Effects of Stocking and Transport Conditions on Physicochemical Properties of Meat and Acute-Phase Proteins in Cattle

This study’s objective was to evaluate the effects of distance and stocking density on physicochemical properties and oxidative stability of meat and acute-phase proteins in Brahman crossbred cattle transported by road under hot and humid tropical conditions. Sixty Brahman crossbred heifers were subjected to road transport from a cattle feedlot farm located in Universiti Putra Malaysia (UPM), Serdang, to a commercial ruminant abattoir in Shah Alam, Selangor. Animals were assigned to long and short distances and high, medium, and low stocking densities. The results revealed that the intensity of response significantly increased in meat samples from animals subjected to long-distance transportation and higher stocking density. Alpha-1-acid glycoprotein and serum amyloid-A values increased considerably and were different from the baseline values recorded at preload. In conclusion, the current results revealed that the color, pH, shear force values, water holding capacity (WHC), glycogen level, and malondilaldehyde assay (MDA) concentrations in meat and acute-phase proteins (APP) were affected by both distances and stocking densities, as evidenced by the significant changes recorded from the parameters above.

Download Full-text

Comparison of host endothelial, epithelial and inflammatory response in ICU patients with and without COVID-19: a prospective observational cohort study

Critical Care ◽

10.1186/s13054-021-03547-z ◽

2021 ◽

Vol 25 (1) ◽

Author(s):

Pavan K. Bhatraju ◽

Eric D. Morrell ◽

Leila Zelnick ◽

Neha A. Sathe ◽

Xin-Ya Chai ◽

...

Keyword(s):

Endothelial Dysfunction ◽

Epithelial Cell ◽

Acute Phase ◽

Cell Injury ◽

Acute Phase Proteins ◽

Invasive Mechanical Ventilation ◽

Icu Patients ◽

Icu Admission ◽

Amyloid A ◽

Epithelial Cell Injury

Abstract Background Analyses of blood biomarkers involved in the host response to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) viral infection can reveal distinct biological pathways and inform development and testing of therapeutics for COVID-19. Our objective was to evaluate host endothelial, epithelial and inflammatory biomarkers in COVID-19. Methods We prospectively enrolled 171 ICU patients, including 78 (46%) patients positive and 93 (54%) negative for SARS-CoV-2 infection from April to September, 2020. We compared 22 plasma biomarkers in blood collected within 24 h and 3 days after ICU admission. Results In critically ill COVID-19 and non-COVID-19 patients, the most common ICU admission diagnoses were respiratory failure or pneumonia, followed by sepsis and other diagnoses. Similar proportions of patients in both groups received invasive mechanical ventilation at the time of study enrollment. COVID-19 and non-COVID-19 patients had similar rates of acute respiratory distress syndrome, severe acute kidney injury, and in-hospital mortality. While concentrations of interleukin 6 and 8 were not different between groups, markers of epithelial cell injury (soluble receptor for advanced glycation end products, sRAGE) and acute phase proteins (serum amyloid A, SAA) were significantly higher in COVID-19 compared to non-COVID-19, adjusting for demographics and APACHE III scores. In contrast, angiopoietin 2:1 (Ang-2:1 ratio) and soluble tumor necrosis factor receptor 1 (sTNFR-1), markers of endothelial dysfunction and inflammation, were significantly lower in COVID-19 (p < 0.002). Ang-2:1 ratio and SAA were associated with mortality only in non-COVID-19 patients. Conclusions These studies demonstrate that, unlike other well-studied causes of critical illness, endothelial dysfunction may not be characteristic of severe COVID-19 early after ICU admission. Pathways resulting in elaboration of acute phase proteins and inducing epithelial cell injury may be promising targets for therapeutics in COVID-19.

Download Full-text

Endotoxemia and hepatic injury in a rodent model of hindlimb unloading

Journal of Applied Physiology ◽

10.1152/japplphysiol.00302.2003 ◽

2003 ◽

Vol 95 (4) ◽

pp. 1656-1663 ◽

Cited By ~ 17

Author(s):

C. A. Rivera ◽

M. H. Tcharmtchi ◽

L. Mendoza ◽

C. W. Smith

Keyword(s):

Acute Phase ◽

Hepatic Injury ◽

Acute Phase Proteins ◽

Elevated Serum ◽

Hindlimb Unloading ◽

Low Grade ◽

Systemic Blood ◽

Blood Samples ◽

Amyloid A ◽

Organ Systems

Hindlimb unloading (HU) is known to induce physiological alterations in various organ systems that mimic some responses observed after exposure to microgravity. In the present study, the effects of up to 4 wk of HU on the liver were assessed in male Wistar rats and two mouse strains: endotoxin-sensitive C57BL/6 mice and endotoxin-resistant C3H/HEJ mice. Plasma levels of endotoxin, a known stimulator of hepatic injury, were measured in portal and systemic blood samples. Endotoxin was elevated by ∼50% in portal blood samples of mice and rats but was not detectable in systemic blood. This low-grade portal endotoxemia was associated with hepatic injury in rats and C57BL/6 mice as indicated by inflammation and elevated serum transaminase activities. Blood levels of the cytokine TNF-α were increased by ∼50% in C57BL/6 mice; no significant elevation of this cytokine was detected in rats. Messenger RNA levels of the acute-phase proteins serum amyloid A, haptoglobin, and lipopolysaccharide binding protein were significantly enhanced after 3 wk of HU in endotoxin-sensitive rodents. In contrast, no histological changes or significant increases in serum enzyme activity were detected after HU in C3H/HEJ mice despite portal endotoxin levels of 222 ± 83.4 pg/ml. At the 3-wk time point, expression of acute-phase proteins was not elevated in C3H/HEJ mice; however, expression after 4 wk of HU was similar to endotoxin-sensitive rodents. In conclusion, these findings indicate that HU induced mild portal endotoxemia, which contributed to the observed hepatic injury in endotoxin-sensitive rodents.

Download Full-text

Variations in the levels of acute-phase proteins and lactoferrin in serum and milk during bovine subclinical mastitis

Journal of Dairy Research ◽

10.1017/s002202992100056x ◽

2021 ◽

pp. 1-5

Author(s):

Aarsha Raj ◽

Vinodkumar Kulangara ◽

Tresamol P. Vareed ◽

Deepa P. Melepat ◽

Latha Chattothayil ◽

...

Keyword(s):

Acute Phase ◽

Acute Phase Proteins ◽

Solid Phase ◽

Bovine Mastitis ◽

Subclinical Mastitis ◽

Clinical Mastitis ◽

Reactive Protein ◽

Amyloid A ◽

California Mastitis Test ◽

Bacterial Organism

Abstract Variations in the levels of acute phase proteins and lactoferrin in serum and milk for diagnosis of subclinical mastitis in dairy cows are described in this research paper. Milking animals from two organized dairy farms in Kerala, India, were screened by California Mastitis Test (CMT), Electrical Conductivity test (EC) and Somatic Cell Count (SCC) test to identify animals affected with sub clinical mastitis (SCM). The concentrations of acute phase proteins (APP) Haptoglobin (Hp), C- reactive protein (CRP), Albumin, Lactoferrin (Lf) and α- 1 acid glycoprotein (AGP) in milk and Hp, Albumin, Serum Amyloid A (SAA) and CRP in the serum of 40 normal cows and 40 cows affected with sub clinical mastitis were assessed. Solid phase ELISA was employed for assessment of all parameters except the albumin levels, for which spectrophotometry was used. The values of Hp in milk; and SAA, AGP and Lf in serum, were significantly elevated in the group with sub clinical mastitis. Such variations were found to be independent of the specific bacterial organism causing the disease. These results show that significant variations exist in the levels of acute phase proteins Hp, AGP and Lf in milk, and SAA in serum of animals affected with subclinical bovine mastitis that are not affected by specific bacterial etiology.

Download Full-text

Immunization with Pneumococcal Polysaccharide Serotype 3 and Lipopolysaccharide Modulates Lung and Liver Inflammation during a Virulent Streptococcus pneumoniae Infection in Mice

Clinical and Vaccine Immunology ◽

10.1128/cvi.00593-12 ◽

2013 ◽

Vol 20 (5) ◽

pp. 639-650 ◽

Cited By ~ 3

Author(s):

Katherine H. Restori ◽

Mary J. Kennett ◽

A. Catharine Ross

Keyword(s):

Gene Expression ◽

Streptococcus Pneumoniae ◽

Acute Phase ◽

Acute Phase Proteins ◽

Expression Profiles ◽

Cytokine Gene Expression ◽

Dependent Manner ◽

Pneumonia Severity ◽

Content Type ◽

Amyloid A

ABSTRACTVaccination reduces morbidity and mortality from pneumonia, but its effect on the tissue-level response to infection is still poorly understood. We evaluated pneumonia disease progression, acute-phase response, and lung gene expression profiles in mice inoculated intranasally with virulent Gram-positiveStreptococcus pneumoniaeserotype 3 (ST 3) with and without prior immunization with pneumococcal polysaccharide ST 3 (PPS3) or after coimmunization with PPS3 and a low dose of lipopolysaccharide (PPS3+LPS). Pneumonia severity was assessed in the acute phase at 5, 12, 24 and 48 h postinoculation (p.i.) and in the resolution phase at 7 days p.i. Primary PPS3-specific antibody production was upregulated, and IgM binding to pneumococci increased in PPS3-immunized mice. Immunizations with PPS3 or PPS3+LPS decreased bacterial recovery in the lung and blood at 24 and 48 h and increased survival. Microarray analysis of whole-lung RNA revealed significant changes in the acute-phase protein serum amyloid A (SAA) levels between noninfected and infected mice, and these changes were attenuated by immunization. SAA transcripts were higher in the liver and lungs of infected controls, and SAA protein was elevated in serum but decreased in PPS3-immunized mice. Thus, during a virulent pneumonia infection, prior immunization with PPS3 in an IgM-dependent manner as well as immunization with PPS3+LPS attenuated pneumonia severity and promoted resolution of infection, concomitant with significant regulation of cytokine gene expression levels in the lungs and acute-phase proteins in the lungs, liver, and serum.

Download Full-text

Study on acute phase proteins (haptoglobin, serum amyloid A, fibrinogen, and ceruloplasmin) changes and their diagnostic values in bovine tropical theileriosis

Parasitology Research ◽

10.1007/s00436-009-1360-x ◽

2009 ◽

Vol 105 (1) ◽

pp. 41-46 ◽

Cited By ~ 25

Author(s):

S. Nazifi ◽

S. M. Razavi ◽

Z. Esmailnejad ◽

H. Gheisari

Keyword(s):

Acute Phase ◽

Serum Amyloid A ◽

Acute Phase Proteins ◽

Serum Amyloid ◽

Tropical Theileriosis ◽

Amyloid A ◽

Bovine Tropical Theileriosis ◽

Diagnostic Values

Download Full-text

The acute phase response and C-reactive protein

Oxford Textbook of Medicine ◽

10.1093/med/9780198746690.003.0239 ◽

2020 ◽

pp. 2199-2207

Author(s):

Mark B. Pepys

Keyword(s):

Acute Phase ◽

Acute Phase Response ◽

Serum Amyloid A ◽

Acute Phase Proteins ◽

Phase Response ◽

Serum Amyloid ◽

C Reactive Protein ◽

Reactive Protein ◽

Amyloid A ◽

Serum Amyloid A Protein

The acute phase response—trauma, tissue necrosis, infection, inflammation, and malignant neoplasia induce a complex series of nonspecific systemic, physiological, and metabolic responses including fever, leucocytosis, catabolism of muscle proteins, greatly increased de novo synthesis and secretion of a number of ‘acute phase’ plasma proteins, and decreased synthesis of albumin, transthyretin, and high- and low-density lipoproteins. The altered plasma protein concentration profile is called the acute phase response. Acute phase proteins—these are mostly synthesized by hepatocytes, in which transcription is controlled by cytokines including interleukin 1, interleukin 6, and tumour necrosis factor. The circulating concentrations of complement proteins and clotting factors increase by up to 50 to 100%; some of the proteinase inhibitors and α‎1-acid glycoprotein can increase three- to fivefold; but C-reactive protein (CRP) and serum amyloid A protein (an apolipoprotein of high-density lipoprotein particles) are unique in that their concentrations can change by more than 1000-fold. C-reactive protein—this consists of five identical, nonglycosylated, noncovalently associated polypeptide subunits. It binds to autologous and extrinsic materials which contain phosphocholine, including bacteria and their products. Ligand-bound CRP activates the classical complement pathway and triggers the inflammatory and opsonizing activities of the complement system, thereby contributing to innate host resistance to pneumococci and probably to recognition and safe ‘scavenging’ of cellular debris. Clinical features—(1) determination of CRP in serum or plasma is the most useful marker of the acute phase response in most inflammatory and tissue damaging conditions. (2) Acute phase proteins may be harmful in some circumstances. Sustained increased production of serum amyloid A protein can lead to the deposition of AA-type, reactive systemic amyloid.

Download Full-text

Abstract B87: Acute-phase proteins (C-reactive protein and Serum Amyloid A) and post-diagnosis mammographic density in breast cancer survivors

Cancer Prevention Research ◽

10.1158/1940-6207.prev-12-b87 ◽

2012 ◽

Vol 5 (11 Supplement) ◽

pp. B87-B87

Author(s):

Anne Dee ◽

Roberta McKean-Cowdin ◽

Anne McTiernan ◽

Richard N. Baumgartner ◽

Kathy B. Baumgartner ◽

...

Keyword(s):

Breast Cancer ◽

Cancer Survivors ◽

Mammographic Density ◽

Acute Phase ◽

Breast Cancer Survivors ◽

Serum Amyloid A ◽

Acute Phase Proteins ◽

C Reactive Protein ◽

Reactive Protein ◽

Amyloid A

Download Full-text

Assessment of Acute-Phase Protein Response Associated with the Different Pathological Forms of Bovine Paratuberculosis

Animals ◽

10.3390/ani10101925 ◽

2020 ◽

Vol 10 (10) ◽

pp. 1925

Author(s):

José Espinosa ◽

Rubén de la Morena ◽

Julio Benavides ◽

Carlos García-Pariente ◽

Miguel Fernández ◽

...

Keyword(s):

Acute Phase ◽

Acute Phase Proteins ◽

Bacterial Load ◽

Control Group ◽

Serum Samples ◽

Focal Lesions ◽

Amyloid A ◽

Cell Mediated Immune Response ◽

Protein Response ◽

Antibody Levels

In this study, the concentrations of two acute-phase proteins (APPs), haptoglobin (Hp) and serum amyloid A (SAA), were quantitatively assessed in serum samples from cattle naturally infected with paratuberculosis (PTB). APP profiles were compared across 190 animals classified according to the different pathological forms associated with infection: uninfected (n = 59), with focal lesions (n = 73), multifocal lesions (n = 19), and diffuse paucibacillary (n = 11) and diffuse multibacillary lesions (n = 28). Our results showed a significant increase in both APPs in infected animals compared to the control group, with differences depending on the type of lesion. Hp and SAA levels were increased significantly in all infected animals, except in cows with diffuse multibacillary lesions that showed similar values to non-infected animals. The expression pattern of both APPs was similar and negatively correlated with the antibody levels against PTB. These results indicate that the release of Hp and SAA is related to the presence of PTB lesions associated with a high cell-mediated immune response and a lower bacterial load, suggesting that the pro-inflammatory cytokines that are associated with these forms are the main stimulus for their synthesis. These molecules could show some potential to be used as putative biomarkers of PTB infection, particularly for the identification of subclinical animals showing pathological forms related to latency or resistance to the development of advanced lesions.

Download Full-text

Okadaic acid, an inhibitor of protein phosphatases 1 and 2A, inhibits induction of acute-phase proteins by interleukin-6 alone or in combination with interleukin-1 in human hepatoma cell lines

Biochemical Journal ◽

10.1042/bj2840645 ◽

1992 ◽

Vol 284 (3) ◽

pp. 645-648 ◽

Cited By ~ 11

Author(s):

M K Ganapathi

Keyword(s):

Acute Phase ◽

Okadaic Acid ◽

Interleukin 6 ◽

Acute Phase Proteins ◽

Protein Phosphatases ◽

Hepatoma Cell ◽

Interleukin 1 ◽

Dependent Manner ◽

Amyloid A ◽

20 Nm

Okadaic acid (OA), a specific inhibitor of protein phosphatases 1 and 2A, inhibited in a dose-dependent manner (5-20 nM) the induction of C-reactive protein (CRP), serum amyloid A (SAA) and fibrinogen by interleukin-6 (IL-6) plus interleukin-1 (IL-1), and of fibrinogen by IL-6 alone, in Hep 3B cells. Induction of alpha 1-proteinase inhibitor (alpha 1-PI) by IL-6 plus IL-1 or IL-6 alone was not significantly affected by OA up to concentrations of 20 nM, above which concentration OA was toxic in Hep 3B cells. OA also inhibited the induction of CRP, fibrinogen and alpha 1-PI by IL-6 in the NPLC/PRF/5 cell line, albeit at a higher concentration (80 nM). These results suggest that the signal transduction mechanisms regulating induction of acute-phase proteins by IL-6, either alone or in combination with IL-1, are mediated by activation of protein phosphatases 1 and/or 2A.

Download Full-text