scholarly journals Gene Expression of the Two Heavy Chains and One Light Chain Forming the Inter-Alpha-Trypsin-Inhibitor in Human Tissues.

1998 ◽  
Vol 21 (2) ◽  
pp. 167-169 ◽  
Author(s):  
Seiichi MIZUSHIMA ◽  
Atsushi NII ◽  
Katsuaki KATO ◽  
Akio UEMURA
Keyword(s):  
Gene Expression ◽  
Trypsin Inhibitor ◽  
Light Chain ◽  
Human Tissues ◽  
Heavy Chains

scholarly journals Expression of inter-alpha-trypsin inhibitor heavy chains in endometrium of cyclic and pregnant gilts

Reproduction ◽  
2003 ◽  
pp. 621-627 ◽  
Author(s):  
RD Geisert ◽  
MD Ashworth ◽  
Keyword(s):  
Gene Expression ◽  
Extracellular Matrix ◽  
Western Blot ◽  
Protease Inhibitor ◽  
Early Pregnancy ◽  
Trypsin Inhibitor ◽  
Serine Protease Inhibitor ◽  
Oestrous Cycle ◽  
Heavy Chains ◽  
Formation Of Complexes

Attachment of the placenta to the uterus in pigs involves extracellular interaction between the expanding trophoblastic membrane and the thick glycocalyx present on the uterine epithelial microvilli. Formation of complexes between members of inter-alpha-trypsin inhibitor family may function in the maintenance of the extracellular matrix. This study investigated the change in the inter-alpha-trypsin inhibitor heavy chains (ITIH1, ITIH2, ITIH3 and ITIH4) during the oestrous cycle and early pregnancy in pigs. Gene expression of ITIH1, ITIH2, ITIH3 and ITIH4 was detected in the endometrium of cyclic and pregnant gilts; however, gene expression of ITIH was not altered throughout the oestrous cycle or early pregnancy. Western blot analysis with an ITIH antiserum identified the possible linkage forms of ITIH with the serine protease inhibitor, bikunin. Pregnancy altered the release of the various inter-alpha-inhibitor forms from the endometrium during the period of trophoblastic attachment. The results from this study indicate that the inter-alpha-trypsin inhibitor family plays an important role in maintenance of the uterine surface glycocalyx during placental attachment in pigs.

scholarly journals Human inter-α-trypsin inhibitor. Synthesis and maturation in hepatoma HepG2 cells

1989 ◽  
Vol 261 (1) ◽  
pp. 305-308 ◽  
Author(s):  
J Bourguignon ◽  
R Sesboüé ◽  
M Diarra-Mehrpour ◽  
M Daveau ◽  
J P Martin
Keyword(s):  
Trypsin Inhibitor ◽  
Light Chain ◽  
Hepg2 Cells ◽  
Light Chains ◽  
Limiting Factor ◽  
Heavy Chains ◽  
Chain Synthesis ◽  
Hepatoma Hepg2

In hepatoma HepG2 cells, human inter-alpha-trypsin inhibitor (ITI) was synthesized as three heavy chains, H-1 (100 kDa), H-2 (110 kDa) and H-3 (113 kDa), and light hybrid chain (49.5 kDa) composed of alpha 1-microglobulin and HI-30 (ITI derivative, human inhibitor of 30 kDa). The association of at least two heavy chains, H-1 and H-3, with the HI-30 part of the light chain gave rise to a molecule similar to serum ITI. A composite protein (approximately 250 kDa) including heavy and light chains was also secreted, while alpha 1-microglobulin and ITI H-2 protein were released as separate entities. Light chain synthesis could be the limiting factor for ITI maturation.

scholarly journals Inter--trypsin Inhibitor Bound to Tumor Cells Is Cleaved into the Heavy Chains and the Light Chain on the Cell Surface

1996 ◽  
Vol 271 (19) ◽  
pp. 11362-11367 ◽  
Author(s):  
Hiroshi Kobayashi ◽  
Junko Gotoh ◽  
Yasuyuki Hirashima ◽  
Toshihiko Terao
Keyword(s):  
Cell Surface ◽  
Tumor Cells ◽  
Trypsin Inhibitor ◽  
Light Chain ◽  
Heavy Chains

Molecular and Microscopic Analysis of Altered Gene Expression in Transgenic and Gene Targeted Mice

1996 ◽  
Vol 54 ◽  
pp. 12-13
Author(s):  
W. K. Jones ◽  
J. Robbins
Keyword(s):  
Gene Expression ◽  
Pulmonary Veins ◽  
Microscopic Analysis ◽  
Mouse Tissue ◽  
Adult Heart ◽  
Heavy Chains ◽  
Altered Gene Expression ◽  
Altered Gene ◽  
Pulmonary Myocardium

Two myosin heavy chains (MyHC) are expressed in the mammalian heart and are differentially regulated during development. In the mouse, the α-MyHC is expressed constitutively in the atrium. At birth, the β-MyHC is downregulated and replaced by the α-MyHC, which is the sole cardiac MyHC isoform in the adult heart. We have employed transgenic and gene-targeting methodologies to study the regulation of cardiac MyHC gene expression and the functional and developmental consequences of altered α-MyHC expression in the mouse.We previously characterized an α-MyHC promoter capable of driving tissue-specific and developmentally correct expression of a CAT (chloramphenicol acetyltransferase) marker in the mouse. Tissue surveys detected a small amount of CAT activity in the lung (Fig. 1a). The results of in situ hybridization analyses indicated that the pattern of CAT transcript in the adult heart (Fig. 1b, top panel) is the same as that of α-MyHC (Fig. 1b, lower panel). The α-MyHC gene is expressed in a layer of cardiac muscle (pulmonary myocardium) associated with the pulmonary veins (Fig. 1c). These studies extend our understanding of α-MyHC expression and delimit a third cardiac compartment.

Immunohistochemical demonstration of bikunin, a light chain of inter-?-trypsin inhibitor, in human brain tumors

Inflammation ◽  
1994 ◽  
Vol 18 (6) ◽  
pp. 589-596 ◽  
Author(s):  
Etsuo Yoshida ◽  
Masugi Maruyama ◽  
Masahiko Sugiki ◽  
Hisashi Mihara
Keyword(s):  
Brain Tumors ◽  
Human Brain ◽  
Trypsin Inhibitor ◽  
Light Chain ◽  
Human Brain Tumors ◽  
Immunohistochemical Demonstration

Xanthine Oxidoreductase Gene Expression and Enzyme Activity in Developing Human Tissues

Neonatology ◽  
1998 ◽  
Vol 74 (4) ◽  
pp. 274-280 ◽  
Author(s):  
Mika Saksela ◽  
Risto Lapatto ◽  
Kari O. Raivio
Keyword(s):  
Gene Expression ◽  
Enzyme Activity ◽  
Xanthine Oxidoreductase ◽  
Human Tissues
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