HYAL1

Official Full Name

hyaluronidase 1

Organism

Homo sapiens

Gene ID

3373

Background

This gene encodes a lysosomal hyaluronidase. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation. This enzyme is active at an acidic pH and is the major hyaluronidase in plasma. Mutations in this gene are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency. The gene is one of several related genes in a region of chromosome 3p21.3 associated with tumor suppression. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Synonyms

MPS9; NAT6; LUCA1; HYAL-1

Cat.No.	Product Name	Price
CSC-DC007364	Panoply™ Human HYAL1 Knockdown Stable Cell Line	Inquiry
CSC-DC010140	Panoply™ Human NAT6 Knockdown Stable Cell Line	Inquiry
CSC-DC014957	Panoply™ Human SPAM1 Knockdown Stable Cell Line	Inquiry
CSC-SC007364	Panoply™ Human HYAL1 Over-expressing Stable Cell Line	Inquiry
CSC-SC010140	Panoply™ Human NAT6 Over-expressing Stable Cell Line	Inquiry
CSC-SC014957	Panoply™ Human SPAM1 Over-expressing Stable Cell Line	Inquiry

Cat.No.	Product Name	Price
AD07840Z	Human HYAL1 adenoviral particles	Inquiry
AD10542Z	Human NAT6 adenoviral particles	Inquiry
AD15346Z	Human SPAM1 adenoviral particles	Inquiry
LV15101L	human HYAL1 (NM_153285) lentivirus particles	Inquiry
LV15102L	human HYAL1 (NM_033159) lentivirus particles	Inquiry
LV15103L	human HYAL1 (NM_153282) lentivirus particles	Inquiry
LV15104L	human HYAL1 (NM_153283) lentivirus particles	Inquiry
LV19137L	human NAT6 (NM_001200018) lentivirus particles	Inquiry
LV19138L	human NAT6 (NM_012191) lentivirus particles	Inquiry
LV26401L	human SPAM1 (NM_153189) lentivirus particles	Inquiry
LV26402L	human SPAM1 (NM_003117) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHH136847	shRNA set against Mouse Hyal1(NM_008317.4)	Inquiry
SHH316153	shRNA set against Mouse HYAL1 (NM_008317.4)	Inquiry
SHH136811	shRNA set against Rat Hyal1(NM_207616.1)	Inquiry
SHH136829	shRNA set against Human HYAL1(NM_153281.1)	Inquiry
SHH316157	shRNA set against Rat HYAL1 (NM_207616.1)	Inquiry
SHH349516	shRNA set against Human NAT6 (NM_012191.3)	Inquiry
SHH349520	shRNA set against Mouse NAT6 (NM_019750.3)	Inquiry
SHH415912	shRNA set against Human SPAM1 (NM_003117.4)	Inquiry
SHH415916	shRNA set against Mouse SPAM1 (NM_009241.2)	Inquiry
SHH415920	shRNA set against Rat SPAM1 (NM_053967.2)	Inquiry
SHL025984	shRNA set against Mouse Spam1(NM_001079875.1)	Inquiry
SHL026038	shRNA set against Mouse Spam1(NM_009241.2)	Inquiry
SHW011042	shRNA set against Danio rerio SPAM1 (NM_001080685)	Inquiry

Cat.No.	Product Name	Price
MiUTR3H-08946	NAT6 miRNA 3'UTR clone	Inquiry
CDFG010069	Human HYAL1 cDNA Clone(NM_153281.1)	Inquiry
CDFH018415	Human SPAM1 cDNA Clone(NM_001174044.1)	Inquiry
CDFH018416	Human SPAM1 cDNA Clone(NM_001174045.1)	Inquiry
CDFH018417	Human SPAM1 cDNA Clone(NM_001174046.1)	Inquiry
CDFL012907	Mouse Spam1 cDNA Clone(NM_009241.2)	Inquiry
CDFR015365	Rat Hyal1 cDNA Clone(NM_207616.1)	Inquiry
MiUTR1H-04764	HYAL1 miRNA 3'UTR clone	Inquiry
MiUTR3H-08944	HYAL1 miRNA 3'UTR clone	Inquiry
MiUTR1M-05862	HYAL1 miRNA 3'UTR clone	Inquiry
CDCH391380	Human NAT6 ORF clone(NM_012191.3)	Inquiry
MiUTR1M-11127	SPAM1 miRNA 3'UTR clone	Inquiry
MiUTR1M-11128	SPAM1 miRNA 3'UTR clone	Inquiry
CDCB195502	Rabbit SPAM1 ORF clone (XM_008258249.1)	Inquiry
MiUTR1R-02556	HYAL1 miRNA 3'UTR clone	Inquiry
MiUTR3H-08941	HYAL1 miRNA 3'UTR clone	Inquiry
MiUTR3H-08943	HYAL1 miRNA 3'UTR clone	Inquiry
MiUTR1M-07511	NAT6 miRNA 3'UTR clone	Inquiry
CDCS409050	Human SPAM1 ORF Clone (BC026163)	Inquiry
CDCR382441	Rat Hyal1 ORF Clone(NM_207616.1)	Inquiry
CDCR380676	Rat Spam1 ORF Clone(NM_053967.2)	Inquiry
CDCR356888	Human SPAM1 ORF Clone(NM_001174046.1)	Inquiry
CDCR356887	Human SPAM1 ORF Clone(NM_001174045.1)	Inquiry
CDCR356884	Human SPAM1 ORF Clone(NM_001174044.1)	Inquiry
CDCR320607	Human HYAL1 ORF Clone(NM_153285.2)	Inquiry
CDCR320605	Human HYAL1 ORF Clone(NM_153283.2)	Inquiry
CDCR320601	Human HYAL1 ORF Clone(NM_153281.1)	Inquiry
CDCR246829	Mouse Spam1 ORF Clone(NM_009241.2)	Inquiry
CDCH391381	Mouse NAT6 ORF clone(NM_019750.3)	Inquiry
CDCH386416	Mouse HYAL1 ORF clone(NM_008317.4)	Inquiry
CDCH084908	Mouse Spam1 ORF clone (NM_001079875.1)	Inquiry
CDCB193806	Rabbit HYAL1 ORF clone (XM_002713360.2)	Inquiry
CDCB193599	Rabbit NAT6 ORF clone (XM_008260690.1)	Inquiry
CDCB172517	Danio rerio SPAM1 ORF Clone (NM_001080685)	Inquiry
CDCS413161	Human HYAL1 ORF Clone (BC035695)	Inquiry
CDCB159894	Human HYAL1 ORF clone (BC035695)	Inquiry

Detailed Information

Recent Research Progress

HYAL1, a hyaluronidase able to degrade the glycosaminoglycans hyaluronic acid (HA) and chondroitin sulfate, is upregulated upon osteoclastogenesis. The findings point out the predominant involvement of HYAL1 in bone HA metabolism and perhaps bone remodeling via the resorption lacuna. Furthermore, the expression of HYAL1 is strongly upregulated, at the mRNA and protein level, upon in vitro differentiation of macrophages into osteoclasts. In addition, it is reported that the osteoclast differentiation process includes changes in the subcellular trafficking of HYAL1 that promote its extracellular residency.

HYAL1 catalyzes the hydrolysis of chondroitin sulfate and binds to chondroitin sulfate proteoglycans such as integrins and other cell surface receptors, so its direct binding is another way in which active HYAL1 may affect cell surface receptor involvement. Specially, HYAL1 may adhere to the surface of the exosome, primarily to promote its cell docking, allowing exosome contents to be delivered to target cells more efficiently. Upon internalization, changes in the vesicle microenvironment may lead to dissociation of HYAL1, and then exosome residues can participate in the subsequent process independently of HYAL1.

What is particularly noteworthy is that HYAL1 expression in tumor cells can influence cancer progression. 22Rv1 cells that over-express HYAL1 are more rapidly metastatic than control cells. HYAL1 is secreted as a soluble factor by the cell, and since its activity requires low pH, it could be locally active within acidic microenvironments at the tumor site. Presence of HYAL1 in exosomes implies that it could also be carried from the primary tumor site through the lymphatics or the circulation and arrive at target cells in remote tissues. In this way, a tumor over-expressing HYAL1 could initiate events to prepare tissues for metastasis. According to the recent research, higher HYAL1 expression was detected among primary tumors from patients with subsequent brain metastases compared with those without brain metastases. Interestingly, brain metastatic tissue showed a significantly reduced HYAL1 expression compared with the corresponding primary tumor. HYAL1 expression in brain metastases was also significantly lower than in skin, liver, and lung metastases. Some results suggest that the enzyme HYAL1 plays a role in tumor dissemination and brain-specific colonization, rather than in subsequent metastatic out-growth.

Coincidentally, the hyaluronidase HYAL1 is clinically and functionally implicated in prostate cancer progression and metastasis. Elevated HYAL1 accelerates vesicular trafficking in prostate tumor cells, thereby enhancing their metastatic potential in an autocrine manner through increased motility and proliferation. HYAL1 protein is a component of exosomes produced by prostate tumor cell lines. The presence of HYAL1 in tumor-derived exosomes and its ability to impact the behavior of stromal cells suggests cell-cell communication via exosomes is a novel mechanism by which elevated HYAL1 promotes prostate cancer progression. Prostate tumor cells over-expressing HYAL1 had accelerated vesicular trafficking rates that increased autocrine proliferation and movement through changes in cell surface integrins and cadherins.

What’s more, the expression of HYAL1 is increased in pancreatic ductal adenocarcinoma (PDAC). Screening of mRNA expression genes identified HYAL1 as a gene over-expressed in PDAC cells, suggesting that epigenetic mechanisms may be involved in the transcriptional regulation of this gene. HYAL1 protein concentrations were significantly higher in primary PDAC tissues as compared with non-tumor pancreatic tissues. Importantly, inhibition of HYAL by dextran sulfate significantly inhibited the migration of PDAC cells and shown strong HYAL1 expression. In other words, these findings suggest that over-expression of HYAL1 is a common mechanism that may contribute to the aggressive phenotype of PDAC.

References:

Mcatee C O, et al. Hyaluronidase HYAL1 increases tumor cell proliferation and motility through accelerated vesicle trafficking. Journal of Biological Chemistry, 2015, 290(21):13144-56.
Kohi S, et al. Increased Expression of HYAL1 in Pancreatic Ductal Adenocarcinoma. Pancreas, 2016, 45(10):1467.
Puissant E, et al. Monocytes/Macrophages Upregulate the Hyaluronidase HYAL1 and Adapt Its Subcellular Trafficking to Promote Extracellular Residency upon Differentiation into Osteoclasts. Plos One, 2016, 11(10):e0165004.
Mcatee C O, et al. Prostate tumor cell exosomes containing hyaluronidase HYAL1 stimulate prostate stromal cell motility by engagement of FAK-mediated integrin signaling. Matrix Biology, 2018.
Witzel I, et al. Role of HYAL1 expression in primary breast cancer in the formation of brain metastases. Breast Cancer Research & Treatment, 2017, 162(3):1-12.

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