Opposing roles of inter-α-trypsin inhibitor heavy chain 4 in recurrent pregnancy loss

Rapid Communication : The Porcine Inter - α Trypsin Inhibitor - Heavy Chain 4 ( ITIH 4 ) Gene Maps to Chromosome 131

1The authors thank A. L. Archibald, M. F. Rothschild, and the EC PiGMaP group for distribution of DNA from the PiGMaP reference families, and D. Nicholson, C. Haley, and G. J. Lee for provision of database services and linkage analyses. Published as paper no. 11935, Journal Series, Agric. Res. Div., Univ. of Nebraska, Lincoln 68583-0908. 2To whom correspondence should be addressed: phone: (402)...

Two RFLPs in human inter-alpha-trypsin inhibitor heavy chain gene ITIH2 on chromosome 10.

SOURCE AND DESCRIPTION OF CLONE : The 0.8 kb Eco RI / Bam HI fragment of lambda HuHITI-9 (1) used as a probe codes for human heavy chain H2 of the inter-alpha-trypsin inhibitor (2). POLYMORPHISMS : Kpn 1 (GGTAC/C) identifies one invariant band at 8.5 kb and a diaJlelic polymorphism with DNA fragments at 26.0 kb or 20.0 kb. Msp I (C/CGG) identifies three invariant bands at 2.35 kb, 2.1 kb and 1....

SHAPs, the Heavy Chains of Inter- - Trypsin Inhibitor

Isolation and Characterization of the Promoter and Partial Enhancer Region of the Porcine Inter- -Trypsin Inhibitor Heavy Chain 4 Gene

A porcine genomic library was screened for clones containing the promoter of the major acute-phase protein in pigs, inter-trypsin heavy chain 4 (ITIH4). Following isolation of the promoter, a functional analysis was performed with Hep3B cells. The promoter was induced by interleukin-6 (IL-6) but not by IL-1 . However, IL-1 was shown to inhibit the IL-6-induced activation of the porcine ITIH4 pr...

Site-Specific Glycan Microheterogeneity of Inter-Alpha-Trypsin Inhibitor Heavy Chain H4

Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum. ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease. In this study, we aimed to characterize glycosylation of recombinant and serum-deri...