Inter-α-inhibitor Is Required for the Formation of the Hyaluronan-containing Coat on Fibroblasts and Mesothelial Cells

Blom, Anna M.; Pertoft, Håkan; Fries, Erik

doi:10.1074/jbc.270.17.9698

Cited by 68 publications

(47 citation statements)

References 30 publications

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“…Therefore, it is very likely that the granule-filament structure represents the SHAP-HA complex. Our findings also help explain the previous observations, which showed that ITI and P␣I stabilized the HA-rich matrix of cultured cells (32,33) and in vitro cumulus expansion (34), and that HA oligomers interfered with ovulation in vivo (35). The cumulus matrix might include other components, such as proteoglycans (36,37), , and the link protein (39).…”

Section: Physiological Functions Of the Shap-ha Complex And Iti Familsupporting

confidence: 73%

Defect in SHAP-Hyaluronan Complex Causes Severe Female Infertility

Zhuo

Yoneda

Zhao

et al. 2001

Journal of Biological Chemistry

256

251

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Hyaluronan (HA) associates with proteins and proteoglycans to form the extracellular HA-rich matrices that significantly affect cellular behaviors. So far, only the heavy chains of the plasma inter-␣-trypsin inhibitor (ITI) family, designated as SHAPs (serum-derived hyaluronan-associated proteins), have been shown to bind covalently to HA. The physiological significance of such a unique covalent complex has been unknown but is of great interest, because HA and the ITI family are abundant in tissues and in plasma, respectively, and the SHAP-HA complex is formed wherever HA meets plasma. We abolished the formation of the SHAP-HA complex in mice by targeting the gene of bikunin, the light chain of the ITI family members, which is essential for their biosynthesis. As a consequence, the cumulus oophorus, an investing structure unique to the oocyte of higher mammals, had a defect in forming the extracellular HA-rich matrix during expansion. The ovulated oocytes were completely devoid of matrix and were unfertilized, leading to severe female infertility. Intraperitoneal administration of ITI, accompanied by the formation of the SHAP-HA complex, fully rescued the defects. We conclude that the SHAP-HA complex is a major component of the HA-rich matrix of the cumulus oophorus and is essential for fertilization in vivo.

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Section: Physiological Functions Of the Shap-ha Complex And Iti Familsupporting

confidence: 73%

Defect in SHAP-Hyaluronan Complex Causes Severe Female Infertility

Zhuo

Yoneda

Zhao

et al. 2001

Journal of Biological Chemistry

256

251

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“…In early studies on the matrices of cultured fibroblasts, mesothelial cells and cumulus-oocyte complexes (15,17), ITI and P␣I were shown to be able to stabilize the HA-rich matrices, suggesting a role for the SHAP-HA complex in stabilizing the HA-rich cell coats. Recently, SHAP-HA complex-deficient mice were generated, and the physiological importance of the complex established as being essential for the expansion of the cumulus oophorus (18).…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies (15,17) suggested that the ITI family molecules, ITI and P␣I, stabilized the HA-rich matrix of cultured cells and cumulus oophorus. Recently, the in vivo implications of the SHAP-HA complex in the extracellular matrix have become evident from our study on bikunin-knockout mice that are unable to form the complex (18).…”

mentioning

confidence: 99%

Molecular Heterogeneity of the SHAP-Hyaluronan Complex

Yingsung

Zhuo

Mörgelin

et al. 2003

Journal of Biological Chemistry

101

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We previously found that a covalent complex of SHAPs (serum-derived hyaluronan-associated proteins), the heavy chains of inter-␣-trypsin inhibitor family molecules, with hyaluronan (HA) is accumulated in synovial fluid of patients with rheumatoid arthritis, and the complex is circulated in patient plasma at high concentrations. How the SHAP-HA complex participates in this disease is unknown. To address this question, it is essential to clarify the structural features of this macromolecule. The SHAP-HA complex purified from synovial fluid of the patients by three sequential CsCl isopycnic centrifugations was heterogeneous in density, and the fractions with different densities had distinct SHAPto-HA ratios. Agarose gel electrophoresis and column chromatography revealed that there was no apparent difference in the size distribution of HA to which SHAPs were bound between the fractions with different densities. The SHAP-HA complex in the higher density fraction had fewer SHAP molecules per HA chain. Therefore, the difference between the fractions with different densities was due to a heterogeneous population of the SHAP-HA complex, namely the different number of SHAP molecules bound to an HA chain. Based on the SHAP and HA contents of the purified preparations, we estimated that an HA chain with a molecular weight of 2 ؋ 10 6 has as many as five covalently bound SHAPs, which could give a proteinaceous multivalency to HA. Furthermore, we also found that the SHAP-HA complex tends to form aggregates, judging from the migration and elution profiles in agarose gel electrophoresis and gel filtration, respectively. The multivalent feature of the SHAP-HA complex was also confirmed by the negative staining electron micrographic images of the purified fractions. Taken together, those structural characteristics may underlie the aggregate-forming and extracellular matrix-stabilizing ability of the SHAP-HA complex.

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“…For example, the Cterminal lectin-like domain of versican has been shown to bind to multimeric tenascin-R and tenascin-C in a calcium-dependent manner, creating the possibility of crosslinking hyaluronan through non-covalent versican-tenascin-versican interactions [33,34]. Other studies have implicated inter-alpha trypsin inhibitor (IαI) as necessary for the formation of cell coats [35,36], for the maintenance of hyaluronan scaffold integrity during cumulus expansion [37], and for potentiating CD44-mediated leukocyte adhesion to hyaluronan-rich matrices [38,39]. IαI heavy chains are transferred from the chondroitin sulfate chain of IαI to the hyaluronan.…”

Section: Hyaluronan Crosslinkingmentioning

confidence: 99%

Hyaluronan-dependent pericellular matrix☆

Evanko¹,

Tammi²,

Tammi³

et al. 2007

Advanced Drug Delivery Reviews

257

238

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Hyaluronan is a multifunctional glycosaminoglycan that forms the structural basis of the pericellular matrix. Hyaluronan is extruded directly through the plasma membrane by one of three hyaluronan synthases and anchored to the cell surface by the synthase or cell surface receptors such as CD44 or RHAMM. Aggregating proteoglycans and other hyaluronan-binding proteins, contribute to the material and biological properties of the matrix and regulate cell and tissue function. The pericellular matrix plays multiple complex roles in cell adhesion/de-adhesion, and cell shape changes associated with proliferation and locomotion. Time-lapse studies show that pericellular matrix formation facilitates cell detachment and mitotic cell rounding. Hyaluronan crosslinking occurs through various proteins, such as tenascin, TSG-6, inter-alpha-trypsin inhibitor, pentraxin and TSP-1. This creates higher order levels of structured hyaluronan that may regulate inflammation and other biological processes. Microvillous or filopodial membrane protrusions are created by active hyaluronan synthesis, and form the scaffold of hyaluronan coats in certain cells. The importance of the pericellular matrix in cellular mechanotransduction and the response to mechanical strain are also discussed.

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Inter-α-inhibitor Is Required for the Formation of the Hyaluronan-containing Coat on Fibroblasts and Mesothelial Cells

Cited by 68 publications

References 30 publications

Defect in SHAP-Hyaluronan Complex Causes Severe Female Infertility

Defect in SHAP-Hyaluronan Complex Causes Severe Female Infertility

Molecular Heterogeneity of the SHAP-Hyaluronan Complex

Hyaluronan-dependent pericellular matrix☆

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