ARSB is human N-acetylgalactosamine-4-sulfatase (P15848; HGNC:714; Gene:411), also called arylsulfatase B, ASB or G4S. Its principal work is removal of GalNAc 4-sulfate during lysosomal chondroitin sulfate and dermatan sulfate degradation. The catalytic calcium and Cys91-derived formylglycine chemistry belong to that same enzymatic function. This review distinguishes physiological glycan substrates from aromatic substrates used to measure arylsulfatase activity.
The complete original abstract of PMID:2303452(https://pubmed.ncbi.nlm.nih.gov/2303452/) describes expression of human ASB in baby-hamster kidney cells, pulse-chase processing, dense-lysosome localization and mannose-6-phosphate-receptor-dependent delivery. This is a human protein expressed in a hamster cell system. The substrate is transported; the abstract does not establish a transport activity of ARSB itself. Complete original Methods/Results were not recovered. Precise signal-cleavage boundaries are omitted from the synthesis because the older abstract and current model use different chain boundaries.
PMID:18285341(https://pubmed.ncbi.nlm.nih.gov/18285341/) uses human MCF7 cells with ASB/GALNS silencing and overexpression. The complete cached abstract reports corresponding changes in C4S/CS pools and proteoglycan expression. Other sulfated GAGs, including DS, did not change in that experimental setting; this is not evidence against the independently established DS reaction. The study is not described here as a newly inspected purified-enzyme substrate assay: its full Methods remain unread. PMID:19306108(https://pubmed.ncbi.nlm.nih.gov/19306108/) explicitly identifies the 4-sulfate-removing activity and describes human NCM460/T84 colonic-cell perturbations. Its complete abstract supports the existing migration-related observations but not an ARSB RhoA catalytic activity.
The identity and complete primary abstract of PMID:9032078(https://pubmed.ncbi.nlm.nih.gov/9032078/), DOI 10.1016/S0969-2126(97)00185-8, were independently checked against the original structural citation and RCSB 1FSU. The human P15848 structure contains a calcium ion at the active site and identifies the modified catalytic residue. The recombinant expression system is distinguished from the organism of the protein. A full crystallographic Methods read is not claimed. The normal abstract-only publication record has now been recovered and checked against this primary identity. The review attaches its calcium statement with the full-text-unavailable flag; no source text has been manufactured.
The original donor references were traced through the official MGI comparative Arsb annotations and its older orthology display. Rat UniProt P50430 and the source Ensembl identifier are preserved. The following six already-existing normal caches were read and left unchanged.
The positive contextual observations can support retaining existing non-core response or migration annotations. They do not warrant new hormone, mercury, growth-factor or RhoA molecular functions. The inaccessible full donor experiment remains explicit for the autophagy and pH assertions. Cell-surface assertions likewise remain unresolved because their precise source localization experiments were not inspected.
The original cached summaries remain immutable. Their actual participant graphs were examined separately.
R-HSA-1606789 models human ARSB-catalyzed DS desulfation, with DS-chain input, desulfated-chain output and sulfate. The catalyst is ARSB:Ca2+, R-HSA-1606792, containing calcium and OxA-ARSB, R-HSA-1606837, explicitly linked to human P15848/HGNC:714 in lysosomal lumen. R-HSA-1793207 places the same catalyst in the CS pathway. Its C4S/C6S summary is broader than established 4-sulfatase specificity; the review does not adopt C6S hydrolysis from that wording.
The mutant sources R-HSA-2282889 and R-HSA-9036065 provide the original lysosomal-lumen annotations. Their full nested mutant sets were not independently reconstructed. The latter's DS title and cached CS wording are inconsistent. These limitations do not refute the compartment independently established for active human ARSB, and neither mutant summary is used to broaden normal substrate specificity.
SUMF1 maturation, R-HSA-1614362, has ARSB in its ER-lumen substrate set R-HSA-1614312 through entity R-HSA-1614331. SUMF1 performs the oxidation; ARSB is its substrate. ER transit is a non-core location, not an ARSB oxidoreductase function.
Azurophil-granule release, R-HSA-6798751, contains ARSB in input set R-HSA-6798742 and extracellular output set R-HSA-6806184, including ARSB granule entity R-HSA-6798774. Ficolin-rich granule release, R-HSA-6800434, similarly contains ARSB in input R-HSA-6800431 and output R-HSA-6806481, with granule entity R-HSA-6800887. These are model-supported cargo locations; being released does not establish that ARSB executes degranulation.
PMID:1718978(https://pubmed.ncbi.nlm.nih.gov/1718978/) identifies the human G137V disease variant. The complete cached abstract and selected original Methods/Results, including precursor-stability and trafficking experiments, were read. The original text distinguishes patient fibroblasts and expression of human constructs in mouse LTK cells. A complete source adjudication for lysosome organization was not achieved; the term is left undecided, without claiming that the paper lacks every relevant experiment. GO:0007040 concerns organelle assembly, arrangement and disassembly. GO:0007041 concerns directed lysosomal transport; M6P-dependent transport of ARSB cargo alone does not establish performance of that process by ARSB.
PMID:23533145(https://pubmed.ncbi.nlm.nih.gov/23533145/) concerns human expressed-prostatic-secretion urine exosomes. The pooled sampling, isolation and proteomics workflow were inspected, but the exact ARSB supplementary protein/peptide row remains unread. The exosome annotation stays undecided. Omission from article prose is neither absence nor contamination evidence.
The PAINT source of the broad sulfatase IBA is PTN002233267. Tree/MSA/IBD placement remains unresolved. Target-specific human chemistry nevertheless supports the inherited function. Neither donor count nor the target's presence among descendant evidence is treated as a flaw.
The pre-existing author-added DS catabolism proposal is supported by the actual human ARSB catalyst in R-HSA-1606789. The enzyme performs the sulfate-removal step; it is not the consumed glycan substrate. Comparator IDUA has a human GO:0030209 IDA assertion linked to PMID:24036510, while human IDS reaction R-HSA-1793182 explicitly links another catalytic DS-degradation step to this process. The local GO-CAM index has no ARSB/P15848 match; that is not a claim that no model exists elsewhere.
The indexed GO:0030209 and GO:0030207 pages have proteoglycan-catabolism/metabolism parents. Current comparative displays use shorter GAG labels. No unverified formal GO:0006027 ancestor relation is asserted. The prior broad author-added GAG-catabolism proposal is omitted because the named CS/DS processes already describe the established work; no original GOA row is deleted.
The actual GO:0003943 definition and parent identify GalNAc-4-sulfatase chemistry and sulfuric ester hydrolase parentage. GO:0004065 describes aryl-sulfate hydrolysis and has the same parent; it is not the more general version of GO:0003943. GO:0005509 refines metal-ion binding to calcium binding. GO:0009268 concerns cell/organism changes responding to pH; it does not require direct sensing by ARSB.
The old main review had 35 original GOA rows and two author-added NEW rows. Deterministic temporary backfill restored 35 qualifiers and 16 WITH/FROM lists without adding annotations or changing old review judgments. All 35 original source objects are retained, including the restored qualifiers and WITH/FROM lists. The pre-existing ARSB-ai-review-CORRECTED.yaml is a historical partial core-only document and is preserved unchanged. The three provider reports, UniProt, GOA and existing normal caches are immutable inputs. Provider reports guide searches but do not verify their own citations; unsupported homodimer, sphingolipid, MLD and 6-sulfatase claims are not adopted.
This is a manual literature and annotation audit. Scientific consultation, source-cache closure, validation, rendering and append-only history are tracked separately from these evidence notes.
The lysosomal-transport TAS judgment is revised to MARK_AS_OVER_ANNOTATED. The cited abstract explicitly identifies receptor-dependent delivery of ARSB cargo; the process role belongs to the trafficking machinery. This does not refute the accepted lysosomal location or assert that every possible trafficking influence of ARSB has been excluded.
The reviewer described the pH cache's repeated abstract as the entire paper. The primary PMC record instead lists five scanned pages, 603–607. The cache remains correctly marked abstract-only. Attempts to access the linked PDF and page images did not yield readable full text. The pH and autophagy donor assertions therefore remain UNDECIDED: their abstracts do not establish participation, and incomplete access does not establish that the unseen experiments refute it. The obsolete A-to-B identity proposal in PMID8037 is rejected separately from the unresolved process assertion.
The nutrient and methylmercury rows retain their existing non-core decisions with the original rat/cell/age and dose/time restrictions. These are contextual activity-response interpretations, not claims of nutrient sensing, mercury detoxification, an exclusive ARSB response, or new molecular functions. Simultaneous effects on other hydrolases do not by themselves negate the measured Arsb activity change. These broad response annotations remain open to source-specific curation reassessment.
Propagation comments now distinguish the named rat protein, its accompanying Ensembl identifier, and the location/family mapping source. The combined GO0008484 row records the rat sources and explicitly unresolved InterPro-rule replay separately. Notes quoted for Reactome participant inspections are author-derived observations with linked entity IDs; they are not independent corroborating references. Rat aromatic-substrate evidence is identified as comparative context alongside the direct human-expression assay. Repeated original-reference identifiers are omitted from additional_reference_ids. No source cache, GOA source object, quote, availability flag, isoform, core function or proposed process is changed.