| Cystatin C (amyloid angiopathy and cerebral hemorrhage)
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| PDB rendering based on 1g96.
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| Available structures: 1g96, 1r4c, 1tij
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| Identifiers
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| Symbol(s)
| CST3; MGC117328
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| External IDs
| OMIM: 604312 MGI: 102519 Homologene: 78
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| Gene Ontology
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| Molecular Function:
| • cysteine protease inhibitor activity
• protein homodimerization activity
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| RNA expression pattern
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Additional recommended knowledge
More reference expression data
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| Orthologs
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| Human
| Mouse
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| Entrez
| 1471
| 13010
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| Ensembl
| ENSG00000101439
| ENSMUSG00000027447
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| Uniprot
| P01034
| Q3U5K7
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| Refseq
| NM_000099 (mRNA)
NP_000090 (protein)
| NM_009976 (mRNA)
NP_034106 (protein)
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| Location
| Chr 20: 23.56 - 23.57 Mb
| Chr 2: 148.56 - 148.57 Mb
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| Pubmed search
| [1]
| [2]
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Cystatin 3, usually called Cystatin C (also CST3 and Gamma trace) is a serum protein used mainly as a measure of glomerular filtration rate. It is a single 120-residue polypeptide belonging to the type 2 cystatin gene family. Studies have shown that Cystatin C allows a more precise testing of kidney function than creatinine.
The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes the most abundant extracellular inhibitor of cysteine proteases, which is found in high concentrations in biological fluids and is expressed in virtually all organs of the body. A mutation in this gene has been associated with amyloid angiopathy. Expression of this protein in vascular wall smooth muscle cells is severely reduced in both atherosclerotic and aneurysmal aortic lesions, establishing its role in vascular disease.[1]
Mutations in the cystatin 3 gene are responsible for the Icelandic type of hereditary cerebral amyloid angiopathy, a condition predisposing to intracerebral haemorrhage.
References
- ^ Entrez Gene: CST3 cystatin C (amyloid angiopathy and cerebral hemorrhage).
Further reading
- Jensson O, Palsdottir A, Thorsteinsson L, Arnason A (1990). "The saga of cystatin C gene mutation causing amyloid angiopathy and brain hemorrhage--clinical genetics in Iceland.". Clin. Genet. 36 (5): 368-77. PMID 2689007.
- Mussap M, Plebani M (2005). "Biochemistry and clinical role of human cystatin C.". Critical reviews in clinical laboratory sciences 41 (5-6): 467-550. PMID 15603510.
- Palsdottir A, Snorradottir AO, Thorsteinsson L (2006). "Hereditary cystatin C amyloid angiopathy: genetic, clinical, and pathological aspects.". Brain Pathol. 16 (1): 55-9. PMID 16612982.
- Levy E, Jaskolski M, Grubb A (2006). "The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models.". Brain Pathol. 16 (1): 60-70. PMID 16612983.
- Bökenkamp A, Herget-Rosenthal S, Bökenkamp R (2006). "Cystatin C, kidney function and cardiovascular disease.". Pediatr. Nephrol. 21 (9): 1223-30. doi:10.1007/s00467-006-0192-5. PMID 16838182.
- Abrahamson M, Jonsdottir S, Olafsson I, et al. (1992). "Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis.". Hum. Genet. 89 (4): 377-80. PMID 1352269.
- Lindahl P, Abrahamson M, Björk I (1992). "Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin.". Biochem. J. 281 ( Pt 1): 49-55. PMID 1731767.
- Abrahamson M, Mason RW, Hansson H, et al. (1991). "Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase.". Biochem. J. 273 ( Pt 3): 621-6. PMID 1996959.
- Lenarcic B, Krasovec M, Ritonja A, et al. (1991). "Inactivation of human cystatin C and kininogen by human cathepsin D.". FEBS Lett. 280 (2): 211-5. PMID 2013314.
- Ghiso J, Saball E, Leoni J, et al. (1990). "Binding of cystatin C to C4: the importance of sense-antisense peptides in their interaction.". Proc. Natl. Acad. Sci. U.S.A. 87 (4): 1288-91. PMID 2304899.
- Abrahamson M, Olafsson I, Palsdottir A, et al. (1990). "Structure and expression of the human cystatin C gene.". Biochem. J. 268 (2): 287-94. PMID 2363674.
- Levy E, Lopez-Otin C, Ghiso J, et al. (1989). "Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases.". J. Exp. Med. 169 (5): 1771-8. PMID 2541223.
- Abrahamson M, Islam MQ, Szpirer J, et al. (1989). "The human cystatin C gene (CST3), mutated in hereditary cystatin C amyloid angiopathy, is located on chromosome 20.". Hum. Genet. 82 (3): 223-6. PMID 2567273.
- Saitoh E, Sabatini LM, Eddy RL, et al. (1989). "The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20.". Biochem. Biophys. Res. Commun. 162 (3): 1324-31. PMID 2764935.
- Palsdottir A, Abrahamson M, Thorsteinsson L, et al. (1988). "Mutation in cystatin C gene causes hereditary brain haemorrhage.". Lancet 2 (8611): 603-4. PMID 2900981.
- Abrahamson M, Grubb A, Olafsson I, Lundwall A (1987). "Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C.". FEBS Lett. 216 (2): 229-33. PMID 3495457.
- Ghiso J, Jensson O, Frangione B (1986). "Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of gamma-trace basic protein (cystatin C).". Proc. Natl. Acad. Sci. U.S.A. 83 (9): 2974-8. PMID 3517880.
- Grubb A, Löfberg H (1982). "Human gamma-trace, a basic microprotein: amino acid sequence and presence in the adenohypophysis.". Proc. Natl. Acad. Sci. U.S.A. 79 (9): 3024-7. PMID 6283552.
- Brzin J, Popovic T, Turk V, et al. (1984). "Human cystatin, a new protein inhibitor of cysteine proteinases.". Biochem. Biophys. Res. Commun. 118 (1): 103-9. PMID 6365094.
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