Hyaluronidase-1 Antibodies

Hyaluronidase-1 (HYAL1)

May have a role in promoting tumor progression. May block the TGFB1-enhanced cell development.

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Gene Information

Human
Gene Name:	HYAL1
Uniprot:	Q12794
Entrez:	3373

Family

Belongs to:
glycosyl hydrolase 56 family

Alternative Names

EC 3.2.1.35; FUS2; HYAL1; HYAL-1; Hyaluronidase 1; Hyaluronoglucosaminidase 1; hyaluronoglucosaminidase-1; LUCA1; luCa-1; LUCA1hyaluronidase-1; Lung carcinoma protein 1; MGC45987; NAT6; plasma hyaluronidase; tumor suppressor LUCA-1

Molecular Weight

Mass (kDA):
48.368 kDA

Genomic Context

Human
Location:	3p21.31
Sequence:	3; NC_000003.12 (50299889..50312951, complement)

Tissue Specificity

Highly expressed in the liver, kidney and heart. Weakly expressed in lung, placenta and skeletal muscle. No expression detected in adult brain. Isoform 1 is expressed only in bladder and prostate cancer cells, G2/G3 bladder tumor tissues and lymph node specimens showing tumor invasive tumors cells. Isoform 3, isoform 4, isoform 5 and isoform 6 are expressed in normal bladder and bladder tumor tissues.

Subcellular Localizations

Secreted. Lysosome.

Diseases

• Neoplasms
• Malignant Neoplasms
• Headache
• Neoplasm Metastasis
• Carcinoma
• Tumor Angiogenesis
• Malignant Paraganglionic Neoplasm
• Tissue Adhesions
• Prostatic Neoplasms
• Malignant Neoplasm Of Prostate
• Lung Neoplasms
• Malignant Neoplasm Of Urinary Bladder

• Pathologic Neovascularization
• Malignant Neoplasm Of Lung
• Malignant Neoplasm Of Breast
• Mucopolysaccharidoses
• Tumor Progression
• Mammary Neoplasms
• Bladder Neoplasm

Pathways

• Angiogenesis
• Cell Cycle
• Cell Growth
• Cell Proliferation
• Localization
• Translation
• Wound Healing
• Cell Adhesion
• Cell Migration
• Cell Cycle Arrest
• Inflammatory Response
• Cell-cell Adhesion
• Glycosylation

• Ovulation
• Methylation
• Regeneration
• Pathogenesis
• Rna Interference
• Secretion
• Transport

PTMs

• Biotinylation
• Cleavage
• Methylation
• Glycosylation

• Demethylation
• Phosphorylation
• Reduction
• Acetylation

• Deglycosylation

Research Areas

• Immunology
• Inflammation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/HYAL1

Best Uses Of The HYAL1 Marker

The HYAL1 marker has several uses. It is an essential protein that can be used to analyze lysosomal hydrolase. Scientists can use it to submit results, species and applications samples, and to earn product credits. Its utility is universal and accessible to all scientists. It is particularly useful for medical testing and forensics.

HYAL1 is a lysosomal hyaluronidase

The HYAL1 mark is a highly-specific protein that is found in most tissues of the human body. Its synthesis depends on the presence at the N and C terminus of two distinct glycsoyl hydrolase domains. Both regions exhibit catalytic ability in vitro. However, the exact mechanism of Hyaluronidase is not known. These two regions could indicate the existence a gene.

The HYAL1 genome encodes a protein called lysosomal hyaluronidase. They degrade the chondroitin sulfate. This protein is found in human cells as the hyaluronan, a major component to the extracellular matrix. It is involved in cell proliferation and migration, as well as differentiation.

Substrat gel zymography can detect hyaluronidase activity. Electrophoresis is used to separate the proteins from the sample. After the separation, the proteins are stained to detect the hyaluronic acid. If the enzyme is present, the substrate gel will show a clear zone. The resulting protein concentration will be interpreted by a variety of analytical methods.

As Hyaluronidase activity is a key factor for cartilage degeneration, the sHASEGP protein has a high affinity for chondroitin sulfate proteoglycans and is the best candidate for a biomarker. It can be used as a marker to assess cartilage disease and other conditions. Its activity is also useful when researching biodegenerative diseases or treating osteoporosis.

Hyaluronidase domains are included in the sHASEGP polypeptide. Hyaluronidase domains of sHASEGP peptides are single-chain or multi-chain proteins. Although the two-chain forms are different in size and constitution, each retains Hyaluronidase activity. Hyaluronidase domains show homology to other hyaluronidaselike sequences.

The sHASEGP peptide includes the catalytic domain Hyaluronidase. Hyaluronidase is present in homodimers and heterodimers. The sequences of polypeptides share at most 85% identity. The sHASEGP polypeptide has 90% identity. It has been shown, that the sHASEGP Protein contains the Hyaluronidase Domain.

It is a lysosomal hyaluronidase

The LYS hyaluronidase HYAL1 protein gene has eight alternative splices and one fully-lengthed protein. Variants 1-5 all have a shortened catalytic domain. This is found in prostate cancer, bladder cancer tissues, and the latter. However, bladder carcinoma cells have a predominant full-length proteins.

The lysosomal hyaluironidase HYAL1 has two opposing functions in cancer. The former promotes malignant cell growth, while HYAL1 suppresses it. Hence, a complete understanding of the hyaluronan anabolic and catabolic systems of cancer may open new therapeutic vistas.

Hyaluronan is not only important in tumorigenesis but can also influence the growth and development of cancer cells. HAS3 increases the amount of hyaluronan produced, which in turn alters the balance needed to support tumor growth. Furthermore, in a tetracycline-inducible expression system, HAS3 is expressed to regulate cell growth.

Human Hyal1 hydrolyzes intracellular human HA and can be found in plasma and urine. The gene is important in the production of angiogenic HA fragments. Mutations in HYAL1 are associated with mucopolysaccharidosis IX, a rare inflammatory disease characterized by reduced stature. It is also possible that HYAL1 may provide a prognostic indicator for prostate cancer.

HAS2 mRNA expression levels were high in HAS3 and HAS3 but HAS1 mRNA levels weren't significantly related to hyaluronan formation in individual tumors. However, HYAL1 mRNA levels in grade 3 serous ovarian carcinoma were significantly lower than in other tumors. HAS3 expression was also associated with tumor hyaluronan levels in the endometrium.

The structural domain structure of HYAL1 resembles that of a lysosomal cytokininase. However HYAL1 lacks an N-terminal helix. Its elongated shape and extensive solvent accessibility are consistent with its role in mediating protein-protein interactions. Given its flexibility and length, the bhairpin units seems to be a good choice for mediating these interactions. Its sequence is highly variable among lysosomal Hyaluronidasses, so it could play a role modulating partner affinities for the full-length enzyme.

Human HYAL1 hydrolyzes b1-4 Glycosyl bonds in HA (a molecule found in plasma or tissues). This enzyme is responsible to the degrading of hyaluronan. It is an important molecular component of the structure of connective tissue and embryonic development. It is involved in angiogenesis and inflammation, as well as cancer. Advanced stages in bladder cancer may cause HYAL1 to be elevated. Moreover, the alternative splice variants of the gene are associated with a lower expression level of HYAL1 within human cells.

435 amino acid protein HYAL1 cleaves HA Polymers into short chains, and tetrasaccharides. The enzyme's activity depends on pH and it contains three N-glycosylation spots. Moreover, its anomeric form is different from that of the bvHyal family.

It is a marker for lysosomal hyaluronidase

HYAL1 enzyme is a highly-regulated gene during osteoclastogenesis. This process involves giant multinucleated cells coming into contact with bone matrix. The cells polarize and form an extracellular latuna. HA is metabolized in the extracellular milk through exocytosis with acid hydrolases, secretory lysosomes, and lysosomal vATPase. The enzyme also plays a role in the differentiation process of osteoclasts. These are the key actors in bone remodeling.

It is highly expressed in liver and kidneys, but only weakly in the placenta or skeletal muscles. Although HYAL1 expression cannot be detected in adult brain tissue it can be found in bladder cancer cells and prostate cancer cells. It is expressed in small-cell lung carcinoma, but not in brain tissues. It has also been identified in glioma cells.

Normal ovaries expressed HYAL1 significantly less than normal ovaries, while HAS2 was and HAS3 was more abundant. However, the association between HYAL1 and hyaluronan in individual samples was not significant. HYAL1 mRNA was found to be significantly correlated with tissue hyaluronidase activity, and inversely correlated hyaluronan concentration.

The genes that encode HYAL1 are tandemly distributed and code for disparate hyaluronidase activities. Mutations in HYAL1 cause mucopolysaccharidosis IX, a genetic disease characterized by the presence of abnormal HYAL1 gene. In addition to mucopolysaccharidosis, HYAL1 has been identified in kidney, bladder, and prostate tissues. HYAL1 as well as HYAL3 were found to play an important role in tumor metastasis and angiogenesis and the progression of cancer growth.

In this study, rhHyal-1 (WT) was injected into Hyal-1/ mice. Hyal-1-/ mice were injected with unlabelled Hyal-1. The intracellular journey of Hyal-1 could be traced by analysing the distribution of the injected proteins. The distribution patterns were compared to those of other lysosomal-hyaluronidase. This is a marker of Lysosomal Hyalinase.

The researchers examined the behavior of Hyal-1 using classical centrifugation techniques. They also compared the protein to reference markers of the same organelle. The researchers also experimented with perfused tissue fractions from rodent liver and human hemoglobin cells. They performed immunodetection using M, L and P fractions.

The researchers studied the association of HYAL1 expression with the development of invasive breast cancer in the general population and cancer patients. The results showed a clear correlation between HYAL1 protein expression and subsequent breast cancer development. This means that early detection could help to reduce the incidence of this condition. HYAL1 could be used to detect tumors.

HYAL1 RNA may be used to detect bladder cancer early. Researchers found that it was sensitiver and more specific than urine analysis. It also showed a correlation to survivin RNA. These results need to be confirmed. It is important to note, however, that HYAL1 can not be used to treat all types and forms of cancer.