-5472.CAN-14-1027 CrossRefPubMedPubMedCentral

Title: The heat shock protein 47 as a potential biomarker and a therapeutic agent in cancer research
Authors: Beatriz Dal Pont Duarte
Diego Bonatto
Publication date: 01-12-2018
Publisher: Springer Berlin Heidelberg
Published in: Journal of Cancer Research and Clinical Oncology / Issue 12/2018
Print ISSN: 0171-5216
Electronic ISSN: 1432-1335
DOI: https://doi.org/10.1007/s00432-018-2739-9

ACC 2024 Congress Coverage

Heart Failure Video

Keynote webinar | Spotlight on sleep in brain health

Springer Medicine

The heat shock protein 47 as a potential biomarker and a therapeutic agent in cancer research

Abstract

ACC 2024 Congress Coverage

Year in Review: Heart failure and cardiomyopathies

Semaglutide benefits people with type 2 diabetes and obesity-related heart failure

Incentivised to exercise

New intervention for STEMI-related cardiogenic shock

» View more highlights on the ACC 2024 congress hub page

Keynote webinar | Spotlight on sleep in brain health

Springer Medicine

Abstract

Please log in to get access to this content

Other articles of this Issue 12/2018

Signaling network involved in the GPC3-induced inhibition of breast cancer progression: role of canonical Wnt pathway

Analysis of unexpected small cell lung cancer following surgery as the primary treatment

Kaposiform hemangioendothelioma without cutaneous involvement

Impact of carboplatin hypersensitivity and desensitization on patients with recurrent ovarian cancer

Progress in gene therapy using oncolytic vaccinia virus as vectors

The concept of the okadaic acid class of tumor promoters is revived in endogenous protein inhibitors of protein phosphatase 2A, SET and CIP2A, in human cancers

ACC 2024 Congress Coverage

Year in Review: Heart failure and cardiomyopathies

Semaglutide benefits people with type 2 diabetes and obesity-related heart failure

Incentivised to exercise

New intervention for STEMI-related cardiogenic shock

» View more highlights on the ACC 2024 congress hub page