Reactome | HYAL2 hydrolyses HA into 20kDa fragments

HYAL2 hydrolyses HA into 20kDa fragments

Stable Identifier

R-HSA-2160892

Type

Reaction [uncertain]

Species

Homo sapiens

Compartment

plasma membrane

ReviewStatus

5/5

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HYAL2 hydrolyses HA into 20kDa fragments

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HYAL2 (hyaluronidase 2) hydrolyses high molecular weight hyaluronate (HA), initially in the form of a complex with HAR (hyaluronan receptors) and HYAL2, generating 20kDa HA fragments fragments, HAR, and HYAL2 (Lepperdinger et al. 1998, Jedrzejas & Stern 2005). The acidic microenvironment required for HYAL2 activity (Bourguignon et al. 2004) is generated by SLC9A1 activated by CHP1 (of calcineurin homologous protein 1) (Lin & Barber 1996, Pang et al. 2004, Mishima et al. 2007), a feature of the reaction captured here as positive regulation of the hydrolysis reaction by SLC9A1:CHP1:Ca2+.

Literature References

PubMed ID	Title	Journal	Year
15090545	CD44 interaction with Na+-H+ exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion Bourguignon, LY, Singleton, PA, Diedrich, F, Stern, R, Gilad, E	J Biol Chem	2004
8901634	A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange Lin, X, Barber, DL	Proc. Natl. Acad. Sci. U.S.A.	1996
15035633	Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural elements Pang, T, Hisamitsu, T, Mori, H, Shigekawa, M, Wakabayashi, S	Biochemistry	2004
16104017	Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis Jedrzejas, MJ, Stern, R	Proteins	2005
17050540	Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1 Mishima, M, Wakabayashi, S, Kojima, C	J. Biol. Chem.	2007
9712871	HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity Lepperdinger, G, Strobl, B, Kreil, G	J Biol Chem	1998