Mucolytic Enzyme Systems. X. Serum Hyaluronidase Inhibitor in Liver Disease 1

Snively, George G.; Glick, David

doi:10.1172/jci102340

Cited by 13 publications

(3 citation statements)

References 6 publications

(5 reference statements)

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“…Furthermore, a number of clinical studies report increased levels of inhibitor in the serum of patients with cancer, liver disease and dermatological disorders (Grais and Glick, 1948;Snively and Glick, 1950;Newman et al, 1955;Kolarova, 1975). Based on these studies, Mio et al (2000) purified a high molecular mass (120 kDa), thermolabile glycoprotein hyaluronidase inhibitor from mouse serum.…”

Section: Hyaluronidase Inhibitorsmentioning

confidence: 99%

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

2007

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Section: Hyaluronidase Inhibitorsmentioning

confidence: 99%

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

2007

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“…The presence of inhibitor was justified by a number of clinical studies that report increased levels of inhibitor in the serum of patients with cancer, liver and dermatological disorders [101][102][103][104]. Based on these studies, Mio et al [105] isolated a high molecular mass (120 kDa), thermolabile glycoprotein HAase inhibitor from mouse serum.…”

Section: Proteinsmentioning

confidence: 99%

Hyaluronidase Inhibitors: A Biological and Therapeutic Perspective

Girish¹,

Kemparaju²,

Nagaraju

et al. 2009

CMC

139

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The hyaluronidases (HAases) are a group of less extensively studied glycosidases distributed throughout the animal kingdom and are popularly known as 'spreading factors'. In recent years, HAases received much attention due to their ability to abruptly alter the hyaluronic acid (HA) homeostasis. HAases preferentially degrade HA, which is a megadalton acidic structural polysaccharide found exclusively in the extracellular matrix (ECM) of animals. The HA-HAase system has been suggested to participate in many pathophysiological conditions. The HA degradation in ECM, crack down the structural integrity with an eventual increased tissue permeability that is attributed for the spreading property. The spreading property has been widely accepted in functions including envenomation, acrosomal reaction/ovum fertilization, cancer progression, microbial pathogenesis such as wound infections, pneumonia, and other sepses like, bacteremia and meningitis. HA fragmentation has dual effects; generation of a wide molecular range bioactive oligosaccharides of angiogenic, pro-inflammatory, and immunostimulatory properties; and impairment in the reservoir capacity of ECM that holds metal ions, growth factors, cytokines and various enzymes for signal transduction. Hence, inhibition of HA degradation appears critical and imperative in HAase mediated pathological conditions. HAase inhibitors are thus potent regulators that maintain HA homeostasis and they might serve as anti-inflammatory, anti-aging, anti-microbial, anticancer and anti-venom/toxin and contraceptive agents. In addition, HAase inhibitors may serve as tools to understand several unexplained and complex functions of HAases in HA metabolism. Therefore, this review is expected to provide an integrated update as of 2008 on the HAase inhibitors and their possible role as therapeutics in the management of a wide range of pathological conditions.

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“…The first studies documenting the existence of a circulating inhibitor of hyaluronidase were published from 1946 to 1949 (21)(22)(23). These studies were followed by clinical reports that increased inhibitor levels occur in the sera of patients with cancer (24 -26), liver disease (27), and dermatological disorders (28). These inhibitors were high molecular mass thermolabile glycoproteins (29) requiring magnesium ion for full activity (30).…”

Section: Hyaluronan (Ha)mentioning

confidence: 99%

Evidence That the Serum Inhibitor of Hyaluronidase May Be a Member of the Inter-α-inhibitor Family

Mio¹,

Carrette²,

Maibach³

et al. 2000

Journal of Biological Chemistry

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A study of the uncharacterized serum inhibitors of hyaluronidase, first described half a century ago, was undertaken. Activity was measured against bovine testicular hyaluronidase using a microtiter-based assay and reverse hyaluronan substrate gel zymography. The predominant inhibitory activity was magnesiumdependent and could be eliminated by protease or chondroitinase digestion and by heat treatment. Kinetics of inhibition were similar against hyaluronidases from testis and snake and bee venoms. The inhibitor had no effect on Streptomyces hyaluronidase, indicating that inhibition was not through protection of the hyaluronan substrate. Inhibition levels in serum were increased in mice following carbon tetrachloride or interleukin-1 injection, inducers of the acute-phase response. Reverse zymography identified a predominant band of 120-kDa relative molecular size, with two bands of greater and one of smaller size. The predominant protein was tentatively identified as a member of the inter-␣-inhibitor family. Inhibition was also observed using either purified inter-␣-inhibitor or an inter-␣-inhibitor-related 120-kDa complex. Inter-␣-inhibitor, found in the hyaluronan-rich cumulus mass surrounding mammalian ova and the coat of fibroblasts and mesothelial cells, may function to stabilize such matrices by protecting against hyaluronidase degradation. Turnover of circulating hyaluronan is extraordinarily rapid, with a half-life of 2-5 min. Prompt increases in levels of serum hyaluronan occur in patients with shock, septicemia, or massive burns, increases that can be attributed, in part, to suppression of degradation by these acute-phase reactants, the inhibitors of hyaluronidase.

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Mucolytic Enzyme Systems. X. Serum Hyaluronidase Inhibitor in Liver Disease 1

Cited by 13 publications

References 6 publications

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

The magic glue hyaluronan and its eraser hyaluronidase: A biological overview

Hyaluronidase Inhibitors: A Biological and Therapeutic Perspective

Evidence That the Serum Inhibitor of Hyaluronidase May Be a Member of the Inter-α-inhibitor Family

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