Gaucher Disease Due to Saposin C Deficiency (PSAP/SapC): Comprehensive Disease Characteristics Report

Target disease

• Disease name: Gaucher disease due to saposin C deficiency (PSAP-related “atypical Gaucher disease”) (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2)
• Category: Mendelian / lysosomal storage disease (autosomal recessive) (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2)
• MONDO ID: Not identified in the retrieved full-text evidence set (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2)

1. Disease Information

1.1 Concise overview (current understanding)

Gaucher disease due to saposin C deficiency is an ultra-rare lysosomal disorder in which biallelic pathogenic variants in PSAP (prosaposin) impair production/function of saposin C (SapC), an essential activator/cofactor for lysosomal glucocerebrosidase (GCase). This causes a Gaucher-like phenotype via impaired degradation of glucosylceramide (GlcCer) and related sphingolipids, and can clinically resemble non-neuronopathic (type 1-like) or neuronopathic (type 3-like) Gaucher disease—sometimes despite normal in vitro GCase activity assays (tamargo2012theroleof pages 1-2, rafi1993mutationalanalysisin pages 1-3, motta2014gaucherdiseasedue pages 1-2).

1.2 Key identifiers (as evidenced in retrieved literature)

Table: This table summarizes the key disease and gene identifiers, core synonyms, and classification facts for Gaucher disease due to saposin C deficiency. It is useful for normalizing nomenclature and linking PSAP-related disease concepts to canonical Gaucher disease subtypes.

Notes on identifiers: Orphanet, MeSH, ICD-10/ICD-11, and MONDO identifiers were not present in the retrieved documents and therefore cannot be reliably populated from this evidence set (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2).

1.3 Synonyms / alternative names

• Gaucher disease due to saposin C deficiency (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2)
• Variant Gaucher disease caused by SAP-2 / saposin C (historical terminology) (rafi1993mutationalanalysisin pages 1-3)
• Atypical Gaucher disease due to PSAP (liaqat2022phenotypeexpansionfor pages 5-7, liaqat2022phenotypeexpansionfor pages 1-2)

1.4 Evidence provenance

The evidence base is dominated by single-patient case reports and small families, plus mechanistic in vitro and animal-model studies; it is not derived from EHR-scale aggregated cohorts (tamargo2012theroleof pages 5-7, liaqat2022phenotypeexpansionfor pages 5-7).

2. Etiology

2.1 Primary causal factors

• Genetic cause: biallelic pathogenic variants in PSAP affecting the SapC domain (autosomal recessive) (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2).
• Mechanistic cause: loss of functional SapC reduces/impairs membrane-associated GCase activity and/or stability, leading to lysosomal glycosphingolipid storage (GlcCer ± GlcSph and other sphingolipids) and downstream macrophage and/or CNS pathology (tamargo2012theroleof pages 4-5, motta2014gaucherdiseasedue pages 1-2, pavan2024deficiencyofglucocerebrosidase pages 9-10).

2.2 Risk factors

• Genetic: consanguinity increases risk by increasing probability of homozygous PSAP variants; a large consanguineous Pakistani family with multiple affected individuals has been reported (liaqat2022phenotypeexpansionfor pages 5-7).
• Environmental / infectious: no disease-specific environmental or infectious risk factors were identified in the retrieved evidence.

2.3 Protective factors

No protective genetic or environmental factors were reported in the retrieved evidence.

2.4 Gene–environment interactions

No PSAP SapC-deficiency-specific gene–environment interaction evidence was found in the retrieved documents.

3. Phenotypes (clinical features) and ontology mapping

3.1 Phenotype spectrum and clinical heterogeneity

Across the limited number of reported patients, SapC deficiency can produce type 1-like (visceral/hematologic/bone) disease and/or type 3-like neuronopathic disease. A review of six reported patients described presentations ranging from type 1-like to type 3-like, including adult siblings with mild neurologic deterioration (tamargo2012theroleof pages 5-7, tamargo2012theroleof pages 1-2).

3.2 Structured phenotype + diagnostic feature table (with HPO suggestions)

Table: This table summarizes the reported clinical spectrum and key diagnostic findings for Gaucher disease due to saposin C deficiency caused by PSAP variants. It is useful for distinguishing this ultra-rare activator deficiency from canonical GBA1-related Gaucher disease, especially when enzyme activity is normal or only mildly reduced.

3.3 Quality of life impact

Formal QoL instruments (e.g., EQ-5D/SF-36/PROMIS) were not reported in the retrieved evidence. Severe infantile neuronopathic disease is expected to substantially impair functioning (hypotonia, swallowing difficulty, seizures), while chronic neurologic disease (ataxia) and visceral disease (organomegaly, cytopenias) can impair daily activity and endurance (pavan2024deficiencyofglucocerebrosidase pages 2-4, tamargo2012theroleof pages 1-2).

4. Genetic / Molecular Information

4.1 Causal gene(s)

• PSAP (prosaposin; SapC derived from prosaposin proteolysis) (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2).

4.2 Pathogenic variants (examples from primary/review literature)

Evidence-supported PSAP/SapC-domain pathogenic or likely pathogenic variants include: - c.1144T>G (p.Cys382Gly) reported in a variant Gaucher case with glucosylceramide accumulation despite normal measured glucocerebrosidase activity (rafi1993mutationalanalysisin pages 1-3). - SapC lesions summarized in mechanistic work: p.C315S, p.342_348FDKMCSKdel, p.L349P, p.C382G, p.C382F (motta2014gaucherdiseasedue pages 1-2). - A consanguineous family with likely pathogenic c.1076A>C (p.Glu359Ala) in the SapC domain; variant is rare in gnomAD and lies in the SapC GCase-binding region (aa 351–390) (liaqat2022phenotypeexpansionfor pages 5-7). - Severe infantile case: c.889G>T (p.E297*) with nonsense-mediated mRNA decay; GD2-like suspicion clinically (pavan2024deficiencyofglucocerebrosidase pages 2-4).

Variant classes observed: missense, in-frame deletion, nonsense, splice-site; many reported variants affect SapC cysteines/disulfide bonds or otherwise destabilize the SapC fold (tamargo2012theroleof pages 5-7, motta2014gaucherdiseasedue pages 1-2).

4.3 Functional consequences

• SapC is a small, cysteine-rich activator/cofactor with disulfide bonds that confer acid stability; multiple disease mutants adopt aberrant disulfide arrangements and are rapidly degraded, with evidence implicating autophagy-mediated degradation as a key pathogenic mechanism in SapC deficiency (motta2014gaucherdiseasedue pages 1-2).
• SapC also protects GCase from proteolysis; absence of SapC can reduce tissue GCase activity and increase degradation, which can be modulated by protease inhibitors in experimental systems (tamargo2012theroleof pages 4-5).

4.4 Modifier genes / epigenetics / chromosomal abnormalities

No SapC-deficiency-specific modifier gene, epigenetic, or chromosomal abnormality evidence was found in the retrieved documents.

5. Environmental Information

No disease-specific environmental, lifestyle, or infectious contributors were identified in the retrieved evidence; the disorder is primarily genetic (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2).

6. Mechanism / Pathophysiology

6.1 Causal chain (trigger → molecular defect → cellular dysfunction → clinical phenotype)

1. Upstream trigger: biallelic PSAP variants reduce/abolish functional SapC production or stability (including nonsense-mediated decay for truncating variants) (pavan2024deficiencyofglucocerebrosidase pages 2-4, pavan2024deficiencyofglucocerebrosidase pages 9-10).
2. Primary molecular defect: SapC normally binds anionic lysosomal membranes and GCase, enabling membrane-associated presentation/access of GlcCer to the enzyme; SapC also stabilizes/protects GCase from proteolysis (tamargo2012theroleof pages 4-5, tamargo2012theroleof pages 5-7).
3. Biochemical consequence: reduced effective GCase-mediated degradation causes storage of GlcCer and often glucosylsphingosine (GlcSph) (and sometimes other sphingolipids) (tamargo2012theroleof pages 5-7, pavan2024deficiencyofglucocerebrosidase pages 9-10).
4. Cellular pathology: lipid-laden macrophages (“Gaucher cells”) drive inflammation and visceral disease; in neuronopathic cases, CNS pathology includes neuronal inclusions, Purkinje cell loss, axonal degeneration, and glial activation/inflammation (sun2010specificsaposinc pages 1-2, tamargo2012theroleof pages 5-7).
5. Clinical manifestations: hepatosplenomegaly, cytopenias, bone disease; and/or neurologic impairment (hypotonia, seizures, ataxia, abnormal eye movements, etc.) (tamargo2012theroleof pages 1-2, pavan2024deficiencyofglucocerebrosidase pages 2-4).

6.2 Pathways, processes, and suggested GO terms

Key molecular/cellular processes (GO Biological Process suggestions): - Lysosomal glycosphingolipid catabolic process / sphingolipid metabolic process (supported conceptually by impaired GlcCer breakdown) (pavan2024deficiencyofglucocerebrosidase pages 1-2, pavan2024deficiencyofglucocerebrosidase pages 9-10) - Lysosome organization and membrane-associated catabolism (SapC-mediated membrane interaction/liftase model) (tamargo2012theroleof pages 4-5) - Autophagy (as a degradation route for mutant SapC proteins) (motta2014gaucherdiseasedue pages 1-2) - Neuroinflammatory response / glial activation (microglia, astrocytes activated in SapC-deficient mouse CNS) (sun2010specificsaposinc pages 1-2)

6.3 Cell types and suggested CL terms

Cell Ontology (CL) suggestions based on evidence: - Macrophage (Gaucher cells; mononuclear phagocyte system involvement) (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2) - Microglial cell (activated microglia in SapC-deficient mouse CNS) (sun2010specificsaposinc pages 1-2) - Astrocyte (astrocyte activation in SapC-deficient mouse CNS) (sun2010specificsaposinc pages 1-2) - Purkinje cell (cerebellar Purkinje neuron loss in SapC-deficient mouse model) (sun2010specificsaposinc pages 1-2)

6.4 Expert mechanistic analysis (authoritative synthesis)

High-citation expert reviews emphasize that SapC functions as a membrane-active cofactor enabling optimal GCase function and that SapC deficiency can yield a Gaucher phenotype even with apparently normal in vitro enzyme assays, which has important diagnostic implications (tamargo2012theroleof pages 1-2, tamargo2012theroleof pages 4-5).

Direct abstract quote (animal model; mechanistic): - Sun et al. report: “The few patients with saposin C deficiency develop a Gaucher disease-like central nervous system (CNS) phenotype attributed to diminished glucosylceramide (GC) cleavage activity by acid β-glucosidase (GCase).” (Human Molecular Genetics; Dec 2010; https://doi.org/10.1093/hmg/ddp531) (sun2010specificsaposinc pages 1-2)

7. Anatomical Structures Affected

7.1 Organ/system level (UBERON suggestions)

• Liver / spleen (hepatosplenomegaly): mononuclear phagocyte system storage involvement (UBERON: liver; UBERON: spleen) (tamargo2012theroleof pages 1-2, pavan2024deficiencyofglucocerebrosidase pages 2-4).
• Bone / skeletal system: bone lesions and kyphosis reported; osteoarticular involvement is typical of Gaucher-like disease (UBERON: bone of lower limb / vertebral column) (tamargo2012theroleof pages 1-2, liaqat2022phenotypeexpansionfor pages 5-7).
• Central nervous system: neuronopathic presentations include seizures, hypotonia, ataxia, eye movement abnormalities; SapC-deficient mice show cerebellar and axonal pathology (UBERON: brain; UBERON: cerebellum; UBERON: spinal cord) (sun2010specificsaposinc pages 1-2, pavan2024deficiencyofglucocerebrosidase pages 2-4).

7.2 Tissue/cell level

• Monocyte/macrophage lineage cells with lysosomal lipid storage (motta2014gaucherdiseasedue pages 1-2).
• Cerebellar neuronal populations (Purkinje cells) and glial cells (microglia, astrocytes) in neurologic disease models (sun2010specificsaposinc pages 1-2).

7.3 Subcellular level (GO Cellular Component suggestions)

• Lysosome (site of glycosphingolipid catabolism and SapC–GCase function) (pavan2024deficiencyofglucocerebrosidase pages 1-2, tamargo2012theroleof pages 4-5).

8. Temporal Development

8.1 Onset

Onset is variable, ranging from infantile severe neurologic disease (including GD2-like presentations) to childhood/adult-onset neurologic deterioration or more type 1-like disease without clear CNS signs in some families (pavan2024deficiencyofglucocerebrosidase pages 2-4, tamargo2012theroleof pages 5-7, liaqat2022phenotypeexpansionfor pages 5-7).

8.2 Progression

Severe infantile cases may progress rapidly and can be fatal within months (pavan2024deficiencyofglucocerebrosidase pages 2-4). Other cases show chronic neurologic progression (e.g., ataxia) or chronic visceral disease (tamargo2012theroleof pages 5-7, tamargo2012theroleof pages 1-2).

9. Inheritance and Population

9.1 Inheritance

Autosomal recessive inheritance is strongly supported by multiple reports of homozygous/biallelic PSAP variants and occurrence in consanguineous families (tamargo2012theroleof pages 1-2, liaqat2022phenotypeexpansionfor pages 5-7, pavan2024deficiencyofglucocerebrosidase pages 2-4).

9.2 Epidemiology

No population-level prevalence or incidence estimates were identified in the retrieved literature. Available synthesis notes only a handful of published patients worldwide (e.g., six described in one review; and ~seven reported cases cited in a later family report), consistent with an ultra-rare condition (tamargo2012theroleof pages 5-7, liaqat2022phenotypeexpansionfor pages 5-7).

9.3 Population genetics / allele frequency example

The likely pathogenic PSAP c.1076A>C (p.Glu359Ala) variant was reported as rare in gnomAD (overall AF 5.3×10−5; South Asian AF 3.6×10−4; no homozygotes in gnomAD per authors) (liaqat2022phenotypeexpansionfor pages 5-7).

10. Diagnostics

10.1 Clinical suspicion

Consider PSAP/SapC deficiency when a patient has a Gaucher-like phenotype (hepatosplenomegaly, cytopenias ± bone disease and/or neurologic disease) but: - GBA1 testing is negative, and/or - GCase activity is normal/low-normal on standard assays (diagnostic pitfall), and/or - biomarkers suggest Gaucher-like macrophage activation and glycosphingolipid storage (pavan2024deficiencyofglucocerebrosidase pages 2-4, rafi1993mutationalanalysisin pages 1-3, tamargo2012theroleof pages 1-2).

10.2 Laboratory biomarkers and statistics from recent study (2024)

A 2024 biochemical profiling study reports markedly elevated Gaucher biomarkers in a PSAP case (PSAP_PT): - Chitotriosidase: 2951.0 nmol/mL/h - Plasma glucosylsphingosine (GlcSph): 19.0 ng/mL - Lyso-Gb3: 1.98 ng/mL - PPCS: 745.9 ng/mL with a homozygous truncating PSAP variant (c.889G>T; p.E297*) and severe infantile disease (Jun 2024; https://doi.org/10.3390/ijms25126615) (pavan2024deficiencyofglucocerebrosidase pages 2-4).

10.3 Enzyme activity testing caveat

A seminal primary report documented glucosylceramide accumulation in spleen despite normal measured glucocerebrosidase activity, supporting “activator deficiency” rather than enzyme deficiency (rafi1993mutationalanalysisin pages 1-3).

10.4 Genetic testing approach

• Confirmatory testing is PSAP sequencing (single-gene, lysosomal storage disease panels, or exome/genome sequencing) and variant interpretation in the context of phenotype and biochemical findings (liaqat2022phenotypeexpansionfor pages 5-7, pavan2024deficiencyofglucocerebrosidase pages 2-4).

11. Outcome / Prognosis

Prognosis appears highly variable and genotype/phenotype dependent. A severe infantile PSAP truncating-variant case with GD2-like features died a few months after diagnosis (pavan2024deficiencyofglucocerebrosidase pages 2-4). Milder phenotypes without overt CNS involvement have been reported in families, implying potentially longer survival (liaqat2022phenotypeexpansionfor pages 5-7). Systematic survival statistics are not available in the retrieved evidence.

12. Treatment

12.1 Disease-directed therapies

No controlled clinical trial evidence specific to SapC deficiency treatment was identified in the retrieved documents, and the clinical trials search did not return SapC-deficiency-specific interventional trials.

Mechanistically, SapC deficiency is an activator/cofactor deficiency rather than a primary GCase catalytic deficiency. Expert reviews discuss that increasing SapC levels or restoring SapC–GCase interactions could be therapeutic in principle, and that chemical chaperones can improve folding/trafficking and SapC–enzyme interactions in experimental contexts, but these are not presented as established clinical therapies for SapC deficiency in the retrieved evidence (tamargo2012theroleof pages 5-7, tamargo2012theroleof pages 7-8).

12.2 Supportive care

Supportive management is implied by clinical features (e.g., management of cytopenias, organomegaly complications, seizures, swallowing dysfunction), but specific guidelines were not found in the retrieved evidence.

12.3 MAXO term suggestions

• Enzyme activity assay / enzyme replacement-related actions are not directly evidenced as effective here; nevertheless, for knowledge-base normalization:
• MAXO: enzyme replacement therapy (as a general Gaucher therapy class; disease-specific effectiveness for SapC deficiency not evidenced)
• MAXO: anticonvulsant therapy (for seizure management in neuronopathic presentations)
• MAXO: supportive respiratory care / feeding support (for severe infantile neurologic disease)

13. Prevention

13.1 Primary/secondary prevention (genetic)

Given autosomal recessive inheritance, prevention is primarily through genetic counseling and prenatal or preimplantation genetic testing in families with known PSAP variants. A PSAP-related infantile case report summary indicates prenatal diagnosis in a subsequent pregnancy identified a carrier fetus who was unaffected postnatally (reported as part of the PSAP infantile case summary in a synthesis) (li2025prosaposinamultifaceted pages 10-11).

14. Other Species / Natural Disease

Natural SapC-deficiency animal disease was not identified in the retrieved evidence.

15. Model Organisms

15.1 Mouse models

A selective SapC-deficient mouse model (knock-in point mutation eliminating SapC) exhibits a CNS-predominant phenotype (hindlimb weakness, progressive ataxia, neurophysiologic impairment, dorsal root ganglion storage cells, Purkinje cell loss, glial activation) with little/no visceral organ storage—highlighting both mechanistic insight and limitations in recapitulating human visceral disease (sun2010specificsaposinc pages 1-2).

Direct abstract quote (mouse model): - “By 1 year, the C−/− mice exhibited weakness of the hind limbs and progressive ataxia.” (Human Molecular Genetics; Dec 2010; https://doi.org/10.1093/hmg/ddp531) (sun2010specificsaposinc pages 1-2)

2023–2024 developments and real-world implementation highlights

1. 2024 biochemical profiling beyond GBA1 Gaucher disease: A 2024 study explicitly compares GCase-deficiency etiologies (GBA1 vs PSAP vs SCARB2/LIMP-2) and provides quantified biomarker data (chitotriosidase, GlcSph, Lyso-Gb3, PPCS) in a PSAP case, supporting real-world diagnostic workflows for “Gaucher-like” presentations with negative GBA1 testing (Jun 2024; https://doi.org/10.3390/ijms25126615) (pavan2024deficiencyofglucocerebrosidase pages 2-4, pavan2024deficiencyofglucocerebrosidase pages 1-2).
2. 2023 case-based evidence of PSAP-related disease burden: A 2023 neonatal case report of combined saposin deficiency illustrates severe neurovisceral presentations and reinforces that enzymatic and genetic confirmation plus counseling are implemented in real clinical settings (Mar 2023; https://doi.org/10.1016/j.mjafi.2021.01.024) (bhat2023combinedsaposindeficiency pages 1-2).

Evidence gaps (important for knowledge base curation)

• Orphanet/MONDO/MeSH/ICD identifiers were not extractable from the retrieved full text and should be populated via dedicated database lookup rather than inferred here (tamargo2012theroleof pages 1-2, motta2014gaucherdiseasedue pages 1-2).
• Treatment efficacy evidence (ERT/SRT/gene therapy) specifically for SapC deficiency was not found in the retrieved documents; mechanistic speculation exists, but clinical outcome evidence is not available in this evidence set (tamargo2012theroleof pages 5-7).
• Epidemiology (prevalence/incidence) is not available in the retrieved literature, beyond statements of extreme rarity and small numbers of published cases (tamargo2012theroleof pages 5-7, liaqat2022phenotypeexpansionfor pages 5-7).

References

1. (tamargo2012theroleof pages 1-2): Rafael J. Tamargo, Arash Velayati, Ehud Goldin, and Ellen Sidransky. The role of saposin c in gaucher disease. Molecular genetics and metabolism, 106 3:257-63, Jul 2012. URL: https://doi.org/10.1016/j.ymgme.2012.04.024, doi:10.1016/j.ymgme.2012.04.024. This article has 208 citations and is from a peer-reviewed journal.

2. (motta2014gaucherdiseasedue pages 1-2): Marialetizia Motta, Serena Camerini, Massimo Tatti, Marialuisa Casella, Paola Torreri, Marco Crescenzi, Marco Tartaglia, and Rosa Salvioli. Gaucher disease due to saposin c deficiency is an inherited lysosomal disease caused by rapidly degraded mutant proteins. Human molecular genetics, 23 21:5814-26, Nov 2014. URL: https://doi.org/10.1093/hmg/ddu299, doi:10.1093/hmg/ddu299. This article has 45 citations and is from a domain leading peer-reviewed journal.

3. (rafi1993mutationalanalysisin pages 1-3): Mohammad A. Rafi, Gregory Gala, Xun-ling Zhang, and David A. Wenger. Mutational analysis in a patient with a variant form of gaucher disease caused by sap-2 deficiency. Somatic Cell and Molecular Genetics, 19:1-7, Jan 1993. URL: https://doi.org/10.1007/bf01233949, doi:10.1007/bf01233949. This article has 102 citations.

4. (liaqat2022phenotypeexpansionfor pages 1-2): Khurram Liaqat, Shabir Hussain, Anushree Acharya, Abdul Nasir, Thashi Bharadwaj, Muhammad Ansar, Sulman Basit, Isabelle Schrauwen, Wasim Ahmad, and Suzanne M. Leal. Phenotype expansion for atypical gaucher disease due to homozygous missense psap variant in a large consanguineous pakistani family. Genes, 13:662, Apr 2022. URL: https://doi.org/10.3390/genes13040662, doi:10.3390/genes13040662. This article has 15 citations.

5. (liaqat2022phenotypeexpansionfor pages 5-7): Khurram Liaqat, Shabir Hussain, Anushree Acharya, Abdul Nasir, Thashi Bharadwaj, Muhammad Ansar, Sulman Basit, Isabelle Schrauwen, Wasim Ahmad, and Suzanne M. Leal. Phenotype expansion for atypical gaucher disease due to homozygous missense psap variant in a large consanguineous pakistani family. Genes, 13:662, Apr 2022. URL: https://doi.org/10.3390/genes13040662, doi:10.3390/genes13040662. This article has 15 citations.

6. (pavan2024deficiencyofglucocerebrosidase pages 2-4): Eleonora Pavan, Paolo Peruzzo, Silvia Cattarossi, Natascha Bergamin, Andrea Bordugo, Annalisa Sechi, Maurizio Scarpa, Jessica Biasizzo, Fabiana Colucci, and Andrea Dardis. Deficiency of glucocerebrosidase activity beyond gaucher disease: psap and limp-2 dysfunctions. International Journal of Molecular Sciences, 25:6615, Jun 2024. URL: https://doi.org/10.3390/ijms25126615, doi:10.3390/ijms25126615. This article has 10 citations.

7. (pavan2024deficiencyofglucocerebrosidase pages 1-2): Eleonora Pavan, Paolo Peruzzo, Silvia Cattarossi, Natascha Bergamin, Andrea Bordugo, Annalisa Sechi, Maurizio Scarpa, Jessica Biasizzo, Fabiana Colucci, and Andrea Dardis. Deficiency of glucocerebrosidase activity beyond gaucher disease: psap and limp-2 dysfunctions. International Journal of Molecular Sciences, 25:6615, Jun 2024. URL: https://doi.org/10.3390/ijms25126615, doi:10.3390/ijms25126615. This article has 10 citations.

8. (tamargo2012theroleof pages 5-7): Rafael J. Tamargo, Arash Velayati, Ehud Goldin, and Ellen Sidransky. The role of saposin c in gaucher disease. Molecular genetics and metabolism, 106 3:257-63, Jul 2012. URL: https://doi.org/10.1016/j.ymgme.2012.04.024, doi:10.1016/j.ymgme.2012.04.024. This article has 208 citations and is from a peer-reviewed journal.

9. (tamargo2012theroleof pages 4-5): Rafael J. Tamargo, Arash Velayati, Ehud Goldin, and Ellen Sidransky. The role of saposin c in gaucher disease. Molecular genetics and metabolism, 106 3:257-63, Jul 2012. URL: https://doi.org/10.1016/j.ymgme.2012.04.024, doi:10.1016/j.ymgme.2012.04.024. This article has 208 citations and is from a peer-reviewed journal.

10. (pavan2024deficiencyofglucocerebrosidase pages 9-10): Eleonora Pavan, Paolo Peruzzo, Silvia Cattarossi, Natascha Bergamin, Andrea Bordugo, Annalisa Sechi, Maurizio Scarpa, Jessica Biasizzo, Fabiana Colucci, and Andrea Dardis. Deficiency of glucocerebrosidase activity beyond gaucher disease: psap and limp-2 dysfunctions. International Journal of Molecular Sciences, 25:6615, Jun 2024. URL: https://doi.org/10.3390/ijms25126615, doi:10.3390/ijms25126615. This article has 10 citations.

11. (li2025prosaposinamultifaceted pages 10-11): Xin Li and Liang Guo. Prosaposin: a multifaceted protein orchestrating biological processes and diseases. Cells, 14:1131, Jul 2025. URL: https://doi.org/10.3390/cells14151131, doi:10.3390/cells14151131. This article has 10 citations.

12. (sun2010specificsaposinc pages 1-2): Y. Sun, H. Ran, M. Zamzow, K. Kitatani, M. R. Skelton, M. T. Williams, C. V. Vorhees, D. P. Witte, Y. A. Hannun, and G. A. Grabowski. Specific saposin c deficiency: cns impairment and acid β-glucosidase effects in the mouse. Human Molecular Genetics, 19:634-647, Dec 2010. URL: https://doi.org/10.1093/hmg/ddp531, doi:10.1093/hmg/ddp531. This article has 41 citations and is from a domain leading peer-reviewed journal.

13. (li2025prosaposinamultifaceted pages 11-13): Xin Li and Liang Guo. Prosaposin: a multifaceted protein orchestrating biological processes and diseases. Cells, 14:1131, Jul 2025. URL: https://doi.org/10.3390/cells14151131, doi:10.3390/cells14151131. This article has 10 citations.

14. (tamargo2012theroleof pages 7-8): Rafael J. Tamargo, Arash Velayati, Ehud Goldin, and Ellen Sidransky. The role of saposin c in gaucher disease. Molecular genetics and metabolism, 106 3:257-63, Jul 2012. URL: https://doi.org/10.1016/j.ymgme.2012.04.024, doi:10.1016/j.ymgme.2012.04.024. This article has 208 citations and is from a peer-reviewed journal.

15. (bhat2023combinedsaposindeficiency pages 1-2): Vivek Bhat, R.W. Thergaonkar, Manisha Thakur, and T. Rajkamal. Combined saposin deficiency: a rare occurrence. Medical Journal Armed Forces India, 79:238-240, Mar 2023. URL: https://doi.org/10.1016/j.mjafi.2021.01.024, doi:10.1016/j.mjafi.2021.01.024. This article has 3 citations.

Artifacts

• Edison artifact artifact-00
• Edison artifact artifact-01