Atherosclerosis ; immunology ; metabolism ; pathology ; Biomarkers ; metabolism ; C-Reactive Protein ; metabolism ; Endothelium, Vascular ; metabolism ; pathology ; physiopathology ; Inflammation ; metabolism ; pathology ; Inflammation Mediators ; metabolism ; Interleukins ; metabolism ; Metabolic Syndrome ; metabolism ; pathology ; Tumor Necrosis Factor-alpha ; metabolism

Fatty Liver ; metabolism ; pathology ; Humans ; Inflammation ; Lipidoses ; metabolism ; pathology ; Non-alcoholic Fatty Liver Disease

OBJECTIVE: To investigate the expression of Ca²⁺/calmodulin-dependent protein kinase II (CaMK Ⅱ) in pancreatic tissues of mice with severe acute pancreatitis (SAP) and explore the protective effect of KN93, a CaMK Ⅱ inhibitor, against pancreatic injury in SAP and the possible mechanism. METHODS: Thirty-six healthy male C57 mice were randomly divided into sham operation group, SAP group, KN93 group and SAP + KN93 group (n=9). Serum and pancreatic tissue samples were collected 24 h after modeling. The pathological changes in the pancreatic tissues were observed using HE staining. Serum lipase and amylase activities and the levels of inflammatory factors were detected using ELISA. Western blotting was used to detect the expressions of CaMK Ⅱ, p-CaMK Ⅱ, p-NF-κB, MAPK and p-MAPK in mouse pancreas. RESULTS: Compared with those in sham operation group, the expressions of p-CaMK Ⅱ, p-NF-κB and p-MAPK were significantly increased in SAP group (P < 0.05). KN93 treatment obviously alleviated pathological injuries of the pancreas in SAP mice, and significantly lowered serum levels of lipase, amylase and inflammatory factors (TNF-α and IL-6) and phosphorylation levels of NF-κB, ERK and MAPK proteins (P < 0.05). CONCLUSION The activity of CaMK Ⅱ is significantly increased in the pancreatic tissue of SAP mice. KN93 can alleviate pancreatic injury and inflammation in SAP mice possibly through the ERK/MAPK signaling pathway.
Acute Disease ; Animals ; Inflammation/metabolism* ; Male ; Mice ; NF-kappa B/metabolism* ; Pancreas/pathology* ; Pancreatitis/pathology*

The pattern of metabolism changes obviously after severe burn trauma, and it is characterized by an immensely increase in energy consumption, persistent strengthening in catabolism, and impediment of utilization of nutrient substrate. It will lead to autophagy, continuous consumption, and progressive emaciation, etc. If these pathological phenomena can not be effectively corrected, the prognosis of patients with serious burn will be poor, with complications of organ damage, immune dysfunction, and delayed wound healing, etc. Hypermetabolism after burn has become one of the leading causes of multiple organ dysfunction and even death. After many years' research, we have a certain understanding of burn hypermetabolism, but it is still difficult to clearly explain the mechanism up to now. Moreover, the measures of regulating hypermetabolism are still not perfect, hampering the advance of treatment of serious burn trauma. The purpose of the article is to analyze and discuss the essential mechanism of hypermetabolism after burn, basing on the new literature and a series of our experimental and clinical studies. Meanwhile the regulation strategy concerning burn hypermetabolism is proposed. It focuses on regulation of endocrine and inflammatory mediators, as well as maintenance of gastrointestinal structure and function.
Burns ; metabolism ; pathology ; therapy ; Endocrine System ; Gastrointestinal Tract ; Humans ; Inflammation ; Inflammation Mediators

Maintenance of cell junctions plays a crucial role in the regulation of cellular functions including cell proliferation, permeability, and cell death. Disruption of cell junctions is implicated in a variety of human disorders, such as inflammatory diseases and cancers. Understanding molecular regulation of cell junctions is important for development of therapeutic strategies for intervention of human diseases. Ubiquitination is an important type of post-translational modification that primarily regulates endogenous protein stability, receptor internalization, enzyme activity, and protein-protein interactions. Ubiquitination is tightly regulated by ubiquitin E3 ligases and can be reversed by deubiquitinating enzymes. Recent studies have been focusing on investigating the effect of protein stability in the regulation of cell-cell junctions. Ubiquitination and degradation of cadherins, claudins, and their interacting proteins are implicated in epithelial and endothelial barrier disruption. Recent studies have revealed that ubiquitination is involved in regulation of Rho GTPases' biological activities. Taken together these studies, ubiquitination plays a critical role in modulating cell junctions and motility. In this review, we will discuss the effects of ubiquitination and deubiquitination on protein stability and expression of key proteins in the cell-cell junctions, including junction proteins, their interacting proteins, and small Rho GTPases. We provide an overview of protein stability in modulation of epithelial and endothelial barrier integrity and introduce potential future search directions to better understand the effects of ubiquitination on human disorders caused by dysfunction of cell junctions.
Animals ; Humans ; Inflammation ; metabolism ; pathology ; Intercellular Junctions ; metabolism ; Neoplasms ; metabolism ; pathology ; Protein Stability ; Ubiquitin-Protein Ligases ; metabolism ; Ubiquitination

Atherosclerosis ; pathology ; C-Reactive Protein ; metabolism ; Dendritic Cells ; metabolism ; Glycation End Products, Advanced ; metabolism ; Humans ; Inflammation

Aged ; Angiofibroma ; metabolism ; pathology ; Desmin ; metabolism ; Diagnosis, Differential ; Female ; Humans ; Inflammation ; Leiomyosarcoma ; pathology ; Neoplasms, Muscle Tissue ; metabolism ; pathology ; Vimentin ; metabolism ; Vulvar Neoplasms ; metabolism ; pathology

Accumulating evidences have documented that angiogenesis is closely linked to inflammation and regulators of angiogenesis play key roles in various inflammatory conditions. PlGF is an angiogenic protein belonging to the VEGF family and is upregulated mainly in pathologic conditions. Recently, PlGF was discovered having a proinflammatory role in inflammatory arthritis and its serum level drew attention not only as a useful surrogate biomarker but also a potential therapeutic target in atherosclerosis and various cancers. Particularly, PlGF has attractive clinical values because endogenous PlGF is redundant for vascular development and physiological vessel maintenance in healthy adults. However, there have been conflicting results about the efficacy of PlGF inhibition depending on the experimental and clinical settings. Further close investigations for resolving the puzzle of PlGF biology are required.
Animals ; Arthritis, Rheumatoid/*metabolism/pathology ; Atherosclerosis/*metabolism/pathology ; Biological Markers/metabolism ; Humans ; Inflammation/metabolism ; Neoplasms/*metabolism/pathology ; Neovascularization, Pathologic ; Pregnancy Proteins/*metabolism ; Signal Transduction

OBJECTIVETo study the expressions of Integrinalpha2beta1 and CD133 in benign prostatic hyperplasia (BPH) complicated by prostatitis and their significance.

METHODSSpecimens were obtained from 56 BPH patients undergoing transvesical prostatectomy. Paraffin sections of the specimens were subjected to HE staining for pathological examination of inflammatory changes under the light microscope. Twenty-four patients with simple BPH were included in Group A, and the other 32 with BPH complicated with prostatitis in Group B. The expressions of Integrinalpha2beta1 and CD133 in the prostatic tissues of the two groups were determined by immunohistochemistry, Western blotting and IPP6.0 image analysis software.

RESULTSThe expressions of Integrinalpha2beta1 and CD133 were significantly higher in Group B than in A (P < 0.05), and so were the mean relative value of the optical density of Integrinalpha2beta1 (0.29 +/- 0.18 vs 0.04 +/- 0.03) and that of CD133 (0.08 +/- 0.07 vs 0.0020 +/- 0.0018) (P < 0.05).

CONCLUSIONInflammation can up-regulate the expressions of Integrinalpha2beta1 and CD133 in BPH tissue.

AC133 Antigen ; Antigens, CD ; metabolism ; Glycoproteins ; metabolism ; Humans ; Inflammation ; metabolism ; Integrin alpha2beta1 ; metabolism ; Male ; Peptides ; metabolism ; Prostatic Hyperplasia ; complications ; metabolism ; pathology ; Prostatitis ; complications ; metabolism ; pathology

Equine endometriosis is a multifactorial disease considered to be a major cause of equine infertility. The purpose of this study was to evaluate the reliability of histomorphological grading for biopsy-like samples compared to entire uterine wall samples, to examine the association between the degree of endometriosis with animal age, and to investigate the role of inflammation in endometriosis and the expression of different matrix metalloproteinases in equine endometrium. Histomorphological lesions in 35 uterine samples were examined while comparing biopsy-like samples and entire-wall samples. Seventeen uterine samples were stained with antibodies against MMP-2, MMP-9, MMP-14, and TIMP-2. The morphologic evaluation results of the biopsy-like tissue and entire-wall samples were significantly correlated. Endometriosis in older mares (>12 years of age) was more severe than in young mares (2~4 years of age), confirming the positive correlation between animal age and disease severity, while inflammation was poorly related to the degree of endometriosis. MMP-2 and MMP-14 were detected in stromal cells, while MMP-9 and TIMP-2 were both found in stromal and glandular epithelial cells. There were no significant differences in MMPs expression between the two groups (young vs. old mares). Additional studies on the activity of MMPs could further define the role of these enzymes in equine endometriosis.
Animals ; Endometriosis/metabolism/pathology/*veterinary ; Female ; Gene Expression Regulation, Enzymologic/*physiology ; Horse Diseases/metabolism/*pathology ; Horses ; Immunohistochemistry/veterinary ; Inflammation/pathology/*veterinary ; Matrix Metalloproteinases/genetics/*metabolism ; Uterus/metabolism/pathology