HyperferritinemiaHyFerrNCT05659017
Candidate Gene for Hyperferritinemia
An observational study of Hyperferritinemia, run by University of Milano Bicocca at 1 site in Italy.
Trial summary
Ferritin is a ubiquitous protein capable of storing iron in the cell cytosol. Stored iron is released and made available for cellular needs by the degradation of ferritin itself. Read more about this study
- Who is it for?
- Ages 18 to 80 years
- Conditions the study is for
- Hyperferritinemia
- What is being tested?
- Genetic analysis
- How many people
- 100 participants
- Where
- 1 siteItaly
- Study dates
- 6 Jun 2022to 30 Sep 2024
- Phase
- Observational
- Are there results?
- None posted in the registry
Key requirements
Who can take part, as listed by the sponsor. Only the study team can confirm whether you are eligible, so take this list to your doctor.
- Ages 18 to 80 years
- All sexes
- No healthy volunteers
- Adult, Older adult
Study population: Hyperferritinemia patients followed at the Rare Diseases Center in San Gerardo Hospital
Who may be able to join
- Among patients referred to the Center for Rare Diseases of Monza will be enrolled only subjects with:
- ferritin > 1000 g / L in men and > 500 g / L,
- transferrin saturation <45%
- absence of hepatic iron overload, evaluated by liver biopsy or MRI, as indicated in the attached flow chart.
Who cannot join
- Patients with hyperferritinemia attributable to:
- genetically determined causes [mutations in the HFE gene (homozygosity or heterozygosity for p.Cys282Tyr, homozygosity for p.His63Asp or compound heterozygosity for variants of p.Cys282Tyr and p. His63Asp), ferroportin and L-Ferritin gene mutations];
- presence of more than one component of metabolic syndrome (according to NCEP-ATPIII criteria: triglycerides >150 mg/dL, blood glucose >100 mg/dL, HDL <40 mg/dL in men and <50 mg/dL in women, waist circumference >102 cm in men and >88 cm in women; blood pressure ≥130/≥85 mm/Hg);
- alcohol intake >5 g/day chronic hepatitis,
- history of blood transfusion or parenteral iron treatment,
- late skin porphyria,
Show all 9Show fewer
- hyperthyroidism,
- presence of cataracts or family history of early-onset cataracts
- acute or chronic inflammatory disorders.
Trial locations and contacts
1 site in 1 country.
Italy1 site, 1 recruiting
- Recruiting
Centre for Rare Disease - Disorders of Iron Metabolism, ASST-Monza, San Gerardo Hospital, European Reference Network - EuroBloodNet
Monza, MB, 20900
Raffaella Mariani, Dr.ssa, +390392339555, r.mariani@asst-monza.it
About this study
Official title: Study to Identify a Genetic Defect in Subjects With Hyperferritinemia.
Ferritin is a ubiquitous protein capable of storing iron in the cell cytosol. Stored iron is released and made available for cellular needs by the degradation of ferritin itself. Small amounts of ferritin are present in the blood and consist of ferritin L, a glycosylated form of L called ferritin G, and trace amounts of ferritin H. It is secreted mainly by macrophages, hepatocytes, and lymphoid cells, but most aspects of its secretion remain not fully elucidated. Serum ferritin has broad clinical utility primarily as an indicator of iron stores, so low values of serum ferritin are indicative of a deficient state and high values of iron overload. However, the causes of increased serum ferritin are numerous, in many cases serum ferritin is increased disproportionately to iron stores such as in acute and chronic liver disease, infectious and inflammatory states, metabolic disorders, and high alcohol intake that are frequently observed in the clinical setting. Therefore, the diagnosis of hyperferritinemia requires a careful strategy including personal and family history, biochemical, instrumental, and targeted genetic testing. In fact, there are rare forms of genetically determined hyperferritinemia not associated with iron overload, such as hereditary cataract hyperferritinemia syndrome (HHCS) due to mutations in the Iron responsive Element (IRE) located in the 5' untranslated region of the FTL gene. More recently, a second dominant form of genetic hyperferritinemia without iron overload or cataract (benign hyperferritinemia) has been identified.
Preliminary results obtained so far have made it possible, through WES analysis, to identify the involvement of the STAB1 gene, which was found to be mutated in the studied subjects in whom reduced serum ferritin glycosylation and reduced plasma concentration of the protein itself were observed. It is therefore deemed necessary to proceed with the assay of glycosylated ferritin and the protein encoded by the gene to assess its sensitivity and specificity as a predictive test before performing the genetic analysis of STAB1. To achieve this goal, patients with undefined hyperferritinemia afferent to the SSD Rare Diseases of the IRCCS San Gerardo Foundation in whom to perform glycosylated ferritin and STAB1 protein assay in parallel with STAB1 sequencing will be evaluated. Similar investigations will be performed in a control group consisting of cases of hyperferritinemia due to genetically determined iron overload.
Read the detailed description
Ferritin is a ubiquitous protein capable of storing iron in the cell cytosol. Cytosolic ferritin consists of two subunits, the light chain (L-ferritin) and the heavy chain (H-ferritin) that assemble in different proportions to form apo-ferritin shells. Ferritin nanoshells consist of 24 subunits of the L- and H-chains that create a cavity in which intracellular iron is collected. The stored iron is released and made available for cellular needs by the degradation of ferritin. Ferritin can bind, oxidize, and store up to 4500 Fe(II) atoms, preventing iron-mediated oxidative stress. This is achieved by regulating ferritin synthesis according to cellular iron content and oxidative stress at both the post-transcriptional (via the Iron Responsive Element (IRE)-regulatory protein (IRP) system) and transcriptional levels. Small amounts of ferritin are present in the blood and consist of ferritin L, a glycosylated form of L called ferritin G, and traces of ferritin H. It is secreted primarily by macrophages, hepatocytes, and lymphoid cells, but most aspects of its secretion remain unknown. Serum ferritin has broad clinical utility primarily as an indicator of intracellular iron stores.
The causes of increased serum ferritin are numerous, including primary and secondary iron overload disorders, but also conditions in which serum ferritin is increased disproportionately to the body's iron stores such as chronic liver disease, inflammatory and metabolic disorders that are frequently observed in the clinical setting. Therefore, the diagnosis of hyperferritinemia requires a systematic strategy including personal and family history, biochemical and instrumental tests. In addition, alterations in the regulation of ferritin synthesis due to mutations in the iron-sensitive element L-ferritin (IRE) cause hereditary hyperferritinemia cataract syndrome (HHCS), an inherited disease characterized by elevated serum ferritin without iron overload and early onset of bilateral cataracts. Recently, a second dominant form of genetic hyperferritinemia without iron overload or cataract has been reported. Amino acid substitutions at positions 26, 27, and 30 in the heterozygous state in the L-ferritin A helix have been found in these patients. The resulting ferritin appears unusually susceptible to glycosylation, leading to serum glycosylated ferritin values consistently >90%. The reason for the development of hyperferritinemia and hyperglycosylation associated with these mutant forms of ferritin has not been established. It is probably related to increased secretion, but may also contribute to delayed clearance. Some cases of hyperferritinemia still remain unexplained, and the currently unknown candidate gene that we think we have identified among candidate genes needs to be validated in a larger population of subjects with the listed characteristics.
The primary objective of the study is to sequence the candidate gene that emerged from previous studies as mutated in patients with the same clinical features.
The secondary objective is to include the candidate gene in the routine genetic diagnosis of subjects with hyperferritinemia without tissue iron overload.
The study will last about 12 months the time needed for the recovery of patients with a genetic diagnosis not yet defined, analysis of medical records and research of the DNA sample stored at the Laboratory of Cytogenetics and Medical Genetics of San Gerardo Hospital and genetic analysis by Next Generation Sequencing. The study, although simple in its idea, requires a very careful organization of access and monitoring of selected patients that require the presence of a study manager dedicated to the project.
The study extension includes:glycosylated ferritin assay in patients with hyperferritinemia referred to the Rare Disease Center of IRCCS Foundation - San Gerardo dei Tintori selected according to the inclusion and exclusion criteria; soluble protein assay encoded by the STAB1 gene in patients in point A and patients in group D.
- Conditions
- Hyperferritinemia
- Being tested
- Genetic analysis
- Medical subject headings
- Hyperferritinemia
What participants receive
What participants receive. In a randomised study each person is assigned to one group by chance.
Genetic analysisGenetic
The DNA will then be analyzed with a custom panel designed ad hoc to study the candidate gene by Next Generation Sequencing according to the protocols of the supplier of the kit.
What is being measured
The primary outcome is the main question the study is designed to answer.
Candidate gene sequencing
For the purpose 100 patients are sufficient to calculate both the allelic and genotypic frequency of mutations in the candidate gene.
Measured: 1 year
Secondary outcomes (1)
DIAGNOSIS ROUTINE
The secondary objective is to include the candidate gene in the routine genetic diagnosis of individuals with hyperferritinemia without tissue iron overload.
Measured: 1 year
Timeline
From the start of the study to its completion; the mark is today. Estimated dates are the sponsor’s plan.
- First posted21 Dec 2022
- Study start6 Jun 2022
- Primary completion3 Jan 2024
- Study completion30 Sep 2024 (estimated)
Resources
- Official record on ClinicalTrials.govThe registry entry this page is built from, with its full change history.
- Publications (23)Papers the sponsor has linked to this study.
- Other trials for HyperferritinemiaStudies of the same condition, open and under way.
- What the trial phases meanHow a treatment moves from first tests in people to approval.
More details
For doctors and researchers: how the study is designed, who runs it, and its registry IDs.
Study design
- Study type
- Observational
- Observational model
- Cohort
- Time perspective
- Retrospective
- Enrolment
- 100 participants (estimated)
Sponsor and investigators
- Lead sponsor
- University of Milano Bicocca
- Sponsor type
- University, hospital or other
- Responsible party
- Principal investigator, Sara Pelucchi, University of Milano Bicocca
IDs, dates and publications
- ClinicalTrials.gov ID
- NCT05659017
- Sponsor's protocol ID
- HyFerr
- Acronym
- HyFerr
- Status last verified
- Jan 2024
- First submitted
- 12 Dec 2022
- Last updated
- 5 Jan 2024
- Results posted
- No
- Data monitoring committee
- No
- FDA-regulated drug
- No
- FDA-regulated device
- No
- Individual data sharing
- No
Publications
Arosio P, Levi S. Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage. Biochim Biophys Acta. 2010 Aug;1800(8):783-92. doi: 10.1016/j.bbagen.2010.02.005. Epub 2010 Feb 20.
PubMed 20176086Torti FM, Torti SV. Regulation of ferritin genes and protein. Blood. 2002 May 15;99(10):3505-16. doi: 10.1182/blood.v99.10.3505. No abstract available.
PubMed 11986201Finazzi D, Arosio P. Biology of ferritin in mammals: an update on iron storage, oxidative damage and neurodegeneration. Arch Toxicol. 2014 Oct;88(10):1787-802. doi: 10.1007/s00204-014-1329-0. Epub 2014 Aug 15.
PubMed 25119494Wang J, Pantopoulos K. Regulation of cellular iron metabolism. Biochem J. 2011 Mar 15;434(3):365-81. doi: 10.1042/BJ20101825.
PubMed 21348856Cragg SJ, Wagstaff M, Worwood M. Sialic acid and the microheterogeneity of human serum ferritin. Clin Sci (Lond). 1980 Mar;58(3):259-62. doi: 10.1042/cs0580259.
PubMed 7363568Santambrogio P, Cozzi A, Levi S, Arosio P. Human serum ferritin G-peptide is recognized by anti-L ferritin subunit antibodies and concanavalin-A. Br J Haematol. 1987 Feb;65(2):235-7. doi: 10.1111/j.1365-2141.1987.tb02271.x.
PubMed 3828232Cohen LA, Gutierrez L, Weiss A, Leichtmann-Bardoogo Y, Zhang DL, Crooks DR, Sougrat R, Morgenstern A, Galy B, Hentze MW, Lazaro FJ, Rouault TA, Meyron-Holtz EG. Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway. Blood. 2010 Sep 2;116(9):1574-84. doi: 10.1182/blood-2009-11-253815. Epub 2010 May 14.
PubMed 20472835Mack U, Cooksley WG, Ferris RA, Powell LW, Halliday JW. Regulation of plasma ferritin by the isolated perfused rat liver. Br J Haematol. 1981 Mar;47(3):403-12. doi: 10.1111/j.1365-2141.1981.tb02808.x.
PubMed 7459278Tran TN, Eubanks SK, Schaffer KJ, Zhou CY, Linder MC. Secretion of ferritin by rat hepatoma cells and its regulation by inflammatory cytokines and iron. Blood. 1997 Dec 15;90(12):4979-86.
PubMed 9389717Dorner MH, Silverstone A, Nishiya K, de Sostoa A, Munn G, de Sousa M. Ferritin synthesis by human T lymphocytes. Science. 1980 Aug 29;209(4460):1019-21. doi: 10.1126/science.6967622.
PubMed 6967622Byg KE, Milman N, Hansen S, Agger AO. Serum Ferritin is a Reliable, Non-invasive Test for Iron Status in Pregnancy: Comparison of Ferritin with Other Iron Status Markers in a Longitudinal Study on Healthy Pregnant Women; Erythropoiesis. Hematology. 2000;5(4):319-325. doi: 10.1080/10245332.2000.11746526.
PubMed 11399631Harrison PM, Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta. 1996 Jul 31;1275(3):161-203. doi: 10.1016/0005-2728(96)00022-9.
PubMed 8695634Jacobs A, Worwood M. Ferritin in serum. Clinical and biochemical implications. N Engl J Med. 1975 May 1;292(18):951-6. doi: 10.1056/NEJM197505012921805. No abstract available.
PubMed 1090831Chen TT, Li L, Chung DH, Allen CD, Torti SV, Torti FM, Cyster JG, Chen CY, Brodsky FM, Niemi EC, Nakamura MC, Seaman WE, Daws MR. TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis. J Exp Med. 2005 Oct 3;202(7):955-65. doi: 10.1084/jem.20042433.
PubMed 16203866Li JY, Paragas N, Ned RM, Qiu A, Viltard M, Leete T, Drexler IR, Chen X, Sanna-Cherchi S, Mohammed F, Williams D, Lin CS, Schmidt-Ott KM, Andrews NC, Barasch J. Scara5 is a ferritin receptor mediating non-transferrin iron delivery. Dev Cell. 2009 Jan;16(1):35-46. doi: 10.1016/j.devcel.2008.12.002.
PubMed 19154717
Study at a glance
From the registry record, last updated by the sponsor on 5 Jan 2024. Recruitment status is as the sponsor reported it: confirm with the study team.
- Official title
- Study to Identify a Genetic Defect in Subjects With Hyperferritinemia.
- ClinicalTrials.gov ID
- NCT05659017
- Acronym / sponsor ID
- HyFerr / HyFerr
- Conditions
- Hyperferritinemia
- Study type
- Observational
- Recruitment status
- Unknown status
- Enrolment
- 100 participants (estimated)
- Lead sponsor
- University of Milano BicoccaUniversity, hospital or other
- Study start
- 6 Jun 2022 (actual)
- Primary completion
- 3 Jan 2024 (actual)
- Study completion
- 30 Sep 2024 (estimated)
- First posted
- 21 Dec 2022 (actual)
- Results
- Not posted in the source record
Clinical summary
The research question as the sponsor registered it. This describes what the study plans to test, not what it found.
Ferritin is a ubiquitous protein capable of storing iron in the cell cytosol. Stored iron is released and made available for cellular needs by the degradation of ferritin itself. Small amounts of ferritin are present in the blood and consist of ferritin L, a glycosylated form of L called ferritin G, and trace amounts of ferritin H. It is secreted mainly by macrophages, hepatocytes, and lymphoid cells, but most aspects of its secretion remain not fully elucidated. Serum ferritin has broad clinical utility primarily as an indicator of iron stores, so low values of serum ferritin are indicative of a deficient state and high values of iron overload. However, the causes of increased serum ferritin are numerous, in many cases serum ferritin is increased disproportionately to iron stores such as in acute and chronic liver disease, infectious and inflammatory states, metabolic disorders, and high alcohol intake that are frequently observed in the clinical setting. Therefore, the diagnosis of hyperferritinemia requires a careful strategy including personal and family history, biochemical, instrumental, and targeted genetic testing. In fact, there are rare forms of genetically determined hyperferritinemia not associated with iron overload, such as hereditary cataract hyperferritinemia syndrome (HHCS) due to mutations in the Iron responsive Element (IRE) located in the 5' untranslated region of the FTL gene. More recently, a second dominant form of genetic hyperferritinemia without iron overload or cataract (benign hyperferritinemia) has been identified.
Preliminary results obtained so far have made it possible, through WES analysis, to identify the involvement of the STAB1 gene, which was found to be mutated in the studied subjects in whom reduced serum ferritin glycosylation and reduced plasma concentration of the protein itself were observed. It is therefore deemed necessary to proceed with the assay of glycosylated ferritin and the protein encoded by the gene to assess its sensitivity and specificity as a predictive test before performing the genetic analysis of STAB1. To achieve this goal, patients with undefined hyperferritinemia afferent to the SSD Rare Diseases of the IRCCS San Gerardo Foundation in whom to perform glycosylated ferritin and STAB1 protein assay in parallel with STAB1 sequencing will be evaluated. Similar investigations will be performed in a control group consisting of cases of hyperferritinemia due to genetically determined iron overload.
Detailed description
Ferritin is a ubiquitous protein capable of storing iron in the cell cytosol. Cytosolic ferritin consists of two subunits, the light chain (L-ferritin) and the heavy chain (H-ferritin) that assemble in different proportions to form apo-ferritin shells. Ferritin nanoshells consist of 24 subunits of the L- and H-chains that create a cavity in which intracellular iron is collected. The stored iron is released and made available for cellular needs by the degradation of ferritin. Ferritin can bind, oxidize, and store up to 4500 Fe(II) atoms, preventing iron-mediated oxidative stress. This is achieved by regulating ferritin synthesis according to cellular iron content and oxidative stress at both the post-transcriptional (via the Iron Responsive Element (IRE)-regulatory protein (IRP) system) and transcriptional levels. Small amounts of ferritin are present in the blood and consist of ferritin L, a glycosylated form of L called ferritin G, and traces of ferritin H. It is secreted primarily by macrophages, hepatocytes, and lymphoid cells, but most aspects of its secretion remain unknown. Serum ferritin has broad clinical utility primarily as an indicator of intracellular iron stores.
The causes of increased serum ferritin are numerous, including primary and secondary iron overload disorders, but also conditions in which serum ferritin is increased disproportionately to the body's iron stores such as chronic liver disease, inflammatory and metabolic disorders that are frequently observed in the clinical setting. Therefore, the diagnosis of hyperferritinemia requires a systematic strategy including personal and family history, biochemical and instrumental tests. In addition, alterations in the regulation of ferritin synthesis due to mutations in the iron-sensitive element L-ferritin (IRE) cause hereditary hyperferritinemia cataract syndrome (HHCS), an inherited disease characterized by elevated serum ferritin without iron overload and early onset of bilateral cataracts. Recently, a second dominant form of genetic hyperferritinemia without iron overload or cataract has been reported. Amino acid substitutions at positions 26, 27, and 30 in the heterozygous state in the L-ferritin A helix have been found in these patients. The resulting ferritin appears unusually susceptible to glycosylation, leading to serum glycosylated ferritin values consistently >90%. The reason for the development of hyperferritinemia and hyperglycosylation associated with these mutant forms of ferritin has not been established. It is probably related to increased secretion, but may also contribute to delayed clearance. Some cases of hyperferritinemia still remain unexplained, and the currently unknown candidate gene that we think we have identified among candidate genes needs to be validated in a larger population of subjects with the listed characteristics.
The primary objective of the study is to sequence the candidate gene that emerged from previous studies as mutated in patients with the same clinical features.
The secondary objective is to include the candidate gene in the routine genetic diagnosis of subjects with hyperferritinemia without tissue iron overload.
The study will last about 12 months the time needed for the recovery of patients with a genetic diagnosis not yet defined, analysis of medical records and research of the DNA sample stored at the Laboratory of Cytogenetics and Medical Genetics of San Gerardo Hospital and genetic analysis by Next Generation Sequencing. The study, although simple in its idea, requires a very careful organization of access and monitoring of selected patients that require the presence of a study manager dedicated to the project.
The study extension includes:glycosylated ferritin assay in patients with hyperferritinemia referred to the Rare Disease Center of IRCCS Foundation - San Gerardo dei Tintori selected according to the inclusion and exclusion criteria; soluble protein assay encoded by the STAB1 gene in patients in point A and patients in group D.
Study design
- Observational model
- Cohort
- Time perspective
- Retrospective
Who may qualify
- Ages
- 18 to 80 years
- Sex
- All
- Healthy volunteers
- Not accepted
- Age groups
- Adult, Older adult
- Study population
- Hyperferritinemia patients followed at the Rare Diseases Center in San Gerardo Hospital
Key inclusion criteria (4 listed)
- Among patients referred to the Center for Rare Diseases of Monza will be enrolled only subjects with:
- ferritin > 1000 g / L in men and > 500 g / L,
- transferrin saturation <45%
- absence of hepatic iron overload, evaluated by liver biopsy or MRI, as indicated in the attached flow chart.
Key exclusion criteria (9 listed)
- genetically determined causes [mutations in the HFE gene (homozygosity or heterozygosity for p.Cys282Tyr, homozygosity for p.His63Asp or compound heterozygosity for variants of p.Cys282Tyr and p. His63Asp), ferroportin and L-Ferritin gene mutations];
- presence of more than one component of metabolic syndrome (according to NCEP-ATPIII criteria: triglycerides >150 mg/dL, blood glucose >100 mg/dL, HDL <40 mg/dL in men and <50 mg/dL in women, waist circumference >102 cm in men and >88 cm in women; blood pressure ≥130/≥85 mm/Hg);
- alcohol intake >5 g/day chronic hepatitis,
- history of blood transfusion or parenteral iron treatment,
- late skin porphyria,
Eligibility is decided by the study team after screening; this overview does not establish that a patient qualifies. Full inclusion and exclusion criteria.
Interventions
| Intervention | Type | Arms |
|---|---|---|
| Genetic analysisThe DNA will then be analyzed with a custom panel designed ad hoc to study the candidate gene by Next Generation Sequencing according to the protocols of the supplier of the kit. | Genetic | – |
Primary outcome
Candidate gene sequencing
Time frame: 1 year
For the purpose 100 patients are sufficient to calculate both the allelic and genotypic frequency of mutations in the candidate gene.
1 secondary outcome
DIAGNOSIS ROUTINE
Time frame: 1 year
Results and safety
Results are not available in the source record.
Research links
- Official record on ClinicalTrials.govLast updated by the sponsor 5 Jan 2024.
- Results publication: PubMed 20176086Arosio P, Levi S. Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage. Biochim Biophys Acta. 2010 Aug;1800(8):783-92. doi: 10.1016/j.bbagen.2010.02.005. Epub 2010 Feb 20.
- Results publication: PubMed 11986201Torti FM, Torti SV. Regulation of ferritin genes and protein. Blood. 2002 May 15;99(10):3505-16. doi: 10.1182/blood.v99.10.3505. No abstract available.
- Results publication: PubMed 25119494Finazzi D, Arosio P. Biology of ferritin in mammals: an update on iron storage, oxidative damage and neurodegeneration. Arch Toxicol. 2014 Oct;88(10):1787-802. doi: 10.1007/s00204-014-1329-0. Epub 2014 Aug 15.
- Results publication: PubMed 21348856Wang J, Pantopoulos K. Regulation of cellular iron metabolism. Biochem J. 2011 Mar 15;434(3):365-81. doi: 10.1042/BJ20101825.
- Results publication: PubMed 7363568Cragg SJ, Wagstaff M, Worwood M. Sialic acid and the microheterogeneity of human serum ferritin. Clin Sci (Lond). 1980 Mar;58(3):259-62. doi: 10.1042/cs0580259.
- Results publication: PubMed 3828232Santambrogio P, Cozzi A, Levi S, Arosio P. Human serum ferritin G-peptide is recognized by anti-L ferritin subunit antibodies and concanavalin-A. Br J Haematol. 1987 Feb;65(2):235-7. doi: 10.1111/j.1365-2141.1987.tb02271.x.
- Results publication: PubMed 20472835Cohen LA, Gutierrez L, Weiss A, Leichtmann-Bardoogo Y, Zhang DL, Crooks DR, Sougrat R, Morgenstern A, Galy B, Hentze MW, Lazaro FJ, Rouault TA, Meyron-Holtz EG. Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway. Blood. 2010 Sep 2;116(9):1574-84. doi: 10.1182/blood-2009-11-253815. Epub 2010 May 14.
- Results publication: PubMed 7459278Mack U, Cooksley WG, Ferris RA, Powell LW, Halliday JW. Regulation of plasma ferritin by the isolated perfused rat liver. Br J Haematol. 1981 Mar;47(3):403-12. doi: 10.1111/j.1365-2141.1981.tb02808.x.
- Results publication: PubMed 9389717Tran TN, Eubanks SK, Schaffer KJ, Zhou CY, Linder MC. Secretion of ferritin by rat hepatoma cells and its regulation by inflammatory cytokines and iron. Blood. 1997 Dec 15;90(12):4979-86.
- Results publication: PubMed 6967622Dorner MH, Silverstone A, Nishiya K, de Sostoa A, Munn G, de Sousa M. Ferritin synthesis by human T lymphocytes. Science. 1980 Aug 29;209(4460):1019-21. doi: 10.1126/science.6967622.
- Results publication: PubMed 11399631Byg KE, Milman N, Hansen S, Agger AO. Serum Ferritin is a Reliable, Non-invasive Test for Iron Status in Pregnancy: Comparison of Ferritin with Other Iron Status Markers in a Longitudinal Study on Healthy Pregnant Women; Erythropoiesis. Hematology. 2000;5(4):319-325. doi: 10.1080/10245332.2000.11746526.
- Results publication: PubMed 8695634Harrison PM, Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta. 1996 Jul 31;1275(3):161-203. doi: 10.1016/0005-2728(96)00022-9.
- Individual participant dataSharing planned: No
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Referral and contact
AzTrials does not enrol participants or take referrals. Contact the study team or a site listed below; they decide who can take part. This study is not recruiting at the moment.
1 site in 1 country: see every site and its status.
Questions about this trial
What is this clinical trial studying?
An observational study of Hyperferritinemia, run by University of Milano Bicocca at 1 site in Italy.
The full registered description is in the About this study section and the official record.
Who may be eligible to take part?
The sponsor lists 4 inclusion and 9 exclusion criteria. Eligibility is decided by the study team after screening, so read the full criteria and contact a listed site.
Is this clinical trial currently recruiting?
The record says: status not confirmed, as of the sponsor's last update on 5 Jan 2024. Status can change between updates, so confirm with the study contact before making plans.
Where is the study taking place?
The record lists 1 site in Italy. Whether a site is taking part right now should be confirmed with that site. See every site.
What are the possible benefits and risks?
They depend on the study and the treatment, and no study can promise a benefit. The study team explains the known risks during informed consent, before anyone joins; the record itself does not list them.
Are results available for this study?
Results are not available in the source record.
How can a doctor refer a patient or contact the research team?
Contact Raffaella Mariani, Dr.ssa (+390392339555, r.mariani@asst-monza.it), or a site near the patient. AzTrials does not enrol participants or take referrals.
What does the primary outcome measure?
Candidate gene sequencing (time frame: 1 year). It is what the study was designed to measure, not a finding.
Where can I read the original study information?
On the ClinicalTrials.gov record for NCT05659017, which also lists 23 linked publications.
Does a listing mean the treatment is approved or proven to work?
No. A listing means the study is registered. It does not show that the treatment is safe, works, or is approved by a regulator.
How often is this information updated?
AzTrials copies changed records from ClinicalTrials.gov every night and reloads the whole registry every week. The sponsor last updated this record on 5 Jan 2024.