scholarly journals TRH-Like Peptides

2011 ◽  
pp. 207-215 ◽  
Author(s):  
R. BÍLEK ◽  
M. BIČÍKOVÁ ◽  
L. ŠAFAŘÍK
Keyword(s):  
Amino Acid ◽  
Biological Function ◽  
Basic Amino Acid ◽  
Thyroid Status ◽  
Peripheral Tissues ◽  
Amino Acid Histidine ◽  
Neural Tissues ◽  
Proliferative Ability ◽  
Endocrine Tissues

TRH-like peptides are characterized by substitution of basic amino acid histidine (related to authentic TRH) with neutral or acidic amino acid, like glutamic acid, phenylalanine, glutamine, tyrosine, leucin, valin, aspartic acid and asparagine. The presence of extrahypothalamic TRH-like peptides was reported in peripheral tissues including gastrointestinal tract, placenta, neural tissues, male reproductive system and certain endocrine tissues. Work deals with the biological function of TRH-like peptides in different parts of organisms where various mechanisms may serve for realisation of biological function of TRH-like peptides as negative feedback to the pituitary exerted by the TRH-like peptides, the role of pEEPam such as fertilization-promoting peptide, the mechanism influencing the proliferative ability of prostatic tissues, the neuroprotective and antidepressant function of TRH-like peptides in brain and the regulation of thyroid status by TRH-like peptides.

The role of glucose, long-chain triglycerides and amino acids for promotion of amino acid balance across peripheral tissues in man

1999 ◽  
Vol 19 (4) ◽  
pp. 311-320 ◽  
Author(s):  
Elisabeth Svanberg ◽  
Ann-Charlotte Möller-Loswick ◽  
Dwight E Matthews ◽  
Ulla Körner ◽  
Marianne Andersson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Peripheral Tissues ◽  
Amino Acid Balance ◽  
Long Chain Triglycerides ◽  
Long Chain

scholarly journals Role of peptide substrate structure in the selective processing of peptide prohormones at basic amino acid pairs by endoproteases

FEBS Letters ◽  
1988 ◽  
Vol 234 (1) ◽  
pp. 149-152 ◽  
Author(s):  
Pablo Gluschankof ◽  
Sophie Gomez ◽  
Agnès Lepage ◽  
Christophe Créminon ◽  
Fred Nyberg ◽  
...  
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Peptide Substrate ◽  
Substrate Structure ◽  
Selective Processing

Fiber Formation from Solutions of Collagen. IV. On the Role of the Basic Amino Acid Residues*

Biochemistry ◽  
1962 ◽  
Vol 1 (2) ◽  
pp. 215-223 ◽  
Author(s):  
Howard B. Bensusan ◽  
Virgil R. Mumaw ◽  
Ann W. Scanu
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Collagen Iv ◽  
Fiber Formation ◽  
Amino Acid Residues

Degradation of Double-Stranded RNA by Human Pancreatic Ribonuclease:  Crucial Role of Noncatalytic Basic Amino Acid Residues†

Biochemistry ◽  
2003 ◽  
Vol 42 (34) ◽  
pp. 10182-10190 ◽  
Author(s):  
Salvatore Sorrentino ◽  
Mariarosaria Naddeo ◽  
Aniello Russo ◽  
Giuseppe D'Alessio
Keyword(s):  
Amino Acid ◽  
Crucial Role ◽  
Basic Amino Acid ◽  
Amino Acid Residues ◽  
Double Stranded Rna ◽  
Pancreatic Ribonuclease ◽  
Human Pancreatic Ribonuclease

scholarly journals The Role of Basic Amino Acid Surface Clusters on the Collagenase Activity of Cathepsin K

Biochemistry ◽  
2013 ◽  
Vol 52 (44) ◽  
pp. 7742-7752 ◽  
Author(s):  
Ferez S. Nallaseth ◽  
Fabien Lecaille ◽  
Zhenqiang Li ◽  
Dieter Brömme
Keyword(s):  
Amino Acid ◽  
Cathepsin K ◽  
Basic Amino Acid ◽  
Collagenase Activity

Quantitative role of splanchnic region in leucine metabolism: L-[1-13C,15N]leucine and substrate balance studies

1990 ◽  
Vol 259 (1) ◽  
pp. E36-E51 ◽  
Author(s):  
Y. M. Yu ◽  
D. A. Wagner ◽  
E. E. Tredget ◽  
J. A. Walaszewski ◽  
J. F. Burke ◽  
...  
Keyword(s):  
Amino Acid ◽  
Whole Body ◽  
Peripheral Tissues ◽  
Carbon And Nitrogen ◽  
Leucine Metabolism ◽  
Leucine Oxidation ◽  
Body Level ◽  
Total Body ◽  
Level 2

The role of the splanchnic region (Sp) in whole body leucine metabolism was assessed in six chronically catheterized fasting mongrel dogs and in eight dogs during constant enteral feeding of a complete amino acid solution (0.24 g.kg-1.h-1). We used primed continuous intravenous infusions of L-[1-13C,15N]leucine and L-[1-14C]leucine and measurements of arteriovenous isotope and leucine balance across the gut, liver, and Sp. In the fasted condition, 3.5% of arterial leucine supply was oxidized in the Sp, accounting for 13% of total body leucine oxidation, with 10% by liver. With amino acid feeding 1) leucine carbon and nitrogen fluxes and oxidation were increased (P less than 0.01) at the whole body level; 2) the percent of whole body leucine oxidation occurring in the Sp and liver increased (P less than 0.01) to 41 and 27%, respectively; 3) fractional metabolic utilization of leucine delivered to the Sp was reduced (P less than 0.01) from 47 to 35%; 4) the deamination rate of leucine in the gut was increased (P less than 0.05), along with an increased reamination rate of alpha-ketoisocaproic acid in the Sp (P less than 0.05). These findings reveal that the Sp accounts for a small fraction of whole body leucine oxidation during the fasting condition, but it plays a quantitatively important role in total body leucine oxidation during amino acid feeding; the gut and liver play cooperative roles in controlling leucine supply to peripheral tissues.

scholarly journals Structural Model of MD-2 and Functional Role of Its Basic Amino Acid Clusters Involved in Cellular Lipopolysaccharide Recognition

2004 ◽  
Vol 279 (27) ◽  
pp. 28475-28482 ◽  
Author(s):  
Anton Gruber ◽  
Mateja Manček ◽  
Hermann Wagner ◽  
Carsten J. Kirschning ◽  
Roman Jerala
Keyword(s):  
Amino Acid ◽  
Functional Role ◽  
Structural Model ◽  
Basic Amino Acid

Proteases and posttranslational processing of prohormones: a review

1983 ◽  
Vol 61 (7) ◽  
pp. 501-515 ◽  
Author(s):  
Claude Lazure ◽  
Nabil G. Seidah ◽  
Didier Pélaprat ◽  
Michel Chrétien
Keyword(s):  
Amino Acid ◽  
Current Knowledge ◽  
Secretory Granules ◽  
Basic Amino Acid ◽  
Biologically Active ◽  
Maturation Process ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Precursor Molecules

Pioneering work on insulin and on lipotropin, published in 1967, led to the formulation of the hypothesis that biologically active peptides such as peptide hormones are derived from larger precursor molecules by enzymatic cleavage at basic amino acid pairs. Since then, an ever-increasing number of hormones and active peptides including neuropeptides have been found to be contained within the sequence of a larger precursor protein and are released by limited proteolytic cleavage. The hypothesis concerning the posttranslational maturation of precursor molecules into smaller active entities is now firmly established in many tissues (e.g., pituitary gland, pancreas) and for all kinds of organisms (e.g. mammals, fish), though the nature of the enzyme(s) responsible for this maturation process still remains unknown. This article presents current knowledge of the intracellular processing of precursor molecules, especially the conversion of prohormone to hormone. The discussion deals principally with the evidences concerning the localization of the maturation process mainly in the secretory granules, the role of basic amino acid pairs at the cleavage site, and the possible involvement of serine and (or) thiol endopeptidases in that process.

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