GALNS removes 6-sulfate groups during lysosomal degradation of chondroitin and keratan glycans. One molecular activity, GO:0043890, covers both natural sugar classes. The current review contains 15 source annotations and one separately identified inherited proposal for keratan sulfate proteoglycan catabolism. See the review for all judgments and reference assessments, and the source archive for literal contexts, history and source locators.
PMID:22940367 directly measures purified human GALNS on synthetic 4-MU-sulfate and 4-MU-Gal6S. The latter assay couples desulfation to beta-galactosidase reporter release and includes omission controls. Synthetic aryl-sulfate turnover supports the arylsulfatase IBA as a real, non-core catalytic capability; it does not establish a physiological aryl substrate. The authors explicitly describe substantial substrate-recognition promiscuity; the non-core arylsulfatase judgment retains that measured catalytic capability. The formylglycine/calcium active site and homodimer are structural findings. The GalNAc product pose is nonproductive, so it is not described as a productive sulfated-substrate pose.
PMID:820716 assays crude human kidney extracts on chondroitin-6-sulfate oligosaccharides and corrects a separate small arylsulfatase B contribution. It does not establish GALNS 4-sulfatase activity or intact-polymer cleavage. Subtracting ARSB contamination also does not prove that GALNS can never hydrolyze a 4-sulfated substrate. The 4S and 6S terms name different positional chemistries. A lateral correction is possible when an actual mapping error is established; non-descendance is not itself a reason to prohibit MODIFY. PMID:15962010 actually assays GALNS cDNA activity and SUMF1 enhancement; the detailed supplementary GALNS substrate protocol remains unread. PMID:8325655 remains abstract-only after bounded original-source checks, leaving its specific 4-sulfatase assertion UNDECIDED.
The author-uploaded original of PMID:18285341, DOI 10.1074/jbc.M707967200, provides the critical per-gene distinction. The cached abstract collectively links ASB-or-GALNS manipulation to CS and C4S outcomes. The selected GALNS-specific Results, Table 2 and Figure 2 caption report total CS changes but no C4S increase after silencing and no C4S change after overexpression. Table 1 separately records enzyme activities, including the effective GALNS manipulation and essentially unchanged ASB activity. The narrower Results govern the current interpretation, and the apparent abstract-versus-Results discrepancy is explicit. These cellular measurements do not demonstrate universal absence of a GALNS 4S side reaction.
The original selected Methods identify human GALNS expression and siRNA in MCF-7 cells. The explicit 4-MU-sulfate recipe is for ASB; detailed GALNS assay chemistry refers to earlier work. The normal cache remains abstract-only. Original text and the Figure 2 caption were inspected externally, but figure images and the prior assay recipe were not. Unchanged keratan abundance in this cell assay is not affirmative keratan-degradation evidence.
PMID:30760748 directly colocalizes GALNS and LAMP1 in primary human airway fibroblasts. Both lysosome rows are accepted alongside the more precise lysosomal-lumen statements. Reactome R-HSA-1630304 describes the normal GALNS keratan-desulfation reaction. R-HSA-2263490 describes failure of defective variants and links that normal reaction; mutant failure is not mistaken for absence of wild-type activity.
The inherited keratan process proposal is retained as TAS with original reference R-HSA-1630304. Its older EXP/PMID:22940367 combination is preserved in the historical record, because the 2012 experiments use synthetic substrates rather than directly measuring natural keratan breakdown. GALNS itself performs the desulfation step. Same-role GLB1/GNS annotations and typed ancestry support the process scope without adding a redundant ancestor.
Official input and output sets for neutrophil event R-HSA-6798751 name OxA-GALNS. They support contextual azurophil-lumen/extracellular occurrence, not GALNS execution of exocytosis. Individual component-page requests returned 404, which is distinguished from the successful named-set membership.
The authentic Supplemental Table 2 of PMID:23533145, sheet SI Table 2, row 319, identifies P34059/GALNS with 7/7/10/9 unique peptides in duplicate pooled cancer/non-cancer preparations. Its 211,902-byte workbook hash and exact column names are in the source archive. This supports positive fraction-associated occurrence. Peptide depth does not distinguish vesicle incorporation, surface association or co-isolation of a secreted lysosomal enzyme. The current decision restores the October 10 over-annotation treatment for specific exosome location because the recovered target table does not resolve that separation problem. Positive detection remains documented; no absence from extracellular vesicles is asserted. The original row and older journal decisions are preserved.
The current official record and direct FASTA specify one canonical 522-residue product, with a signal peptide at 1-26 and mature-chain annotation at 27-522. No alternative products are declared. Processing, purification tags and recombinant constructs do not create natural isoforms.
In the actual PTHR42693 tree, the exact target sequence at PTN002533499 descends from the arylsulfatase IBD node PTN000819263. The original incoming five-donor record and later six-donor PAINT assertion remain distinct; the latter adds P15289. This is dated provenance, not an error inferred from donor count. No negative assertion interrupts the target path.
The 15 original contexts, one part_of atom, one canonical sequence and all 29 inherited quotation associations remain recoverable. Nine short excerpts now anchor the current review. All original quotation associations remain recoverable at their historical locators, and eight inherited finding statements are restored in the reference objects with claim-specific assessments. Current excerpts are not repeated in this guide or the new journal section. The old review is linked at its immutable Git revision; all prior journal bytes remain as a prefix. Reference assessments distinguish normal-cache availability from selected external-original reading.
Genuine native acquisition reconciled all 15 original contexts with the actual 16-column export and private native seed. The separate TAS keratan proposal remains identifiable as an authored NEW. At initial publication, all 36 sources and four active quotations were checked against their actual bytes: 18 main sources were reused unchanged and 18 missing sources were acquired. The original part_of atom is restored on native row 11. The inherited review, 29 quotation associations, journal and four prior history records remain preserved. Default and strict GOA validation, history, status and private rendering passed with zero advisories. Computed COMPLETE retains the one UNDECIDED scientific judgment.
The normal GALNS reaction now anchors the retained TAS keratan-process proposal directly; the keratan degradation pathway supplies the proteoglycan-level context. The Morquio A record states normal 6-sulfate chemistry separately from mutant deficiency. These records are manually assessed, not treated as new experiments. The repository glycan-degradation module is concordant, but because it cites this gene review it is not independent support for the annotation.
The additional PMID:1522213(https://pubmed.ncbi.nlm.nih.gov/1522213/) abstract concerns Morquio mutations and transfection assays. Selected PMID:24726177(https://pubmed.ncbi.nlm.nih.gov/24726177/) Methods concern diagnostic fibroblast/leukocyte assays. Neither inspected source supplies a matched purified-GALNS 4S-versus-6S comparison. Distinct enzyme labels, normal 6S activity and a corrected ARSB contribution leave the specific 4S TAS assertion unresolved. The original 8325655 no-4S-assay statement is restored with a DISPUTED assessment: the absence claim was stronger than the available access, not experimentally disproved.
The current 18285341 excerpt explicitly names both ASB and GALNS and supports the broad chondroitin conclusion only; its claim-specific limitations are reconciled above against the original per-gene Results. All eight restored finding statements retain their scope notes. The UniProt finding's record_section was derived from its exact published source. The 22940367 anchors separately expose normal 6S specificity, the authors' promiscuity interpretation and the coupled-assay desulfation step; their total is 23 words and the core cites the source without repeating an excerpt. Earlier journal and acquisition statements retain their historical meanings.