# GLB1

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Protein

GLB1 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3THC, 3THD, 3WEZ, 3WF0, 3WF1, 3WF2, 3WF3, 3WF4 Identifiers Aliases GLB1, EBP, ELNR1, MPS4B, galactosidase beta 1 External IDs OMIM: 611458; MGI: 88151; HomoloGene: 47922; GeneCards: GLB1; OMA:GLB1 - orthologs Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p22.3 Start 32,996,609 bp[1] End 33,097,202 bp[1] Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9 F3|9 64.4 cM Start 114,230,144 bp[2] End 114,303,966 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte stromal cell of endometrium secondary oocyte islet of Langerhans corpus epididymis granulocyte rectum epithelium of colon gallbladder tibia Top expressed in right kidney human kidney proximal tubule migratory enteric neural crest cell seminal vesicula epithelium of small intestine blastocyst stroma of bone marrow calvaria yolk sac More reference expression data BioGPS More reference expression data Gene ontology Molecular function protein binding hydrolase activity, hydrolyzing O-glycosyl compounds galactoside binding hydrolase activity, acting on glycosyl bonds hydrolase activity exo-alpha-sialidase activity beta-galactosidase activity protein homodimerization activity Cellular component perinuclear region of cytoplasm Golgi apparatus lysosome lysosomal lumen intracellular membrane-bounded organelle extracellular exosome cytoplasm vacuole extracellular region extracellular space azurophil granule lumen ficolin-1-rich granule lumen Biological process galactose catabolic process glycosphingolipid metabolic process cellular carbohydrate metabolic process keratan sulfate catabolic process metabolism glycosaminoglycan catabolic process neutrophil degranulation response to cortisone response to Thyroglobulin triiodothyronine carbohydrate metabolic process Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 2720 12091 Ensembl ENSG00000170266 ENSMUSG00000045594 UniProt P16278 P23780 RefSeq (mRNA) NM_001135602 NM_000404 NM_001079811 NM_001317040 NM_001393580 NM_009752 RefSeq (protein) NP_000395 NP_001073279 NP_001129074 NP_001303969 NP_033882 Location (UCSC) Chr 3: 33 – 33.1 Mb Chr 9: 114.23 – 114.3 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Galactosidase, beta 1**, also known as **GLB1**, is a [protein](/source/Protein) which in humans is encoded by the *GLB1* [gene](/source/Gene).[5][6]

The GLB1 protein is a [beta-galactosidase](/source/Beta-galactosidase) that cleaves the terminal beta-[galactose](/source/Galactose) from [ganglioside](/source/Ganglioside) substrates and other glycoconjugates.[7] The *GLB1* gene also encodes an [elastin](/source/Elastin) binding protein.[8]

In [corn](/source/Maize) (*[Zea mays](/source/Zea_mays)*), *Glb1* is a gene coding for the storage protein [globulin](/source/Globulin).

## Clinical significance

[GM1-gangliosidosis](/source/GM1_gangliosidoses) is a [lysosomal storage disease](/source/Lysosomal_storage_disease) that can be caused by a deficiency of β-galactosidase (GLB1). Some cases of [Morquio syndrome B](/source/Morquio_syndrome) have been shown to be due to GLP1 mutations that cause patients to have abnormal [elastic fibers](/source/Elastic_fiber).[9]

## Elastin receptor

The [RNA](/source/RNA) [transcript](/source/Transcription_(genetics)) of the GLB1 gene is [alternatively spliced](/source/Alternative_splicing) and produces 2 mRNAs. The 2.5-[kilobase](/source/Base_pair#Length_measurements) transcript [encodes](/source/Translation_(genetics)) the beta-galactosidase enzyme of 677 amino acids. The alternative 2.0-[kb](/source/Base_pair#Length_measurements) mRNA encodes a beta-galactosidase-related protein (S-Gal) that is only 546 amino acids long and that has no enzymatic activity. The S-Gal protein does bind [elastin](/source/Elastin) and fragments of elastin that are generated by [proteolysis](/source/Proteolysis).[10]

The S-Gal protein is a [peripheral membrane protein](/source/Peripheral_membrane_protein) that functions as part of an elastin [receptor](/source/Receptor_(biochemistry)) complex on the surface of cells.[11] The elastin receptor complex includes S-Gal, [neuraminidase](/source/NEU1) and [Cathepsin A](/source/Cathepsin_A). When elastin-derived [peptides](/source/Peptide) bind to the S-Gal protein then the associated neuraminidase [enzyme](/source/Enzyme) activity is activated and responding cells can have altered [signal transduction](/source/Signal_transduction) involving [extracellular signal-regulated kinases](/source/Extracellular_signal-regulated_kinases) and regulated [matrix metallopeptidase](/source/MMP1) production. Elastin-derived peptides are [chemotactic](/source/Chemotaxis) for some [cell](/source/Cell_(biology)) types[12] and can alter [cell cycle](/source/Cell_cycle) progression.[13] The ability of the GLB1-derived elastin binding protein and the elastin receptor complex to influence cell proliferation appears to be indirect and involve removal of [sialic acid](/source/Sialic_acid) from extracellular and cell surface proteins such as [growth factor receptors](/source/Growth_factor_receptor).

The S-Gal protein functions during the normal assembly of [elastin](/source/Elastin) into [extracellular](/source/Extracellular_matrix) [elastic fibers](/source/Elastic_fiber). Elastin is initially present as newly synthesized [tropoelastin](/source/Tropoelastin) which can be found in association with S-Gal. The enzymatic activity of neuraminidase in the elastin receptor complex is involved in the release of tropoelastin molecules from the S-Gal [chaperone](/source/Chaperone_(protein)).[14] [Cathepsin A](/source/Cathepsin_A) is also required for normal elastin biosynthesis.[15]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000170266](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000170266) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000045594](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000045594) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=2720). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=12091). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid110522_5-0)** Shows TB, Scrafford-Wolff L, Brown JA, Meisler M (1978). "Assignment of a beta-galactosidase gene (beta GALA) to chromosome 3 in man". *Cytogenetics and Cell Genetics*. **22** (1–6): 219–22. [doi](/source/Doi_(identifier)):[10.1159/000130940](https://doi.org/10.1159%2F000130940). [PMID](/source/PMID_(identifier)) [110522](https://pubmed.ncbi.nlm.nih.gov/110522).

1. **[^](#cite_ref-pmid3143362_6-0)** Oshima A, Tsuji A, Nagao Y, Sakuraba H, Suzuki Y (Nov 1988). "Cloning, sequencing, and expression of cDNA for human beta-galactosidase". *Biochemical and Biophysical Research Communications*. **157** (1): 238–44. [doi](/source/Doi_(identifier)):[10.1016/S0006-291X(88)80038-X](https://doi.org/10.1016%2FS0006-291X%2888%2980038-X). [PMID](/source/PMID_(identifier)) [3143362](https://pubmed.ncbi.nlm.nih.gov/3143362).

1. **[^](#cite_ref-pmid1907800_7-0)** Yoshida K, Oshima A, Shimmoto M, Fukuhara Y, Sakuraba H, Yanagisawa N, Suzuki Y (Aug 1991). ["Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683306). *American Journal of Human Genetics*. **49** (2): 435–42. [PMC](/source/PMC_(identifier)) [1683306](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683306). [PMID](/source/PMID_(identifier)) [1907800](https://pubmed.ncbi.nlm.nih.gov/1907800).

1. **[^](#cite_ref-pmid15714521_8-0)** Caciotti A, Donati MA, Boneh A, d'Azzo A, Federico A, Parini R, Antuzzi D, Bardelli T, Nosi D, Kimonis V, Zammarchi E, Morrone A (Mar 2005). "Role of beta-galactosidase and elastin binding protein in lysosomal and nonlysosomal complexes of patients with GM1-gangliosidosis". *Human Mutation*. **25** (3): 285–92. [doi](/source/Doi_(identifier)):[10.1002/humu.20147](https://doi.org/10.1002%2Fhumu.20147). [hdl](/source/Hdl_(identifier)):[2158/312510](https://hdl.handle.net/2158%2F312510). [PMID](/source/PMID_(identifier)) [15714521](https://pubmed.ncbi.nlm.nih.gov/15714521). [S2CID](/source/S2CID_(identifier)) [36584440](https://api.semanticscholar.org/CorpusID:36584440).

1. **[^](#cite_ref-pmid10841810_9-0)** Hinek A, Zhang S, Smith AC, Callahan JW (Jul 2000). ["Impaired elastic-fiber assembly by fibroblasts from patients with either Morquio B disease or infantile GM1-gangliosidosis is linked to deficiency in the 67-kD spliced variant of beta-galactosidase"](https://web.archive.org/web/20050118201219/http://www.jbc.org/cgi/content/full/273/11/6319). *American Journal of Human Genetics*. **67** (1): 23–36. [doi](/source/Doi_(identifier)):[10.1086/302968](https://doi.org/10.1086%2F302968). [PMC](/source/PMC_(identifier)) [1287082](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1287082). [PMID](/source/PMID_(identifier)) [10841810](https://pubmed.ncbi.nlm.nih.gov/10841810). Archived from [the original](http://www.jbc.org/cgi/content/full/273/11/6319) on 2005-01-18. Retrieved 2009-05-31.

1. **[^](#cite_ref-pmid9497360_10-0)** Privitera S, Prody CA, Callahan JW, Hinek A (Mar 1998). ["The 67-kDa enzymatically inactive alternatively spliced variant of beta-galactosidase is identical to the elastin/laminin-binding protein"](https://web.archive.org/web/20050118201219/http://www.jbc.org/cgi/content/full/273/11/6319). *The Journal of Biological Chemistry*. **273** (11): 6319–26. [doi](/source/Doi_(identifier)):[10.1074/jbc.273.11.6319](https://doi.org/10.1074%2Fjbc.273.11.6319). [PMID](/source/PMID_(identifier)) [9497360](https://pubmed.ncbi.nlm.nih.gov/9497360). Archived from [the original](http://www.jbc.org/cgi/content/full/273/11/6319) on 2005-01-18. Retrieved 2009-05-31.

1. **[^](#cite_ref-pmid17327233_11-0)** Duca L, Blanchevoye C, Cantarelli B, Ghoneim C, Dedieu S, Delacoux F, Hornebeck W, Hinek A, Martiny L, Debelle L (Apr 2007). ["The elastin receptor complex transduces signals through the catalytic activity of its Neu-1 subunit"](https://web.archive.org/web/20080922051001/http://www.jbc.org/cgi/content/full/282/17/12484). *The Journal of Biological Chemistry*. **282** (17): 12484–91. [doi](/source/Doi_(identifier)):[10.1074/jbc.M609505200](https://doi.org/10.1074%2Fjbc.M609505200). [PMID](/source/PMID_(identifier)) [17327233](https://pubmed.ncbi.nlm.nih.gov/17327233). Archived from [the original](http://www.jbc.org/cgi/content/full/282/17/12484) on 2008-09-22. Retrieved 2009-05-31.

1. **[^](#cite_ref-pmid18243041_12-0)** Adair-Kirk TL, Senior RM (December 2008). ["Fragments of extracellular matrix as mediators of inflammation"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2478752). *The International Journal of Biochemistry & Cell Biology*. **40** (6–7): 1101–10. [doi](/source/Doi_(identifier)):[10.1016/j.biocel.2007.12.005](https://doi.org/10.1016%2Fj.biocel.2007.12.005). [PMC](/source/PMC_(identifier)) [2478752](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2478752). [PMID](/source/PMID_(identifier)) [18243041](https://pubmed.ncbi.nlm.nih.gov/18243041).

1. **[^](#cite_ref-pmid18772331_13-0)** Hinek A, Bodnaruk TD, Bunda S, Wang Y, Liu K (Oct 2008). ["Neuraminidase-1, a subunit of the cell surface elastin receptor, desialylates and functionally inactivates adjacent receptors interacting with the mitogenic growth factors PDGF-BB and IGF-2"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2543072). *The American Journal of Pathology*. **173** (4): 1042–56. [doi](/source/Doi_(identifier)):[10.2353/ajpath.2008.071081](https://doi.org/10.2353%2Fajpath.2008.071081). [PMC](/source/PMC_(identifier)) [2543072](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2543072). [PMID](/source/PMID_(identifier)) [18772331](https://pubmed.ncbi.nlm.nih.gov/18772331).

1. **[^](#cite_ref-pmid16314420_14-0)** Hinek A, Pshezhetsky AV, von Itzstein M, Starcher B (Feb 2006). ["Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly"](https://web.archive.org/web/20080919153253/http://www.jbc.org/cgi/content/full/281/6/3698). *The Journal of Biological Chemistry*. **281** (6): 3698–710. [doi](/source/Doi_(identifier)):[10.1074/jbc.M508736200](https://doi.org/10.1074%2Fjbc.M508736200). [PMID](/source/PMID_(identifier)) [16314420](https://pubmed.ncbi.nlm.nih.gov/16314420). Archived from [the original](http://www.jbc.org/cgi/content/full/281/6/3698) on 2008-09-19. Retrieved 2009-05-31.

1. **[^](#cite_ref-pmid18391110_15-0)** Seyrantepe V, Hinek A, Peng J, Fedjaev M, Ernest S, Kadota Y, Canuel M, Itoh K, Morales CR, Lavoie J, Tremblay J, Pshezhetsky AV (Apr 2008). ["Enzymatic activity of lysosomal carboxypeptidase (cathepsin) A is required for proper elastic fiber formation and inactivation of endothelin-1"](https://web.archive.org/web/20080919153253/http://www.jbc.org/cgi/content/full/281/6/3698). *Circulation*. **117** (15): 1973–81. [doi](/source/Doi_(identifier)):[10.1161/CIRCULATIONAHA.107.733212](https://doi.org/10.1161%2FCIRCULATIONAHA.107.733212). [PMID](/source/PMID_(identifier)) [18391110](https://pubmed.ncbi.nlm.nih.gov/18391110). Archived from [the original](http://www.jbc.org/cgi/content/full/281/6/3698) on 2008-09-19. Retrieved 2009-05-31.

## Further reading

- Hinek A (1997). "Biological roles of the non-integrin elastin/laminin receptor". *Biological Chemistry*. **377** (7–8): 471–80. [doi](/source/Doi_(identifier)):[10.1515/bchm3.1996.377.7-8.411](https://doi.org/10.1515%2Fbchm3.1996.377.7-8.411). [PMID](/source/PMID_(identifier)) [8922281](https://pubmed.ncbi.nlm.nih.gov/8922281).

- Kaye EM, Shalish C, Livermore J, Taylor HA, Stevenson RE, Breakefield XO (Jun 1997). "beta-Galactosidase gene mutations in patients with slowly progressive GM1 gangliosidosis". *Journal of Child Neurology*. **12** (4): 242–7. [doi](/source/Doi_(identifier)):[10.1177/088307389701200404](https://doi.org/10.1177%2F088307389701200404). [PMID](/source/PMID_(identifier)) [9203065](https://pubmed.ncbi.nlm.nih.gov/9203065). [S2CID](/source/S2CID_(identifier)) [27281171](https://api.semanticscholar.org/CorpusID:27281171).

- Callahan JW (Oct 1999). ["Molecular basis of GM1 gangliosidosis and Morquio disease, type B. Structure-function studies of lysosomal beta-galactosidase and the non-lysosomal beta-galactosidase-like protein"](https://doi.org/10.1016%2FS0925-4439%2899%2900075-7). *Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease*. **1455** (2–3): 85–103. [doi](/source/Doi_(identifier)):[10.1016/S0925-4439(99)00075-7](https://doi.org/10.1016%2FS0925-4439%2899%2900075-7). [PMID](/source/PMID_(identifier)) [10571006](https://pubmed.ncbi.nlm.nih.gov/10571006).

- Shows TB, Scrafford-Wolff L, Brown JA, Meisler M (1979). "Assignment of a beta-galactosidase gene (beta GALA) to chromosome 3 in man". *Cytogenetics and Cell Genetics*. **22** (1–6): 219–22. [doi](/source/Doi_(identifier)):[10.1159/000130940](https://doi.org/10.1159%2F000130940). [PMID](/source/PMID_(identifier)) [110522](https://pubmed.ncbi.nlm.nih.gov/110522).

- Shows TB, Scrafford-Wolff LR, Brown JA, Meisler MH (Mar 1979). ["GM1-gangliosidosis: chromosome 3 assignment of the beta-galactosidase-A gene (beta GALA)"](https://deepblue.lib.umich.edu/bitstream/2027.42/45554/1/11188_2005_Article_BF01539157.pdf) (PDF). *Somatic Cell Genetics*. **5** (2): 147–58. [doi](/source/Doi_(identifier)):[10.1007/BF01539157](https://doi.org/10.1007%2FBF01539157). [hdl](/source/Hdl_(identifier)):[2027.42/45554](https://hdl.handle.net/2027.42%2F45554). [PMID](/source/PMID_(identifier)) [113895](https://pubmed.ncbi.nlm.nih.gov/113895). [S2CID](/source/S2CID_(identifier)) [21896411](https://api.semanticscholar.org/CorpusID:21896411).

- Yoshida K, Oshima A, Sakuraba H, Nakano T, Yanagisawa N, Inui K, Okada S, Uyama E, Namba R, Kondo K (Mar 1992). "GM1 gangliosidosis in adults: clinical and molecular analysis of 16 Japanese patients". *Annals of Neurology*. **31** (3): 328–32. [doi](/source/Doi_(identifier)):[10.1002/ana.410310316](https://doi.org/10.1002%2Fana.410310316). [PMID](/source/PMID_(identifier)) [1353343](https://pubmed.ncbi.nlm.nih.gov/1353343). [S2CID](/source/S2CID_(identifier)) [5103186](https://api.semanticscholar.org/CorpusID:5103186).

- Mosna G, Fattore S, Tubiello G, Brocca S, Trubia M, Gianazza E, Gatti R, Danesino C, Minelli A, Piantanida M (Nov 1992). "A homozygous missense arginine to histidine substitution at position 482 of the beta-galactosidase in an Italian infantile GM1-gangliosidosis patient". *Human Genetics*. **90** (3): 247–50. [doi](/source/Doi_(identifier)):[10.1007/bf00220071](https://doi.org/10.1007%2Fbf00220071). [PMID](/source/PMID_(identifier)) [1487238](https://pubmed.ncbi.nlm.nih.gov/1487238). [S2CID](/source/S2CID_(identifier)) [21873727](https://api.semanticscholar.org/CorpusID:21873727).

- Oshima A, Yoshida K, Ishizaki A, Shimmoto M, Fukuhara Y, Sakuraba H, Suzuki Y (May 1992). "GM1-gangliosidosis: tandem duplication within exon 3 of beta-galactosidase gene in an infantile patient". *Clinical Genetics*. **41** (5): 235–8. [doi](/source/Doi_(identifier)):[10.1111/j.1399-0004.1992.tb03672.x](https://doi.org/10.1111%2Fj.1399-0004.1992.tb03672.x). [PMID](/source/PMID_(identifier)) [1606711](https://pubmed.ncbi.nlm.nih.gov/1606711). [S2CID](/source/S2CID_(identifier)) [21921420](https://api.semanticscholar.org/CorpusID:21921420).

- Yoshida K, Oshima A, Shimmoto M, Fukuhara Y, Sakuraba H, Yanagisawa N, Suzuki Y (Aug 1991). ["Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683306). *American Journal of Human Genetics*. **49** (2): 435–42. [PMC](/source/PMC_(identifier)) [1683306](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683306). [PMID](/source/PMID_(identifier)) [1907800](https://pubmed.ncbi.nlm.nih.gov/1907800).

- Nishimoto J, Nanba E, Inui K, Okada S, Suzuki K (Sep 1991). ["GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683129). *American Journal of Human Genetics*. **49** (3): 566–74. [PMC](/source/PMC_(identifier)) [1683129](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683129). [PMID](/source/PMID_(identifier)) [1909089](https://pubmed.ncbi.nlm.nih.gov/1909089).

- Morreau H, Bonten E, Zhou XY, D'Azzo A (Sep 1991). "Organization of the gene encoding human lysosomal beta-galactosidase". *DNA and Cell Biology*. **10** (7): 495–504. [doi](/source/Doi_(identifier)):[10.1089/dna.1991.10.495](https://doi.org/10.1089%2Fdna.1991.10.495). [PMID](/source/PMID_(identifier)) [1909871](https://pubmed.ncbi.nlm.nih.gov/1909871).

- Oshima A, Yoshida K, Shimmoto M, Fukuhara Y, Sakuraba H, Suzuki Y (Nov 1991). ["Human beta-galactosidase gene mutations in morquio B disease"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683264). *American Journal of Human Genetics*. **49** (5): 1091–3. [PMC](/source/PMC_(identifier)) [1683264](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1683264). [PMID](/source/PMID_(identifier)) [1928092](https://pubmed.ncbi.nlm.nih.gov/1928092).

- Yamamoto Y, Hake CA, Martin BM, Kretz KA, Ahern-Rindell AJ, Naylor SL, Mudd M, O'Brien JS (Mar 1990). "Isolation, characterization, and mapping of a human acid beta-galactosidase cDNA". *DNA and Cell Biology*. **9** (2): 119–27. [doi](/source/Doi_(identifier)):[10.1089/dna.1990.9.119](https://doi.org/10.1089%2Fdna.1990.9.119). [PMID](/source/PMID_(identifier)) [2111707](https://pubmed.ncbi.nlm.nih.gov/2111707).

- Morreau H, Galjart NJ, Gillemans N, Willemsen R, van der Horst GT, d'Azzo A (Dec 1989). ["Alternative splicing of beta-galactosidase mRNA generates the classic lysosomal enzyme and a beta-galactosidase-related protein"](https://doi.org/10.1016%2FS0021-9258%2819%2947114-7). *The Journal of Biological Chemistry*. **264** (34): 20655–63. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(19)47114-7](https://doi.org/10.1016%2FS0021-9258%2819%2947114-7). [PMID](/source/PMID_(identifier)) [2511208](https://pubmed.ncbi.nlm.nih.gov/2511208).

- Hoogeveen AT, Reuser AJ, Kroos M, Galjaard H (May 1986). ["GM1-gangliosidosis. Defective recognition site on beta-galactosidase precursor"](https://doi.org/10.1016%2FS0021-9258%2817%2938439-9). *The Journal of Biological Chemistry*. **261** (13): 5702–4. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(17)38439-9](https://doi.org/10.1016%2FS0021-9258%2817%2938439-9). [PMID](/source/PMID_(identifier)) [3084469](https://pubmed.ncbi.nlm.nih.gov/3084469).

- Verheijen FW, Palmeri S, Galjaard H (Jan 1987). ["Purification and partial characterization of lysosomal neuraminidase from human placenta"](https://doi.org/10.1111%2Fj.1432-1033.1987.tb10542.x). *European Journal of Biochemistry*. **162** (1): 63–7. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1987.tb10542.x](https://doi.org/10.1111%2Fj.1432-1033.1987.tb10542.x). [PMID](/source/PMID_(identifier)) [3102233](https://pubmed.ncbi.nlm.nih.gov/3102233).

- Oshima A, Tsuji A, Nagao Y, Sakuraba H, Suzuki Y (Nov 1988). "Cloning, sequencing, and expression of cDNA for human beta-galactosidase". *Biochemical and Biophysical Research Communications*. **157** (1): 238–44. [doi](/source/Doi_(identifier)):[10.1016/S0006-291X(88)80038-X](https://doi.org/10.1016%2FS0006-291X%2888%2980038-X). [PMID](/source/PMID_(identifier)) [3143362](https://pubmed.ncbi.nlm.nih.gov/3143362).

- Sips HJ, de Wit-Verbeek HA, de Wit J, Westerveld A, Galjaard H (1985). "The chromosomal localization of human beta-galactosidase revisited: a locus for beta-galactosidase on human chromosome 3 and for its protective protein on human chromosome 22". *Human Genetics*. **69** (4): 340–4. [doi](/source/Doi_(identifier)):[10.1007/BF00291653](https://doi.org/10.1007%2FBF00291653). [PMID](/source/PMID_(identifier)) [3921454](https://pubmed.ncbi.nlm.nih.gov/3921454). [S2CID](/source/S2CID_(identifier)) [26594537](https://api.semanticscholar.org/CorpusID:26594537).

- Verheijen FW, Palmeri S, Hoogeveen AT, Galjaard H (Jun 1985). ["Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein"](https://doi.org/10.1111%2Fj.1432-1033.1985.tb08928.x). *European Journal of Biochemistry*. **149** (2): 315–21. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1985.tb08928.x](https://doi.org/10.1111%2Fj.1432-1033.1985.tb08928.x). [PMID](/source/PMID_(identifier)) [3922758](https://pubmed.ncbi.nlm.nih.gov/3922758).

- Goldman JE, Katz D, Rapin I, Purpura DP, Suzuki K (May 1981). "Chronic GM1 gangliosidosis presenting as dystonia: I. Clinical and pathological features". *Annals of Neurology*. **9** (5): 465–75. [doi](/source/Doi_(identifier)):[10.1002/ana.410090509](https://doi.org/10.1002%2Fana.410090509). [PMID](/source/PMID_(identifier)) [6791574](https://pubmed.ncbi.nlm.nih.gov/6791574). [S2CID](/source/S2CID_(identifier)) [26073976](https://api.semanticscholar.org/CorpusID:26073976).

v t e Metabolism: carbohydrate metabolism proteoglycan enzymes glycosaminoglycan anabolism L-xylulose reductase L-gulonolactone oxidase UDP-glucuronate 5'-epimerase Xylosyltransferase Sulfotransferase Heparan sulfate EXT1 EXT2 Chondroitin sulfate PAPSS1 PAPSS2 glycosaminoglycan catabolism Hunter, Hurler Iduronate-2-sulfatase Iduronidase Sanfilippo, Sly Heparan sulfamidase N-acetyltransferase Alpha-N-acetylglucosaminidase Glucuronidase N-acetylglucosamine-6-sulfatase Morquio/Maroteaux-Lamy Arylsulfatase B Galactosamine-6 sulfatase Beta-galactosidase (GLB1)

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Adapted from the Wikipedia article [GLB1](https://en.wikipedia.org/wiki/GLB1) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/GLB1?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.