Prognostic relevance of serum hyaluronan levels in patients with breast cancer

Ponting, J; Howell, Anthony; Pye, David; Kumar, Shant

doi:10.1002/ijc.2910520607

Cited by 21 publications

(14 citation statements)

References 39 publications

(13 reference statements)

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“…9,22 Hyaluronidase activity was therefore measured in serum samples from breast cancer patients with primary tumors (n ϭ 16), metastatic breast cancer (n ϭ 17) and control patients with nonmalignant conditions (n ϭ 16). The hyaluronidase activity was assessed using a novel aggrecan assay (Table I) and some samples were also tested using HA substrate gel zymography.…”

Section: Measurement Of Hyaluronidase Activity In the Serum Of Breastmentioning

confidence: 99%

“…4 In some types of cancer such as bladder, breast and colorectal, the serum levels of HA have been found to be of prognostic value, [5][6][7][8] although conflicting results have been obtained from patients with breast cancer. 9 The hyaluronidases that degrade HA have also been implicated in tumor progression and metastasis, as well as angiogenesis. 10 Hyaluronidase-1 (hyal-1) was originally isolated from human plasma, has a pH optimum of 3.8 and cleaves HA to small (Ͻ20 kDa) MW fragments.…”

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confidence: 99%

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Hyaluronidase gene profiling and role of HYAL‐1 overexpression in an orthotopic model of prostate cancer

Patel¹,

Turner²,

Stubberfield³

et al. 2001

Intl Journal of Cancer

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The mRNA levels of hyal-1, hyal-2, LUCA3 and PH20, the 4 hyaluronidases with demonstrated endoglucosaminidase activity, were extensively profiled in normal and tumor tissues and cell lines, using dot blot analysis and quantitative PCR. In normal tissues, hyal-1, hyal-2 and LUCA3 all showed unique patterns of mRNA expression, but were generally of widespread distribution, whereas PH20 mRNA was restricted to testes. In a small set of breast tumor samples, no elevations in hyal-1, hyal-2 or LUCA3 mRNA were seen. Hyaluronidase activity measured by a novel assay or zymography was also not elevated in sera from a number of breast cancer patients, compared to sera from normal volunteers. In ex vivo xenograft tumor cell lines, however, hyal-1 or hyal-2 mRNA levels were frequently elevated, whereas LUCA3 was only infrequently elevated and PH20 not at all. The hyaluronidases are a family of degradative endoglucosaminidase enzymes 1 whose substrate, hyaluronic acid (HA), is a major constituent of the extracellular matrix (ECM). 2 Cellular interactions with the underlying ECM are crucial in development, 3 for the maintenance of normal cellular functions and in response to injury and infection. In situations where malignant cell growth and subsequent metastasis occur, the degradation of the ECM is required. HA, a large polysaccharide of approximately ten thousand disaccharide repeats, is known to inhibit cell differentiation, promote proliferation, regulate cell motility and HA synthesis occurs before mitosis. 1 Increased serum or tissue associated levels of HA have been correlated with tumor progression 2 and metastatic behavior. 4 In some types of cancer such as bladder, breast and colorectal, the serum levels of HA have been found to be of prognostic value, 5-8 although conflicting results have been obtained from patients with breast cancer. 9 The hyaluronidases that degrade HA have also been implicated in tumor progression and metastasis, as well as angiogenesis. 10 Hyaluronidase-1 (hyal-1) was originally isolated from human plasma, has a pH optimum of 3.8 and cleaves HA to small (Ͻ20 kDa) MW fragments. 11 Hyaluronidase-2 (hyal-2) is also an acidactive enzyme that digests HA polymers down to 20 kDa sizes. 12 Hyal-2 has been shown to be located in lysosomes 12 but is also reported to be a GPI-anchored cell surface protein. 13 PH20 was identified as a GPI linked sperm acrosomal enzyme with a neutral pH optimum and cleaves HA to smaller (Ͻ20 kDa) MW fragments. 1 More recently, the hyaluronidase LUCA3 (Barry et al., in preparation) and meningioma expressed antigen 5 (MGEA5, chromosome 10) have also been shown to have activity at neutral pH. 14 Hyal-4 and the pseudogene Hyal-P1, both of which co-localize to chromosome 7q31.3 with PH20, 15 have not yet been demonstrated to possess enzymatic activities.Elevated mRNA levels or increased hyaluronidase enzymatic activity have been associated with invasion and metastasis for ovarian and endometrial cancers, 16 progression of prostate cancer, 17 bladder cancer, 18 colorectal carcino...

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Section: Measurement Of Hyaluronidase Activity In the Serum Of Breastmentioning

confidence: 99%

mentioning

confidence: 99%

Hyaluronidase gene profiling and role of HYAL‐1 overexpression in an orthotopic model of prostate cancer

Patel¹,

Turner²,

Stubberfield³

et al. 2001

Intl Journal of Cancer

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“…Elevated concentrations of HA have also been found in several human tumors such as mesothelioma [4], Wilm's tumor [5], and colorectal [6], gastric [7,8] or breast carcinomas [9][10][11][12][13]. In addition, there are several evidences that point to a key role of HA in the regulation steps of tumor growth, tissue invasion, and metastasis occurrence.…”

Section: Introductionmentioning

confidence: 99%

Expression and Clinical Signification of Cytosolic Hyaluronan Levels in Invasive Breast Cancer

Corte

González

Lamelas

et al. 2006

Breast Cancer Res Treat

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“…Therefore, clearance of the circulating HA from lymph and blood is likely to be important for normal health. Indeed, it is reported that elevated serum HA levels are found in several disease conditions, such as liver cirrhosis [29][30][31], rheumatoid arthritis [32][33][34], scleroderma [35,36], psoriasis [37] and cancer [38][39][40]. These have been already described by Zhou et al [12].…”

Section: Introductionmentioning

confidence: 90%

Uptake of Enzymatically-Digested Hyaluronan by Liver Endothelial Cells in Vivo and in Vitro

Mochizuki

Kano

Shimada

et al. 2009

Journal of Biomaterials Science, Polymer Edition

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Intravenously-injected hyaluronan (HA) is distributed into liver in which endothelium is a site of uptake and degradation of HA. The role and fate of HA have been widely investigated; however, effects of size and dose of HA on its metabolism have not been well documented yet. To investigate these effects, we prepared fluorescein-labeled HAs, according to the modified methods described by de Belder and Wik, which were enzymatically digested. The 90 kDa fluorescein-labeled HA gradually accumulated in a liver that was distributed into the endothelium; however, 10 kDa or less HA did not. Cell fractionation and flow cytometry further demonstrated the cell of uptake in the liver is an endothelial cell, both in vivo and in vitro. Interestingly, the largest uptake by liver endothelial cells in vitro was observed in 10 kDa HA, even though which did not accumulate in liver in vivo. These results suggest that the result observed with 10 kDa HA in vivo is due to the rapid excretion in urine. Thus, inhibiting of the digestion or suppressing of the urinary excretion would enhance uptake of HA in vivo. These ideas may help to deliver drugs or genes targeting to liver endothelium.

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Prognostic relevance of serum hyaluronan levels in patients with breast cancer

Cited by 21 publications

References 39 publications

Hyaluronidase gene profiling and role of HYAL‐1 overexpression in an orthotopic model of prostate cancer

Hyaluronidase gene profiling and role of HYAL‐1 overexpression in an orthotopic model of prostate cancer

Expression and Clinical Signification of Cytosolic Hyaluronan Levels in Invasive Breast Cancer

Uptake of Enzymatically-Digested Hyaluronan by Liver Endothelial Cells in Vivo and in Vitro

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