Health Dictionary
Reliable, easy-to-read patient information on common medical conditions ā written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
SDPR
Introduction
Cavin-2 or Serum deprivation-response protein (SDPR) is a protein that in humans is encoded by the SDPR gene.[1][2][3] Cavin-2 is highly expressed in a variety of human endothelial cells.[4]
This gene encodes a calcium-independent phospholipid-binding protein whose expression increases in serum-starved cells. This protein has also been shown to be a substrate for protein kinase C (PKC) phosphorylation.[3]
Function
Function
Cavin-2 is required for blood vessel formation (angiogenesis) in humans and zebrafish and required also for the endothelial cell proliferation, migration and invasion in humans.[4] Cavin-2 plays an important role in endothelial cell maintenance by regulating eNOS activity.[4] Cavin-2 controls the generation of nitric oxide (NO) in human endothelial cells by controlling the activity and stability of the protein endothelial nitric-oxide synthase (eNOS).[4]
Secretion
Secretion
Cavin-2 is highly secreted from human endothelial cells (HUVEC), they are secreted through endothelial microparticles (EMPs) but not exosomes and is required for EMP biogenesis.[4]
Clinical significance
Clinical significance
SDPR is shown to act as a metastasis suppressor by xenograft studies utilizing breast cancer cell lines.[5] SDPR may elicit its metastasis suppressor function by directly interacting with ERK and limiting its pro-survival role.[5] Moreover, it is suggested that SDPR is silenced during breast cancer progression by promoter DNA methylation.[5] Metastasis suppressor role of SDPR may go beyond breast cancer since tumor samples from bladder, colorectal, lung, pancreatic, and ovarian cancers as well as sarcomas also exhibited loss of SDPR expression.[5]
References
References
- ā Gustincich S, Vatta P, Goruppi S, Wolf M, Saccone S, Della Valle G, Baggiolini M, Schneider C (Jun 1999). “The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein”. Genomics. 57 (1): 120ā9. doi:10.1006/geno.1998.5733. PMIDĀ 10191091.
- ā Gustincich S, Schneider C (Dec 1993). “Serum deprivation response gene is induced by serum starvation but not by contact inhibition”. Cell Growth Differ. 4 (9): 753ā60. PMIDĀ 8241023.
- ā 3.0 3.1 “Entrez Gene: SDPR serum deprivation response (phosphatidylserine binding protein)”.
- ā 4.0 4.1 4.2 4.3 4.4 Boopathy GT, Kulkarni M, Ho SY, Boey A, Chua EW, Barathi VA, Carney TJ, Wang X, Hong W (2017). “Cavin-2 regulates the activity and stability of endothelial nitric oxide synthase (eNOS) in angiogenesis”. The Journal of Biological Chemistry. 292: 17760ā17776. doi:10.1074/jbc.M117.794743. PMCĀ 5663877. PMIDĀ 28912276.
- ā 5.0 5.1 5.2 5.3 Sait Ozturk; Panagiotis Papageorgis; Chen Khuan Wong; Arthur W. Lambert; Hamid M. Abdolmaleky; Arunthathi Thiagalingam; Herbert T. Cohen & Sam Thiagalingam (Jan 2016). “SDPR functions as a metastasis suppressor in breast cancer by promoting apoptosis”. PNAS. 113: 638ā643. doi:10.1073/pnas.1514663113. PMCĀ 4725521. PMIDĀ 26739564.
Further reading
Further reading
- Burgener R, Wolf M, Ganz T, Baggiolini M (1990). “Purification and characterization of a major phosphatidylserine-binding phosphoprotein from human platelets”. Biochem. J. 269 (3): 729ā34. PMCĀ 1131648. PMIDĀ 2390065.
- Cross SH, Charlton JA, Nan X, Bird AP (1994). “Purification of CpG islands using a methylated DNA binding column”. Nat. Genet. 6 (3): 236ā44. doi:10.1038/ng0394-236. PMIDĀ 8012384.
- Mineo C, Ying YS, Chapline C, et al. (1998). “Targeting of Protein Kinase CĪ± to Caveolae”. J. Cell Biol. 141 (3): 601ā10. doi:10.1083/jcb.141.3.601. PMCĀ 2132740. PMIDĀ 9566962.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899ā903. doi:10.1073/pnas.242603899. PMCĀ 139241. PMIDĀ 12477932.
- Gevaert K, Goethals M, Martens L, et al. (2004). “Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides”. Nat. Biotechnol. 21 (5): 566ā9. doi:10.1038/nbt810. PMIDĀ 12665801.
- Brandenberger R, Wei H, Zhang S, et al. (2005). “Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation”. Nat. Biotechnol. 22 (6): 707ā16. doi:10.1038/nbt971. PMIDĀ 15146197.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121ā7. doi:10.1101/gr.2596504. PMCĀ 528928. PMIDĀ 15489334.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). “Generation and annotation of the DNA sequences of human chromosomes 2 and 4”. Nature. 434 (7034): 724ā31. doi:10.1038/nature03466. PMIDĀ 15815621.
- Rual JF, Venkatesan K, Hao T, et al. (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173ā8. doi:10.1038/nature04209. PMIDĀ 16189514.