scholarly journals THE MECHANISM OF ANAPHYLACTIC SHOCK

1915 ◽  
Vol 22 (4) ◽  
pp. 401-417 ◽  
Author(s):  
James W. Jobling ◽  
William Petersen ◽  
A. A. Eggstein
Keyword(s):  
Amino Acids ◽  
Anaphylactic Shock ◽  
Serum Proteins ◽  
Progressive Increase ◽  
Acute Intoxication ◽  
Foreign Protein ◽  
Serum Lipase ◽  
Maximum Period ◽  
Specific Protease ◽  
Protease B

1. The serum ferments are practically unaltered by a primary injection of foreign protein. 2. During the course of sensitization the injection of the antigen is followed by the mobilization of a non-specific protease which increases in rapidity and intensity as the maximum period of sensitization is reached. 3. Acute shock is accompanied by: (a) The instantaneous mobilization of a large amount of non-specific protease; (b) a decrease in antiferment; (c) an increase in non-coagulable nitrogen of the serum; (d) an increase in amino-acids; (e) a primary decrease in serum proteoses. 4. Later there is a progressive increase in the non-coagulable nitrogen, in proteoses, and in serum lipase. 5. The acute intoxication is brought about by the cleavage of serum proteins (and proteoses) through the peptone stage by a non-specific protease. 6. The specific elements lie in the rapid, mobilization of this ferment and the colloidal serum changes which bring about the change in antiferment titer.

scholarly journals SERUM CHANGES FOLLOWING KAOLIN INJECTIONS

1915 ◽  
Vol 22 (5) ◽  
pp. 590-596 ◽  
Author(s):  
James W. Jobling ◽  
William Petersen ◽  
A. A. Eggstein
Keyword(s):  
Amino Acids ◽  
Intravenous Injection ◽  
Serum Proteins ◽  
Initial Increase ◽  
Serum Lipase

1. The intoxication produced by the intravenous injection of inert substances such as kaolin is due to protein split products derived from the serum proteins. 2. The kaolin acts as an adsorbing medium for the serum antiferment, bringing about an alteration in the ferment-antiferment balance. 3. The intoxication is accompanied by an increase in serum protease, and of proteoses. 4. The serum lipase, the amino-acids, and the total non-coagulable nitrogen show relatively little change. 5. The antiferment shows an initial increase, followed by a loss.

scholarly journals THE BASIC AMINO ACIDS OF SERUM PROTEINS

1934 ◽  
Vol 104 (2) ◽  
pp. 347-350
Author(s):  
Richard J. Block ◽  
Daniel C. Darrow ◽  
M. Katherine Cary
Keyword(s):  
Amino Acids ◽  
Serum Proteins ◽  
Basic Amino Acids

scholarly journals The Carboxy-Terminal Region ofFlavobacterium johnsoniaeSprB Facilitates Its Secretion by the Type IX Secretion System and Propulsion by the Gliding Motility Machinery

2019 ◽  
Vol 201 (19) ◽  
Author(s):  
Surashree S. Kulkarni ◽  
Joseph J. Johnston ◽  
Yongtao Zhu ◽  
Zachary T. Hying ◽  
Mark J. McBride
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cell Surface ◽  
Type A ◽  
Secretion System ◽  
Gliding Motility ◽  
Foreign Protein ◽  
Type B ◽  
Content Type ◽  
Type Ix Secretion System

ABSTRACTFlavobacterium johnsoniaeSprB moves rapidly along the cell surface, resulting in gliding motility. SprB secretion requires the type IX secretion system (T9SS). Proteins secreted by the T9SS typically have conserved C-terminal domains (CTDs) belonging to the type A CTD or type B CTD family. Attachment of 70- to 100-amino-acid type A CTDs to a foreign protein allows its secretion. Type B CTDs are common but have received little attention. Secretion of the foreign protein superfolder green fluorescent protein (sfGFP) fused to regions spanning the SprB type B CTD (sfGFP-CTDSprB) was analyzed. CTDs of 218 amino acids or longer resulted in secretion of sfGFP, whereas a 149-amino-acid region did not. Some sfGFP was secreted in soluble form, whereas the rest was attached on the cell surface. Surface-attached sfGFP was rapidly propelled along the cell, suggesting productive interaction with the motility machinery. This did not result in rapid cell movement, which apparently requires additional regions of SprB. Secretion of sfGFP-CTDSprBrequired coexpression withsprF, which lies downstream ofsprB. SprF is similar in sequence toPorphyromonas gingivalisPorP. MostF. johnsoniaegenes encoding proteins with type B CTDs lie immediately upstream ofporP/sprF-like genes. sfGFP was fused to the type B CTD from one such protein (Fjoh_3952). This resulted in secretion of sfGFP only when it was coexpressed with its cognate PorP/SprF-like protein. These results highlight the need for extended regions of type B CTDs and for coexpression with the appropriate PorP/SprF-like protein for efficient secretion and cell surface localization of cargo proteins.IMPORTANCETheF. johnsoniaegliding motility adhesin SprB is delivered to the cell surface by the type IX secretion system (T9SS) and is rapidly propelled along the cell by the motility machinery. How this 6,497-amino-acid protein interacts with the secretion and motility machines is not known. Fusion of the C-terminal 218 amino acids of SprB to a foreign cargo protein resulted in its secretion, attachment to the cell surface, and rapid movement by the motility machinery. Efficient secretion of SprB required coexpression with the outer membrane protein SprF. Secreted proteins that have sequence similarity to SprB in their C-terminal regions are common in the phylumBacteroidetesand may have roles in adhesion, motility, and virulence.

222 Corn-expressed Phytase Modulates Serum Amino Acids and Proteomics Profiles in Nursery Pigs Fed with Low-protein, -calcium, and -phosphorous Diets

2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 116-116
Author(s):  
Cedrick N N Shili ◽  
Mohammad Habibi ◽  
Parniyan Goodarzi ◽  
Frank Kiyimba ◽  
Steve Hartsen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Growth Performance ◽  
Growth Regulation ◽  
Serum Proteins ◽  
Bone Mineralization ◽  
Negative Control ◽  
Differentially Expressed ◽  
High Dose ◽  
Blood Proteins ◽  
Low Protein

Abstract Feeding pigs with very low-protein (VLP) and low-phosphorous (P) diets may be useful for decreasing the nutrients excretion to the environment; however, this practice negatively impacts the animals’ growth performance. A beneficial effect of corn-expressed phytase (CEP) on growth performance of pigs fed with VLP diets was shown by our group recently. Little is known whether this improvement is related with alterations in profile of blood proteins and amino acids (AA). The objective of this study was to investigate whether supplementation of VLP, low-calcium (Ca) and low-P diets with a CEP can influence the serum AA and proteomics profiles in pigs. Forty-eight weaned barrows were subjected into one of the following groups (n = 8/group) for 4 weeks: positive control (PC), negative control-reduced protein (NC), NC+low-dose CEP, i.e 2,000 FTU/kg (LD), NC+high-dose CEP, i.e. 4,000 FTU/kg (HD), LD with reduced Ca/P (LDR), and HD with reduced Ca/P (HDR). At week 4, blood samples were collected from all pigs. Compared to PC, NC reduced the serum leucine and phenylalanine concentrations; however, LD recovered their levels. Using trypsinolysis and mass spectrometry, 703 serum proteins were identified and quantified, wherein 25 were found to be differentially expressed among groups. Hierarchical clustering showed a clear separation in proteins identified among dietary groups. Compared to NC, 23 and 24 proteins were found to be differentially expressed in serum of LD and HD groups, respectively, with some important proteins in growth regulation such as SELENOP being upregulated and the IGFBP family being downregulated in these groups. A positive correlation was detected between growth and abundance of BGN, TLN1, PDLIM1 and COL1A2 that are involved in bone mineralization and muscle structure development. Thus, CEP improved the serum profile of some essential AA and affected the expression of proteins involved in regulation of growth in pigs fed with VLP diets.

Evolution of Serum Proteins and Amino Acids on Hemodialysis and after Kidney Transplantation

2015 ◽  
pp. 110-115
Author(s):  
J. Pascual ◽  
R. Marc�n ◽  
R. Martin del Rio ◽  
M. E. Rivera ◽  
M. T. Naya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Kidney Transplantation ◽  
Serum Proteins

Influence of organic cations on basic amino-acid uptake by human placental villi

1995 ◽  
Vol 7 (6) ◽  
pp. 1491
Author(s):  
RB Krishna ◽  
J Dancis ◽  
M Levitz
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Basic Amino Acid ◽  
Amino Acid Uptake ◽  
Progressive Increase ◽  
Amino Acid Transporters ◽  
Acid Uptake ◽  
Chorionic Villi ◽  
Basic Amino Acids ◽  
Kinetics Of

Human placental chorionic villi were incubated for 30 min with [3H]lysine or [3H]arginine and the distribution ratios (intracellular:extracellular concentrations) were determined. The ratios remained unchanged when Na+ in Earle's buffered salt solution was replaced with Li+. When Na+ was replaced with choline there was a significant increase is distribution ratios (lysine 1.34 +/- 0.33 v. 3.99 +/- 0.15, arginine 1.95 +/- 0.37 v. 5.05 +/- 1.16). Leucine, a neutral amino acid with a Na(+)-independent transport system, was unaffected by choline substitution. The distribution ratio for alanine, which is Na(+)-dependent, was reduced (2.50 +/- 0.41 v. 1.45 +/- 0.20). Two other quarternary amines, acetyl-beta-methylcholine and tetraethylammonium chloride (TEA) caused similar increases in the distribution ratios of the basic amino acids. Hordenine, a tertiary amine, was less effective and there was little or no effect with ephedrine, a secondary amine. The choline effect was first observable at concentrations of 105 mM. With TEA, there was a progressive increase in distribution ratios beginning at 29 mM. Lysine efflux was measured after incubation of villi with lysine in Earle's buffer or choline buffer. Lysine was rapidly released to the fresh medium with 25% more retained in choline-exposed villi. The amines may cause alterations in the kinetics of basic amino-acid transporters or may modify other aspects of placental physiology permitting an increase retention of the basic amino acids.

scholarly journals Pinocytosis and intracellular degradation of exogenous protein: modulation by amino acids.

1983 ◽  
Vol 96 (6) ◽  
pp. 1586-1591 ◽  
Author(s):  
J M Besterman ◽  
J A Airhart ◽  
R B Low ◽  
D E Rannels
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
De Novo ◽  
Serum Proteins ◽  
Fluid Phase ◽  
Cellular Protein ◽  
Intracellular Degradation ◽  
Exogenous Protein

Intracellular degradation of exogenous (serum) proteins provides a source of amino acids for cellular protein synthesis. Pinocytosis serves as the mechanism for delivering exogenous protein to the lysosomes, the major site of intracellular degradation of exogenous protein. To determine whether the availability of extracellular free amino acids altered pinocytic function, we incubated monolayers of pulmonary alveolar macrophages with the fluid-phase marker, [14C]sucrose, and we dissected the pinocytic process by kinetic analysis. Additionally, intracellular degradation of endogenous and exogenous protein was monitored by measuring phenylalanine released from the cell monolayers in the presence of cycloheximide. Results revealed that in response to a subphysiological level of essential amino acids or to amino acid deprivation, (a) the rate of fluid-phase pinocytosis increased in such a manner as to preferentially increase both delivery to and size of an intracellular compartment believed to be the lysosomes, (b) the degradation of exogenously supplied albumin increased, and (c) the fraction of phenylalanine derived from degradation of exogenous albumin and reutilized for de novo protein synthesis increased. Thus, modulation of the pinosome-lysosome pathway may represent a homeostatic mechanism sensitive to the availability of extracellular free amino acids.

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