Journal articles: 'Acute phase proteins'

1

Migita, Shunsuke. "Acute phase proteins." SEIBUTSU BUTSURI KAGAKU 30, no. 6 (1986): 387–94. http://dx.doi.org/10.2198/sbk.30.387.

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2

WHICHER, J. T., and P. A. DIEPPE. "Acute Phase Proteins." Clinics in Immunology and Allergy 5, no. 3 (October 1985): 425–46. http://dx.doi.org/10.1016/s0260-4639(22)00144-x.

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Gruys, E., M. J. M. Toussaint, T. A. Niewold, and S. J. Koopmans. "Acute phase reaction and acute phase proteins." Journal of Zhejiang University SCIENCE 6B, no. 11 (November 2005): 1045–56. http://dx.doi.org/10.1631/jzus.2005.b1045.

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4

Wakefield, Denis. "Acute Phase Proteins in the Acute Phase Response." Pathology 23, no. 3 (1991): 278. http://dx.doi.org/10.1016/s0031-3025(16)36104-9.

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5

Weston, KS. "Acute Phase Proteins in the Acute Phase Response." Biochemical Education 18, no. 3 (July 1990): 153. http://dx.doi.org/10.1016/0307-4412(90)90234-f.

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6

Sipe, Jean D. "Acute-phase proteins in osteoarthritis." Seminars in Arthritis and Rheumatism 25, no. 2 (October 1995): 75–86. http://dx.doi.org/10.1016/s0049-0172(95)80020-4.

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Ceciliani, F., J. J. Ceron, P. D. Eckersall, and H. Sauerwein. "Acute phase proteins in ruminants." Journal of Proteomics 75, no. 14 (July 2012): 4207–31. http://dx.doi.org/10.1016/j.jprot.2012.04.004.

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DREWS, KRZYSZTOF, JANA SKRZYPCZAK, TOMASZ ŻAK, KRZYSZTOF SZYMANOWSKI, and ANDRZEJ MACKIEWICZ. "Acute Phase Proteins in Endometriosis." Annals of the New York Academy of Sciences 762, no. 1 (December 17, 2006): 508–9. http://dx.doi.org/10.1111/j.1749-6632.1995.tb32384.x.

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9

Correale, Michele, Natale Brunetti, Luisa De Gennaro, and Matteo Biase. "Acute Phase Proteins In Atherosclerosis (Acute Coronary Syndrome)." Cardiovascular & Hematological Agents in Medicinal Chemistry 6, no. 4 (October 1, 2008): 272–77. http://dx.doi.org/10.2174/187152508785909537.

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10

Jensen, L. E., M. P. Hiney, D. C. Shields, C. M. Uhlar, A. J. Lindsay, and A. S. Whitehead. "Acute phase proteins in salmonids: evolutionary analyses and acute phase response." Journal of Immunology 158, no. 1 (January 1, 1997): 384–92. http://dx.doi.org/10.4049/jimmunol.158.1.384.

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Abstract Inflammation induces dramatic changes in the biosynthetic profile of the liver, leading to increased serum concentrations of positive acute phase (AP) proteins and decreased concentrations of negative AP proteins. Serum amyloid A (SAA) and the pentraxins C-reactive protein (CRP) and serum amyloid P component (SAP) are major AP proteins: their serum levels can rise by 1000-fold, indicating that they play a critical role in defense and/or the restoration of homeostasis. We have cloned SAA and a SAP-like pentraxin from salmonid fish species. The salmonid SAA shares approximately 70% amino acid identity with mammalian AP SAA. When salmonids are challenged with an AP stimulus, i.e., Aeromonas salmonicida, SAA responds dramatically as a major AP reactant. The salmonid pentraxin shows approximately 40% amino acid identity to both mammalian SAP and CRP. Evolutionary analysis suggests the presence of only a single such protein in teleosts and lower animal species. Surprisingly, the salmonid pentraxin behaves as a negative AP reactant, reminiscent of the SAP-like Syrian hamster female protein, in that hepatic mRNA concentrations decline to 50% of prestimulus levels. This study reinforces the hypothesis that SAA induction is an essential and universal feature of the vertebrate AP response and that it represents part of an ancient host defense system. Conversely, the species-dependent heterogeneity of pentraxin expression during the vertebrate AP response supports the possibility that its most important ancestral (and perhaps present) function is not related to its AP behavior.

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11

Baker, Robert D., and Stephanie Long. "Acute Phase Proteins in Neonatal Rabbits." Journal of Pediatric Gastroenterology and Nutrition 11, no. 4 (November 1990): 534–41. http://dx.doi.org/10.1002/j.1536-4801.1990.tb10161.x.

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Acute phase protein response accompanies tissue injury, inflammation, or infection. During the acute phase, serum levels of C‐reactive protein (CRP) can increase as much as 1,000‐fold. We found that in response to an intramuscular injection of turpentine, neonatal rabbit CRP‐specific RNA and serum CRP rose minimally. In contrast, adult serum levels of CRP increased 20‐fold and mRNA for CRP in adults increased commensurately. However, during neonatal acute phase reactions, changes in the synthesis of the third component of complement (C3) and albumin were induced, implying a dysynchronous development of the response of various acute phase proteins.

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12

Jain, Sachin, Vidhi Gautam, and Sania Naseem. "Acute-phase proteins: As diagnostic tool." Journal of Pharmacy and Bioallied Sciences 3, no. 1 (2011): 118. http://dx.doi.org/10.4103/0975-7406.76489.

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Baker, Robert D., and Stephanie Long. "Acute Phase Proteins in Neonatal Rabbits." Journal of Pediatric Gastroenterology and Nutrition 11, no. 4 (November 1990): 534–41. http://dx.doi.org/10.1097/00005176-199011000-00015.

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14

BURGER, DANIELLE, and JEAN-MICHEL DAYER. "Cytokines, Acute-Phase Proteins, and Hormones." Annals of the New York Academy of Sciences 966, no. 1 (June 2002): 464–73. http://dx.doi.org/10.1111/j.1749-6632.2002.tb04248.x.

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15

Skinner, J. Gordon. "International Standardization of Acute Phase Proteins." Veterinary Clinical Pathology 30, no. 1 (March 2001): 2–7. http://dx.doi.org/10.1111/j.1939-165x.2001.tb00248.x.

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16

Clark, Geraldine H., and Callum G. Fraser. "Biological Variation of Acute Phase Proteins." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 30, no. 4 (July 1993): 373–76. http://dx.doi.org/10.1177/000456329303000404.

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The analytical, within-subject and between-subject components of variation were estimated for serum albumin, transthyretin, α1-acid glycoprotein, α1-antichymotrypsin, haptoglobin, β2-microglobulin and C-reactive protein in a cohort of 19 apparently healthy subjects over 20 weeks. Desirable analytical goals based on biological variation should be able to be met except for serum albumin and β2-microglobulin for which methodological improvement is warranted. All proteins showed marked individuality which casts doubt on the utility of conventional population-based reference values as interpretative criteria. The critical differences required for significance of changes in serial results differ markedly from protein to protein and the data presented allow generation of objective criteria for monitoring individuals.

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17

Giometto, B., V. Argentiero, F. Sanson, G. Ongaro, and B. Tavolato. "Acute-Phase Proteins in Alzheimer’s Disease." European Neurology 28, no. 1 (1988): 30–33. http://dx.doi.org/10.1159/000116224.

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18

Berk, M., A. A. Wadee, R. H. Kuschke, and A. O'Neill-Kerr. "Acute phase proteins in major depression." Journal of Psychosomatic Research 43, no. 5 (November 1997): 529–34. http://dx.doi.org/10.1016/s0022-3999(97)00139-6.

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19

Gerwick, Lena, and Christopher J. Bayne. "KP2 Acute phase proteins in trout." Developmental & Comparative Immunology 21, no. 2 (March 1997): 173. http://dx.doi.org/10.1016/s0145-305x(97)88663-6.

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20

Hornig-Rohan, M., C. T. Van Bell, P. Kuhn, and J. D. Amsterdam. "Acute phase proteins in affective illness." Biological Psychiatry 37, no. 9 (May 1995): 607. http://dx.doi.org/10.1016/0006-3223(95)94464-8.

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21

Eckersall, P. D., and J. G. Conner. "Bovine and canine acute phase proteins." Veterinary Research Communications 12, no. 2-3 (1988): 169–78. http://dx.doi.org/10.1007/bf00362798.

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22

Heller, Meera C., and Jennifer L. Johns. "Acute phase proteins in healthy goats." Journal of Veterinary Diagnostic Investigation 27, no. 2 (March 2015): 177–81. http://dx.doi.org/10.1177/1040638715575750.

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23

Whicher, J. T. "Interleukin-1 and Acute Phase Proteins." Rheumatology XXIV, suppl 1 (January 1, 1985): 21–24. http://dx.doi.org/10.1093/rheumatology/xxiv.suppl_1.21.

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24

Berk, Michael, Ahmed A. Wadee, and Alex J. O’Neill-Kerr. "Acute phase proteins in major depression." European Neuropsychopharmacology 6 (June 1996): 141. http://dx.doi.org/10.1016/0924-977x(96)87955-7.

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25

Tothova, C., O. Nagy, and G. Kovac. "Acute phase proteins and their use in the diagnosis of diseases in ruminants: a review." Veterinární Medicína 59, No. 4 (June 17, 2014): 163–80. http://dx.doi.org/10.17221/7478-vetmed.

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The acute phase response is a complex systemic early-defence system of reactions activated by trauma, infection, tissue damage, inflammation, stress or neoplasia. One of the most important elements of this response is the increased hepatic synthesis of some plasma proteins, collectively known as acute phase proteins. The discovery of these new biomarkers has allowed the clinical monitoring of different diseases; therefore, their clinical application has been studied widely in human medicine in order to improve the diagnosis, evaluation, treatment, prognosis and therapeutics of many diseases. Although a wide range of studies have been carried out to determine the usefulness of acute phase proteins in several diseases also in animals, they are still relatively under-utilised in veterinary medicine, predominantly in farm animals. The acute phase response and clinical application of acute phase proteins in ruminants are reviewed in this article, including their diagnostic use in clinical practice and application in the monitoring of treatment, which is one of the most promising practical uses of these proteins.  

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26

Tamam, Yusuf, Kenan Iltumur, and Ismail Apak. "Assessment of Acute Phase Proteins in Acute Ischemic Stroke." Tohoku Journal of Experimental Medicine 206, no. 2 (2005): 91–98. http://dx.doi.org/10.1620/tjem.206.91.

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27

Thomsen, Karen Louise, Niels Jessen, Andreas Buch Møller, Niels Kristian Aagaard, Henning Grønbæk, Jens Juul Holst, and Hendrik Vilstrup. "Regulation of urea synthesis during the acute-phase response in rats." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 7 (April 1, 2013): G680—G686. http://dx.doi.org/10.1152/ajpgi.00416.2012.

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The acute-phase response is a catabolic event involving increased waste of amino-nitrogen (N) via hepatic urea synthesis, despite an increased need for amino-N incorporation into acute-phase proteins. This study aimed to clarify the regulation of N elimination via urea during different phases of the tumor necrosis factor-α (TNF-α)-induced acute-phase response in rats. We used four methods to study the regulation of urea synthesis: We examined urea cycle enzyme mRNA levels in liver tissue, the hepatocyte urea cycle enzyme proteins, the in vivo capacity of urea-N synthesis (CUNS), and known humoral regulators of CUNS at 1, 3, 24, and 72 h after TNF-α injection (25 μg/kg iv rrTNF-α) in rats. Serum acute-phase proteins and their liver mRNA levels were also measured. The urea cycle enzyme mRNA levels acutely decreased and then gradually normalized, whereas the urea cycle enzyme proteins remained essentially unchanged over time. The CUNS rose after 3 h and then normalized. The acute-phase response was fully activated at 24 h with markedly increased serum levels of the acute-phase proteins. TNF-α acutely upregulated the CUNS. Later, despite the fully established 24-h acute-phase response and the decreased activity of the urea cycle enzyme genes, there was no change in the urea cycle enzyme proteins or the CUNS. Thus in no phase after the initiation of the acute-phase response was in vivo urea synthesis orchestrated in combination with acute-phase protein synthesis so as to limit N waste.

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28

Damatopoulou, Athanasia, Basil Agroyannis, Constantinos Dardoufas, Androniki Dalamangas, Dimitris Koutsikos, and Labros Vlachos. "Changes Acute Phase Proteins by Radiation Treatment." Acta Oncologica 35, no. 6 (January 1996): 766. http://dx.doi.org/10.3109/02841869609084016.

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29

Mackiewicz, A., M. K. Ganapathi, D. Schultz, and I. Kushner. "Monokines regulate glycosylation of acute-phase proteins." Journal of Experimental Medicine 166, no. 1 (July 1, 1987): 253–58. http://dx.doi.org/10.1084/jem.166.1.253.

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The acute-phase response to inflammatory stimuli, characterized by increased synthesis of acute-phase proteins (APP), is often accompanied by changes in the glycosylation patterns of some of these proteins. While expression of APP genes in hepatocytes is regulated by monokines, mechanisms governing changes in glycosylation are not known. Exposure of human hepatoma cell line Hep 3B to conditioned medium from LPS-activated human monocytes and to medium from the keratocarcinoma cell line COLO-16 led to increased synthesis of alpha 1 proteinase-inhibitor and ceruloplasmin and to alterations of their glycosylation patterns similar to those seen in human serum in various inflammatory states. IL-1, tumor necrosis factor, and hepatocyte stimulating factor I increased synthesis of ceruloplasmin without alterations in the pattern of its glycosylation. These findings demonstrate that altered glycosylation seen in plasma in some inflammatory states can be explained by the effects of monokines on glycosylation in hepatocytes and that gene expression and glycosylation of some APP during the acute-phase response may be regulated by different mechanisms.

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30

Johnson, A. M. "Concentrations of acute-phase proteins in infants." Clinical Chemistry 41, no. 11 (November 1, 1995): 1673. http://dx.doi.org/10.1093/clinchem/41.11.1673.

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31

Chamanza, R., L. van Veen, M. T. Tivapasi, and M. J. M. Toussaint. "Acute phase proteins in the domestic fowl." World's Poultry Science Journal 55, no. 1 (March 1, 1999): 61–71. http://dx.doi.org/10.1079/wps19990005.

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32

YAMADA, YOSHINORI, KATHLEEN KIMBALL, SEIJIRO OKUSAWA, GLORIA VACHINO, NATHAN MARGOLIS, JEONGWON SOHN, JENNY J. LI, et al. "Cytokines, Acute Phase Proteins, and Tissue Injury." Annals of the New York Academy of Sciences 587, no. 1 (June 1990): 351–61. http://dx.doi.org/10.1111/j.1749-6632.1990.tb00176.x.

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33

Shimizu, Sumie. "Acute phase reactant proteins in subarachnoid hemorrhages." Nosotchu 14, no. 3 (1992): 262–71. http://dx.doi.org/10.3995/jstroke.14.262.

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34

Runyon, Bruce A. "Acute phase proteins in patients with cirrhosis." Liver International 32, no. 4 (March 8, 2012): 526–27. http://dx.doi.org/10.1111/j.1478-3231.2011.02746.x.

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35

Maury, C. P. J., A.-M. Teppo, and K. Höckerstedt. "Acute phase proteins and liver allograft rejection." Liver 8, no. 2 (December 10, 2008): 75–79. http://dx.doi.org/10.1111/j.1600-0676.1988.tb00971.x.

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36

Philip, A. G. S., L. Sann, and F. Bienvenu. "Acute Phase Proteins in Neonatal Necrotizing Enterocolitis." Acta Paediatrica 75, no. 6 (November 1986): 1032–33. http://dx.doi.org/10.1111/j.1651-2227.1986.tb10337.x.

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37

Casella, Stefania, Francesco Fazio, Carmelo Russo, Elisabetta Giudice, and Giuseppe Piccione. "Acute phase proteins response in hunting dogs." Journal of Veterinary Diagnostic Investigation 25, no. 5 (July 17, 2013): 577–80. http://dx.doi.org/10.1177/1040638713495851.

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38

Song, Hongmei, Hiromi Tasaki, Akira Yashiro, Kazuhito Yamashita, Hatsumi Taniguchi, and Yasuhide Nakashima. "Acute-Phase Proteins and Chlamydia pneumoniae Infection." Japanese Circulation Journal 65, no. 10 (2001): 853–57. http://dx.doi.org/10.1253/jcj.65.853.

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39

Mantovani, Alberto, and Cecilia Garlanda. "Humoral Innate Immunity and Acute-Phase Proteins." New England Journal of Medicine 388, no. 5 (February 2, 2023): 439–52. http://dx.doi.org/10.1056/nejmra2206346.

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40

Najafi, Laily, Mojtaba Malek, Ameneh Ebrahim Valojerdi, and Mohammad E. Khamseh. "Acute phase proteins and diabetes microvascular complications." International Journal of Diabetes in Developing Countries 36, no. 1 (October 15, 2015): 10–17. http://dx.doi.org/10.1007/s13410-015-0389-x.

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41

Liberatori, Sabrina, Luca Bini, Claudio De Felice, Barbara Magi, Barbara Marzocchi, Roberto Raggiaschi, Vitaliano Pallini, and Rodolfo Bracci. "Acute-phase proteins in perinatal human plasma." Electrophoresis 18, no. 3-4 (1997): 520–26. http://dx.doi.org/10.1002/elps.1150180331.

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42

Slunga, L., O. Johnson, G. H. Dahlén, S. Eriksson, and Lisbeth Slunga. "Lipoprotein(a) and acute-phase proteins in acute myocardial infarction." Scandinavian Journal of Clinical and Laboratory Investigation 52, no. 2 (January 1992): 95–101. http://dx.doi.org/10.3109/00365519209088771.

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43

Erdogan, Okan, and Zeki Öngen. "The importance of acute phase proteins in acute coronary syndromes." American Journal of Cardiology 79, no. 10 (May 1997): 1439–40. http://dx.doi.org/10.1016/s0002-9149(97)89266-1.

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44

Koj, A. "Cytokines regulating acute inflammation and synthesis of acute phase proteins." Blut 51, no. 4 (October 1985): 267–74. http://dx.doi.org/10.1007/bf00320521.

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45

Jawor, P., S. Steiner, T. Stefaniak, W. Baumgartner, and A. Rzasa. "Determination of selected acute phase proteins during the treatment of limb diseases in dairy cows." Veterinární Medicína 53, No. 4 (April 23, 2008): 173–83. http://dx.doi.org/10.17221/1920-vetmed.

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The purpose of this study was to assess the diagnostic value of fibrinogen, haptoglobin, and serum amyloid A determination in the monitoring of the treatment of limb diseases in dairy cows. Fourteen lame cows were examined, while 10 clinically healthy cows constituted the control group. Blood samples from the ill animals were collected on three occasions: (1) upon arrival at the clinic, (2) between the third and sixth day after arriving, and (3) upon return to the owner. Blood samples from the control cows were collected once. Plasma levels of fibrinogen, haptoglobin, serum amyloid A, and total serum protein and its fractions (albumin, α-, β-, γ-globulins) were measured. Significantly higher fibrinogen, haptoglobin, and serum amyloid A levels were observed in the affected cows upon arrival at the clinic than in the control cows. Based on the changes in fibrinogen, haptoglobin, and serum amyloid A concentrations, the cows were divided into those with a systematic decrease in acute-phase protein levels during treatment (Group I, n = 6) and those which showed an increase in one or more acute-phase proteins despite treatment (Group II, n = 8). A stepwise decrease in the examined acute-phase proteins was observed in the first group and indicated an uncomplicated course of treatment; however, treatment of the second group did not appear to be wholly successful. A majority of the cows under treatment (n = 13) exhibited abnormal levels of the examined acute-phase proteins upon return to the owner. This indicates that these patients did not recover completely. The monitoring of plasma acute-phase protein concentrations can be a valuable complement to the clinical assessment of the treatment course and in the early detection of disease complications.

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46

Duff, G. W. "Cytokines and Acute Phase Proteins in Rheumatoid Arthritis." Scandinavian Journal of Rheumatology 23, sup100 (January 1994): 9–19. http://dx.doi.org/10.3109/03009749409095197.

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47

ÇENESİZ, Sena, Hande GÜRLER, Arzu FINDIK, Gülay ÇİFTCİ, Ali ERTEKİN, and Metin ÇENESİZ. "Acute Phase Proteins in Staphylococcus aureus Positive Milks." Etlik Veteriner Mikrobiyoloji Dergisi 29, no. 2 (December 30, 2018): 111–15. http://dx.doi.org/10.35864/evmd.513501.

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48

Abdullah, Mahdi Ali. "Acute phase proteins in veterinary medicine: A review." Journal of Animal Science and Veterinary Medicine 6, no. 6 (December 30, 2021): 188–94. http://dx.doi.org/10.31248/jasvm2020.216.

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The acute phase proteins (APPs) are a group of blood proteins that contribute to restoring homeostasis and limiting microbial growth in an antibody-independent manner in animals which are exposed to different pathological conditions like infection, inflammation, surgical trauma and stress. In the last two decades, many advances have been made in monitoring APPs in both farm and companion animals for clinical and experimental purposes. Also, the mechanism of the APPs response is receiving attention in veterinary science in connection with the innate immune systems of animals. This review describes the many of new results of research and role APPs in farm animal, with special reference to their functions, types, induction and regulatory expression, some of biological functions, and their current and future applications to veterinary diagnosis and animal production.

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49

Munhoz, Thiago Demarchi, Joice Lara Maia Faria, Giovanni Vargas-Hérnandez, José Jurandir Fagliari, Áureo Evangelista Santana, Rosangela Zacarias Machado, and Mirela Tinucci-Costa. "Experimental Ehrlichia canis infection changes acute-phase proteins." Revista Brasileira de Parasitologia Veterinária 21, no. 3 (September 2012): 206–12. http://dx.doi.org/10.1590/s1984-29612012000300006.

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Early diagnosis of canine ehrlichiosis favors prompt institution of treatment and improves the prognosis for the animal, since this disease causes mortality among dogs. Studies have shown that determining the concentration of acute-phase proteins (APPs) may contribute towards early detection of disease and aid in predicting the prognosis. This study aimed to evaluate the APP profile in dogs experimentally infected with Ehrlichia canis, at the start of the infection and after treatment. It also investigated whether any correlation between APP levels and the clinical and laboratory alterations over the course of the disease would be possible. The results obtained showed abnormal levels of all the APPs on the third day after infection (D3), with the highest levels being reached on D18, with the exception of ceruloplasmin and acid glycoprotein, which presented their peaks on D6 and D12 respectively. We concluded that assessment of APP levels could contribute towards establishing an early diagnosis of canine ehrlichiosis, particularly regarding acid glycoprotein and ceruloplasmin, since these proteins were detected at increased levels even before the onset of clinical and laboratory findings of the disease.

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50

Bing, Jens. "RELATION BETWEEN RENIN SUBSTRATE AND ACUTE PHASE PROTEINS." Acta Pathologica Microbiologica Scandinavica Section A Pathology 80A, no. 5 (August 15, 2009): 646–50. http://dx.doi.org/10.1111/j.1699-0463.1972.tb00329.x.

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Journal articles on the topic 'Acute phase proteins'

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