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.

Working from within: how secretory leukocyte protease inhibitor regulates the expression of pro-inflammatory genes

2021 ◽  
Author(s):  
Tinsley C. Douglas ◽  
Sari S Hannila
Keyword(s):  
Gene Expression ◽  
Protease Inhibitor ◽  
Neutrophil Infiltration ◽  
Serine Protease Inhibitor ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Inflammatory Factor ◽  
Murine Models ◽  
Anti Inflammatory ◽  
Additional Role ◽  
Pro Inflammatory Cytokines

Secretory leukocyte protease inhibitor (SLPI) is a small but powerful member of the serine protease inhibitor family, which includes proteins such as elafin and alpha1 anti-trypsin. These proteins all have similar structure and antiprotease abilities, but SLPI has been found to have an additional role as an anti-inflammatory factor. It can inhibit the production of pro-inflammatory cytokines in cells stimulated with lipopolysaccharide, prevent neutrophil infiltration in murine models of lung and liver injury, and regulate the activity of the transcription factor NF-κB. In this review, we will revisit SLPI’s unique biochemistry, and then explore how its anti-inflammatory functions can be linked to more recent findings showing that SLPI can localize to the nuclei of cells, bind DNA, and act as a regulator of gene expression.

scholarly journals Regulation of serine protease inhibitor Kazal type-5 (SPINK5) gene expression in the keratinocytes

2014 ◽  
Vol 19 (4) ◽  
pp. 307-313 ◽  
Author(s):  
Ngoc Anh Le ◽  
Midori Katsuyama ◽  
Masashi Demura ◽  
Hideji Tanii ◽  
Hironobu Katsuyama ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Serine Protease Inhibitor

scholarly journals Bovine scavenger receptor class A (SR-A) exhibit specific patterns of regulation in the endometrium during the oestrous cycle and early pregnancy

2019 ◽  
Vol 31 (6) ◽  
pp. 1078 ◽  
Author(s):  
A. Vitorino Carvalho ◽  
C. Eozenou ◽  
C. Richard ◽  
N. Forde ◽  
G. D. Healey ◽  
...  
Keyword(s):  
Gene Expression ◽  
High Throughput ◽  
Early Pregnancy ◽  
Scavenger Receptor ◽  
Oestrous Cycle ◽  
Endometrial Gland ◽  
Class A ◽  
Scavenger Receptor Class ◽  
Immune Factors ◽  
Bovine Species

In mammals, tight regulation of maternal endometrial function is critical for pregnancy success. In bovine species, endometrial expression of members of the scavenger receptor class A (SR-A) has been listed in high-throughput analyses, but very little is known about the involvement of these immune factors during implantation in mammals. To provide first insights into the contribution of SR-A to endometrial physiology, we analysed the expression and regulation of all members of SR-A (SR-A1, SR-A3–SR-A6) during the oestrous cycle and early pregnancy in cattle. Levels of SR-A1 were increased on Day 20 of pregnancy, whereas SR-A3 levels were increased on Day 13 of the oestrous cycle and of the pregnancy. Although SR-A4 levels were reduced on Day 20 of the oestrous cycle, they remained high in pregnant animals. SR-A5 levels increased by Day 13 of the oestrous cycle and decreased on Day 20, but remained high in pregnant animals. Interferon-τ does not affect SR-A gene expression, whereas progesterone regulates the expression of the SR-A3 and SR-A5 transcripts. Endometrial SR-A3 appeared significantly higher in cows carrying invitro-produced embryos than in AI cows. Our data suggest that members of the SR-A family are involved in endometrial remodelling and regulation of endometrial gland physiology, both processes being critical for implantation in mammals.

Glycosaminoglycan-bound and free inter-α-trypsin inhibitor components of follicular fluid

Zygote ◽  
2001 ◽  
Vol 9 (4) ◽  
pp. 283-288 ◽  
Author(s):  
Lars Ødum ◽  
Torben E. Jessen ◽  
Claus Yding Andersen
Keyword(s):  
Extracellular Matrix ◽  
Trypsin Inhibitor ◽  
Follicular Fluid ◽  
Normal Female ◽  
Heavy Chains ◽  
Rate Limiting Step ◽  
Fluid Concentration ◽  
Rate Limiting

The proteinase inhibitor inter-α trypsin inhibitor (ITI) is a blood-derived protein necessary for normal female fertility. Absence of ITI leads to ovulation of naked oocytes that cannot fertilise. ITI consists of two heavy chains (ITI-HC) and bikunin linked by a chrondroitin sulphate. By binding to hyaluronate, ITI-HC stabilises the extracellular matrix, but ITI-HC also binds to proteoglycans in follicular fluid. In vivo concentrations of ITI components in preovulatory follicular fluid, free as well as bound to hyaluronate or proteoglycan, are unknown. In order to quantify these components, 58 follicular fluids and 13 blood samples were collected in connection with in vitro fertilisation and embryo transfer treatment of 13 women. Quantitation of glycosaminoglycan-bound ITI-HC was performed after separation from free ITI in agarose gel. ITI components were determined by immunoelectrophoresis and hyaluronate by an ELISA method. The follicular fluid concentration of ITI was on average 70% of that in plasma and the concentration of hyaluronate remained low despite follicular production, suggesting that the production of hyaluronate is the rate-limiting step in the formation of the extracellular matrix of the oocyte-cumulus complex. In follicular fluid, the concentration of free ITI-HC was higher than that of glycosaminoglycan-bound ITI-HC. Addition of exogeneous hyaluronate doubled the amount of hyaluronate-bound ITI-HC, further supporting the notion that ITI in follicular fluid is not rate-limiting for cumulus expansion in vivo.

scholarly journals Functional Characterization and Novel Rickettsiostatic Effects of a Kunitz-Type Serine Protease Inhibitor from the Tick Dermacentor variabilis

2008 ◽  
Vol 76 (11) ◽  
pp. 5429-5435 ◽  
Author(s):  
Shane M. Ceraul ◽  
Sheila M. Dreher-Lesnick ◽  
Albert Mulenga ◽  
M. Sayeedur Rahman ◽  
Abdu F. Azad
Keyword(s):  
Gene Expression ◽  
Salivary Gland ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Blood Meal ◽  
Serine Protease Inhibitor ◽  
Dermacentor Variabilis ◽  
Mammalian Host ◽  
Spotted Fever Group ◽  
Kunitz Type

ABSTRACT Here we report the novel bacteriostatic function of a five-domain Kunitz-type serine protease inhibitor (KPI) from the tick Dermacentor variabilis. As ticks feed, they release anticoagulants, anti-inflammatory and immunosuppressive molecules that mediate the formation of the feeding lesion on the mammalian host. A number of KPIs have been isolated and characterized from tick salivary gland extracts. Interestingly, we observe little D. variabilis KPI gene expression in the salivary gland and abundant expression in the midgut. However, our demonstration of D. variabilis KPI's anticoagulant properties indicates that D. variabilis KPI may be important for blood meal digestion in the midgut. In addition to facilitating long-term attachment and blood meal acquisition, gene expression studies of Drosophila, legumes, and ticks suggest that KPIs play some role in the response to microbial infection. Similarly, in this study, we show that challenge of D. variabilis with the spotted fever group rickettsia, Rickettsia montanensis, results in sustained D. variabilis KPI gene expression in the midgut. Furthermore, our in vitro studies show that D. variabilis KPI limits rickettsial colonization of L929 cells (mouse fibroblasts), implicating D. variabilis KPI as a bacteriostatic protein, a property that may be related to D. variabilis KPI's trypsin inhibitory capability. This work suggests that anticoagulants play some role in the midgut during feeding and that D. variabilis KPI may be involved as part of the tick's defense response to rickettsiae.

scholarly journals Chemerin Affects P4 and E2 Synthesis in the Porcine Endometrium during Early Pregnancy

2022 ◽  
Vol 23 (2) ◽  
pp. 945
Author(s):  
Marlena Gudelska ◽  
Kamil Dobrzyn ◽  
Marta Kiezun ◽  
Katarzyna Kisielewska ◽  
Edyta Rytelewska ◽  
...  
Keyword(s):  
Western Blot ◽  
Early Pregnancy ◽  
Luteal Phase ◽  
Oestrous Cycle ◽  
Signalling Pathway ◽  
Signalling Pathways ◽  
Steroidogenic Enzyme ◽  
Akt Phosphorylation ◽  
Pathway Activation

Chemerin, belonging to the adipokine family, exhibits pleiotropic activity. We hypothesised that the adipokine could be involved in the regulation of steroidogenesis in the porcine endometrium. Thus, the aim of this study was to determine the effect of chemerin on the key steroidogenic enzyme proteins’ abundance (Western blot), as well as on P4 and E2 secretion (radioimmunoassay) by the porcine endometrium during early pregnancy and the mid-luteal phase of the oestrous cycle. Moreover, we investigated the hormone impact on Erk and Akt signalling pathway activation (Western blot). Chemerin stimulated E2 production on days 10 to 11 of pregnancy. On days 10 to 11 and 15 to 16 of gestation, and on days 10 to 11 of the cycle, chemerin enhanced the expression of StAR and all steroidogenic enzyme proteins. On days 12 to 13 of pregnancy, chemerin decreased StAR and most of the steroidogenic enzyme proteins’ abundance, whereas the P450C17 abundance was increased. On days 27 to 28 of pregnancy, chemerin increased StAR and P450C17 protein contents and decreased 3βHSD protein amounts. It was noted that the adipokine inhibited Erk1/2 and stimulated Akt phosphorylation. The obtained results indicate that chemerin affected P4 and E2 synthesis through the Erk1/2 and Akt signalling pathways.

scholarly journals Growth hormone rapidly activates rat serine protease inhibitor 2.1 gene transcription and induces a DNA-binding activity distinct from those of Stat1, -3, and -4.

1995 ◽  
Vol 15 (1) ◽  
pp. 12-18 ◽  
Author(s):  
M J Thomas ◽  
A M Gronowski ◽  
S A Berry ◽  
P L Bergad ◽  
P Rotwein
Keyword(s):  
Gene Expression ◽  
Growth Hormone ◽  
Protease Inhibitor ◽  
Protein Binding ◽  
Serine Protease ◽  
Dna Sequences ◽  
Gene Promoter ◽  
Serine Protease Inhibitor ◽  
Gh Treatment ◽  
Gh Receptor

Transcriptional regulation by growth hormone (GH) represents the culmination of signal transduction pathways that are initiated by the cell surface GH receptor and are targeted to the nucleus. Recent studies have demonstrated that the activated GH receptor can stimulate Stat1, a cytoplasmic transcription factor that becomes tyrosine phosphorylated and translocates to the nucleus, where it can interact with specific DNA sequences to modulate gene expression. GH also has been found to induce protein binding to a portion of the rat serine protease inhibitor (Spi) 2.1 gene promoter that is required for GH-induced transcription of Spi 2.1. Using GH-deficient hypophysectomized rats as a model, we show that GH treatment rapidly and potently induces both nuclear Spi 2.1 mRNA expression in the liver and specific nuclear protein binding to a 45-bp segment of the Spi 2.1 gene promoter. A GH-inducible gel-shifted complex appears within 15 min of systemic hormone administration and can be inhibited by an antiphosphotyrosine monoclonal antibody but is not blocked by a polyclonal antiserum to Stat1, Stat3, or Stat4, even though the nucleotide sequence contains two gamma interferon-activated sequence-like elements that could interact with STAT proteins. By Southwestern (DNA-protein) blot analysis, approximately 41- and 35-kDa GH-inducible proteins were detected in hepatic nuclear extracts with the Spi 2.1 DNA probe. Thus, a GH-activated signaling pathway stimulates Spi 2.1 gene expression through a unique mechanism that does not appear to involve known members of the STAT family of transcription factors.

Sign in / Sign up

Export Citation Format

Share Document