ReviewBiomolecules2023
Heme Scavenging and Delivery: The Role of Human Serum Albumin.
Review in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Heme enhances B-cell proliferation and plasma cell formation through reduced p21 and Rb expression.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- Murine Biocompatibility Evaluation of an Albumin-Derived Complex and Nanoparticle Delivery System for Ocular Applications.Journal of biomedical materials research. Part A · 2026Article
- The survival status ofJournal of oral microbiology · 2026Review
- Binding and transport functions of human serum albumin and its clinical implications in liver disease: a narrative review.Translational gastroenterology and hepatology · 2026Review
- Role of hydrogen sulfide in catalyzing the formation of NO-ferroheme.Nitric oxide : biology and chemistry · 2025Article
- Structural Instability of Human Serum Albumin during Microparticles Synthesis.ACS applied bio materials · 2025Article
- Dual-Function Role of Phenolated Albumin in Hemin-Mediated Hydrogel Formation.Gels (Basel, Switzerland) · 2025Article
- Heme and iron toxicity in the aged spleen impairs T cell immunity through iron deprivation.Nature aging · 2025Article
- The interactions of non-functionalized polystyrene nanoparticles with human albumin and erythrocyte proteins: implications and potential consequences.Scientific reports · 2025Article
- Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- HmuY proteins of theFrontiers in cellular and infection microbiology · 2025Article
- Regulated cell death and DAMPs as biomarkers and therapeutic targets in normothermic perfusion of transplant organs. Part 2: implementation strategies.Frontiers in transplantation · 2025Review
- Wolf in Sheep's Clothing: Taming Cancer's Resistance with Human Serum Albumin?International journal of nanomedicine · 2025Review
- Role of environmental pollutants-induced ferroptosis in pulmonary diseases.Frontiers in medicine · 2025Review
- Defining the role of Hmu and Hus systems in Porphyromonas gingivalis heme and iron homeostasis and virulence.Scientific reports · 2024Article
- Targeting circulating labile heme as a defense strategy against malaria.Life science alliance · 2024Article
- The Hepatic Porphyrias: Revealing the Complexities of a Rare Disease.Seminars in liver disease · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heme is the reactive center of several metal-based proteins that are involved in multiple biological processes. However, free heme, defined as the labile heme pool, has toxic properties that are derived from its hydrophobic nature and the Fe-atom. Therefore, the heme concentration must be tightly controlled to maintain cellular homeostasis and to avoid pathological conditions. Therefore, different systems have been developed to scavenge either Hb (i.e., haptoglobin (Hp)) or the free heme (i.e., high-density lipoproteins (HDL), low-density lipoproteins (LDL), hemopexin (Hx), and human serum albumin (HSA)). In the first seconds after heme appearance in the plasma, more than 80% of the heme binds to HDL and LDL, and only the remaining 20% binds to Hx and HSA. Then, HSA slowly removes most of the heme from HDL and LDL, and finally, heme transits to Hx, which releases it into hepatic parenchymal cells. The Hx:heme or HSA:heme complexes are internalized via endocytosis mediated by the CD91 and CD71 receptors, respectively. As heme constitutes a major iron source for pathogens, bacteria have evolved hemophores that can extract and uptake heme from host proteins, including HSA:heme. Here, the molecular mechanisms underlying heme scavenging and delivery from HSA are reviewed. Moreover, the relevance of HSA in disease states associated with increased heme plasma concentrations are discussed.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.