Cited by 204Proteoglycans and glycosaminoglycans researchHydrogels: synthesis, properties, applicationsProtease and Inhibitor Mechanisms

Emerging Roles for Hyaluronidase in Cancer Metastasis and Therapy

Open access
Caitlin O. McAtee, Joseph J. Barycki, Melanie A. Simpson·2014·Advances in Cancer Research

Abstract

Hyaluronidases are a family of five human enzymes that have been differentially implicated in the progression of many solid tumor types, both clinically and in functional studies. Advances in the past 5 years have clarified many apparent contradictions: (1) by demonstrating that specific hyaluronidases have alternative substrates to hyaluronan (HA) or do not exhibit any enzymatic activity, (2) that high-molecular weight HA polymers elicit signaling effects that are opposite those of the hyaluronidase-digested HA oligomers, and (3) that it is actually the combined overexpression of HA synthesizing enzymes with hyaluronidases that confers tumorigenic potential. This review examines the literature supporting these conclusions and discusses novel mechanisms by which hyaluronidases impact invasive tumor cell processes. In addition, a detailed structural and functional comparison of the hyaluronidases is presented with insights into substrate selectivity and potential for therapeutic targeting. Finally, technological advances in targeting hyaluronidase for tumor imaging and cancer therapy are summarized.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/b978-0-12-800092-2.00001-0

Cites

123 of 123 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Hyaluronidase, γ-Glutamyltranspeptidase, prostate-specific antigen, Trysin, β-galactosidase, Azoreductase, etc. are also used in enzyme-stimulated response smart nano-delivery systems.

    “In addition, hyaluronidase, γ-Glutamyltranspeptidase, prostate-specific antigen, Trysin, β-galactosidase, Azoreductase, etc. are also used in enzyme-stimulated response smart nano-delivery systems.157–162”

    From Smart nanoparticles for cancer therapy (2023) · cites this paper as [158]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

1 retracted

Flagged first, then by citations

4 of the 127 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

  1. Godin DA Fitzpatrick PC Scandurro AB Belafsky PC Woodworth BA Amedee RG 2000 PH20: a novel tumor marker for laryngeal cancer Arch Otolaryngol Head Neck Surg 126 402 404 10722016

Cited by

Sorted by citations

Authors
McAtee, C. O., Barycki, J. J., & Simpson, M. A.
Affiliations
University of Nebraska–Lincoln (US)
Corresponding author
Melanie A. Simpson
Venue
Advances in Cancer Research
Publisher
Elsevier
Published
2014
Volume
123
Pages
1-34
ISSN
0065-230X (ISSN-L)
OpenAlex
W2394990651
Cited by
204
References
127
Citations by year
2026: 3 · 2025: 17 · 2024: 14 · 2023: 24 · 2022: 19 · 2021: 20 · 2020: 25 · 2019: 28 · 2018: 14 · 2017: 15 · 2016: 12 · 2015: 12 · 2014: 1
FWCI
18.61
Type
book chapter
Language
en
Open access
Locations
  • Advances in cancer research (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • Lincoln (University of Nebraska) (submittedVersion)
Funders
  • National Institutes of Health (8p20gm103489-10)
  • National Cancer Institute (R01CA165574)
  • National Institute of General Medical Sciences (P20-GM103489)
  • National Center for Research Resources (P20RR018759)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
hyaluronidase, hyaluronic acid, metastasis, tumor invasion, hyaluronan oligosaccharides, hyaluronan synthase, substrate specificity, enzyme structure, hyaluronidase inhibitors, tumor imaging, cancer therapy
MeSH terms
Animals, Cell Movement, Fibroblasts, Humans, Hyaluronic Acid, Hyaluronoglucosaminidase, Molecular Conformation, Molecular Weight, Neoplasm Metastasis, Neoplasms, Polymers, Prognosis, Alternative Splicing, Disease Progression, Mole Rats, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review